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Cytoplasmic protein NCK1 (NCK adaptor protein 1) (Nck-1) (SH2/SH3 adaptor protein NCK-alpha)

 NCK1_HUMAN              Reviewed;         377 AA.
P16333; B7Z751; D3DNE3;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
25-OCT-2017, entry version 197.
RecName: Full=Cytoplasmic protein NCK1;
AltName: Full=NCK adaptor protein 1;
Short=Nck-1;
AltName: Full=SH2/SH3 adaptor protein NCK-alpha;
Name=NCK1; Synonyms=NCK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2107526; DOI=10.1093/nar/18.4.1048;
Lehmann J.M., Riethmueller G., Johnson J.P.;
"Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the
src homology units SH2 and SH3.";
Nucleic Acids Res. 18:1048-1048(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION, AND PARTIAL PROTEIN SEQUENCE.
PubMed=1333046; DOI=10.1128/MCB.12.12.5816;
Park D., Rhee S.G.;
"Phosphorylation of Nck in response to a variety of receptors, phorbol
myristate acetate, and cyclic AMP.";
Mol. Cell. Biol. 12:5816-5823(1992).
[7]
PHOSPHORYLATION.
PubMed=1448108; DOI=10.1128/MCB.12.12.5843;
Meisenhelder J., Hunter T.;
"The SH2/SH3 domain-containing protein Nck is recognized by certain
anti-phospholipase C-gamma 1 monoclonal antibodies, and its
phosphorylation on tyrosine is stimulated by platelet-derived growth
factor and epidermal growth factor treatment.";
Mol. Cell. Biol. 12:5843-5856(1992).
[8]
INTERACTION WITH PDGFRB, AND PHOSPHORYLATION.
PubMed=7692233; DOI=10.1128/MCB.13.11.6889;
Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J.,
Schlessinger J.;
"Two signaling molecules share a phosphotyrosine-containing binding
site in the platelet-derived growth factor receptor.";
Mol. Cell. Biol. 13:6889-6896(1993).
[9]
INTERACTION WITH SOCS7.
PubMed=9344857; DOI=10.1006/bbrc.1997.7492;
Matuoka K., Miki H., Takahashi K., Takenawa T.;
"A novel ligand for an SH3 domain of the adaptor protein Nck bears an
SH2 domain and nuclear signaling motifs.";
Biochem. Biophys. Res. Commun. 239:488-492(1997).
[10]
INTERACTION WITH FLT1.
PubMed=9600074; DOI=10.1006/bbrc.1998.8578;
Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.;
"Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2.";
Biochem. Biophys. Res. Commun. 246:95-99(1998).
[11]
INTERACTION WITH BLNK; GRB2; PLCG1 AND VAV.
PubMed=9697839; DOI=10.1016/S1074-7613(00)80591-9;
Fu C., Turck C.W., Kurosaki T., Chan A.C.;
"BLNK: a central linker protein in B cell activation.";
Immunity 9:93-103(1998).
[12]
FUNCTION IN CELL ADHESION, AND INTERACTION WITH EPHB1.
TISSUE=Kidney;
PubMed=9430661; DOI=10.1074/jbc.273.3.1303;
Stein E., Huynh-Do U., Lane A.A., Cerretti D.P., Daniel T.O.;
"Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation
to c-Jun kinase.";
J. Biol. Chem. 273:1303-1308(1998).
[13]
FUNCTION, INTERACTION WITH EGFR; PAK1; PKN2 AND SOS1, AND
PHOSPHORYLATION.
PubMed=10026169; DOI=10.1074/jbc.274.9.5542;
Braverman L.E., Quilliam L.A.;
"Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-
containing adapter protein having similar binding and biological
properties to Nck.";
J. Biol. Chem. 274:5542-5549(1999).
[14]
INTERACTION WITH RALGPS1.
PubMed=10747847; DOI=10.1074/jbc.C000085200;
Rebhun J.F., Chen H., Quilliam L.A.;
"Identification and characterization of a new family of guanine
nucleotide exchange factors for the ras-related GTPase Ral.";
J. Biol. Chem. 275:13406-13410(2000).
[15]
INTERACTION WITH CAV2.
PubMed=12091389; DOI=10.1074/jbc.M204367200;
Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E.,
Lisanti M.P.;
"Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-
caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains
associated with lipid rafts/caveolae, but no longer forms a high
molecular mass hetero-oligomer with caveolin-1.";
J. Biol. Chem. 277:34556-34567(2002).
[16]
INTERACTION WITH CAV2.
PubMed=15504032; DOI=10.1021/bi049295+;
Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W.,
Campos-Gonzalez R., Lisanti M.P.;
"Tyrosine phosphorylation of caveolin-2 at residue 27: differences in
the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27).";
Biochemistry 43:13694-13706(2004).
[17]
INTERACTION WITH MINK1.
PubMed=15469942; DOI=10.1074/jbc.M404497200;
Hu Y., Leo C., Yu S., Huang B.C., Wang H., Shen M., Luo Y.,
Daniel-Issakani S., Payan D.G., Xu X.;
"Identification and functional characterization of a novel human
misshapen/Nck interacting kinase-related kinase, hMINK beta.";
J. Biol. Chem. 279:54387-54397(2004).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[19]
IDENTIFICATION IN COMPLEX WITH PP1 AND PPP1R15B, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=16835242; DOI=10.1074/jbc.M513556200;
Latreille M., Larose L.;
"Nck in a complex containing the catalytic subunit of protein
phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling
and cell survival to endoplasmic reticulum stress.";
J. Biol. Chem. 281:26633-26644(2006).
[20]
INTERACTION WITH KDR.
PubMed=16966330; DOI=10.1074/jbc.M603928200;
Lamalice L., Houle F., Huot J.;
"Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of
Nck and activation of Fyn leading to SAPK2/p38 activation and
endothelial cell migration in response to VEGF.";
J. Biol. Chem. 281:34009-34020(2006).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SOCS7.
PubMed=17803907; DOI=10.1016/j.cell.2007.06.053;
Kremer B.E., Adang L.A., Macara I.G.;
"Septins regulate actin organization and cell-cycle arrest through
nuclear accumulation of NCK mediated by SOCS7.";
Cell 130:837-850(2007).
[22]
FUNCTION, INTERACTION WITH EIF2AK2, AND PHOSPHORYLATION.
PubMed=18835251; DOI=10.1016/j.bbrc.2008.09.112;
Cardin E., Larose L.;
"Nck-1 interacts with PKR and modulates its activation by dsRNA.";
Biochem. Biophys. Res. Commun. 377:231-235(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[24]
INTERACTION WITH ADAM15.
PubMed=18296648; DOI=10.1158/1541-7786.MCR-07-2028;
Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M.,
Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C.,
Edwards D.R.;
"Distinct functions of natural ADAM-15 cytoplasmic domain variants in
human mammary carcinoma.";
Mol. Cancer Res. 6:383-394(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-91 AND SER-96,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND TYR-105, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
INTERACTION WITH RASA1, AND MUTAGENESIS OF TRP-38; TRP-143; TRP-229
AND ARG-308.
PubMed=21664272; DOI=10.1016/j.cellsig.2011.05.019;
Ger M., Zitkus Z., Valius M.;
"Adaptor protein Nck1 interacts with p120 Ras GTPase-activating
protein and regulates its activity.";
Cell. Signal. 23:1651-1658(2011).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-91; SER-96 AND
SER-166, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[34]
FUNCTION IN CELL MIGRATION, AND INTERACTION WITH EPHA2.
PubMed=23358419; DOI=10.1128/MCB.01708-12;
Lee H., Bennett A.M.;
"Receptor protein tyrosine phosphatase-receptor tyrosine kinase
substrate screen identifies EphA2 as a target for LAR in cell
migration.";
Mol. Cell. Biol. 33:1430-1441(2013).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-89 AND SER-166,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[36]
STRUCTURE BY NMR OF 99-174.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH3 domain of the human cytoplasmic protein
NCK1.";
Submitted (NOV-2005) to the PDB data bank.
[37]
STRUCTURE BY NMR OF 1-61 AND 107-165, AND INTERACTION WITH EGFR.
PubMed=18269246; DOI=10.1021/bi701549a;
Hake M.J., Choowongkomon K., Kostenko O., Carlin C.R.,
Sonnichsen F.D.;
"Specificity determinants of a novel Nck interaction with the
juxtamembrane domain of the epidermal growth factor receptor.";
Biochemistry 47:3096-3108(2008).
-!- FUNCTION: Adapter protein which associates with tyrosine-
phosphorylated growth factor receptors, such as KDR and PDGFRB, or
their cellular substrates. Maintains low levels of EIF2S1
phosphorylation by promoting its dephosphorylation by PP1. Plays a
role in the DNA damage response, not in the detection of the
damage by ATM/ATR, but for efficient activation of downstream
effectors, such as that of CHEK2. Plays a role in ELK1-dependent
transcriptional activation in response to activated Ras signaling.
Modulates the activation of EIF2AK2/PKR by dsRNA. May play a role
in cell adhesion and migration through interaction with ephrin
receptors. {ECO:0000269|PubMed:10026169,
ECO:0000269|PubMed:16835242, ECO:0000269|PubMed:17803907,
ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:23358419,
ECO:0000269|PubMed:9430661}.
-!- SUBUNIT: Interacts (via SH2 domain and SH3 domain 2) with EGFR.
Interacts with PAK1 and SOS1. Interacts (via SH3 domains) with
PKN2. Associates with BLNK, PLCG1, VAV1 and NCK1 in a B-cell
antigen receptor-dependent fashion. Interacts with SOCS7. This
interaction is required for nuclear import. Part of a complex
containing PPP1R15B, PP1 and NCK1. Interacts with RALGPS1.
Interacts with CAV2 (tyrosine phosphorylated form). Interacts with
ADAM15. Interacts with FASLG. Directly interacts with RASA1.
Interacts with isoform 4 of MINK1. Interacts with FLT1 (tyrosine
phosphorylated). Interacts with KDR (tyrosine phosphorylated).
Interacts (via SH2 domain) with EPHB1; activates the JUN cascade
to regulate cell adhesion. Interacts with EPHA2. Interacts (via
SH2 domain) with PDGFRB (tyrosine phosphorylated). Interacts with
the inactive form of EIF2AK2/PKR. {ECO:0000269|PubMed:10026169,
ECO:0000269|PubMed:10747847, ECO:0000269|PubMed:12091389,
ECO:0000269|PubMed:15469942, ECO:0000269|PubMed:15504032,
ECO:0000269|PubMed:16835242, ECO:0000269|PubMed:16966330,
ECO:0000269|PubMed:17803907, ECO:0000269|PubMed:18269246,
ECO:0000269|PubMed:18296648, ECO:0000269|PubMed:18835251,
ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:21664272,
ECO:0000269|PubMed:23358419, ECO:0000269|PubMed:7692233,
ECO:0000269|PubMed:9344857, ECO:0000269|PubMed:9430661,
ECO:0000269|PubMed:9600074, ECO:0000269|PubMed:9697839}.
-!- INTERACTION:
Q9H222:ABCG5; NbExp=2; IntAct=EBI-389883, EBI-1761423;
P00519:ABL1; NbExp=2; IntAct=EBI-389883, EBI-375543;
P42684:ABL2; NbExp=4; IntAct=EBI-389883, EBI-1102694;
Q15109:AGER; NbExp=2; IntAct=EBI-389883, EBI-1646426;
O43918:AIRE; NbExp=2; IntAct=EBI-389883, EBI-1753081;
O15085:ARHGEF11; NbExp=3; IntAct=EBI-389883, EBI-311099;
Q9ULH1:ASAP1; NbExp=6; IntAct=EBI-389883, EBI-346622;
Q96NS5:ASB16; NbExp=2; IntAct=EBI-389883, EBI-1751918;
Q9UIF9:BAZ2A; NbExp=2; IntAct=EBI-389883, EBI-934890;
Q9NZM4:BICRA; NbExp=3; IntAct=EBI-389883, EBI-1754943;
O60885:BRD4; NbExp=2; IntAct=EBI-389883, EBI-723869;
Q9ULD4:BRPF3; NbExp=3; IntAct=EBI-389883, EBI-1753470;
P13671:C6; NbExp=2; IntAct=EBI-389883, EBI-1753221;
P20810:CAST; NbExp=2; IntAct=EBI-389883, EBI-1268770;
Q13191:CBLB; NbExp=4; IntAct=EBI-389883, EBI-744027;
P20963:CD247; NbExp=2; IntAct=EBI-389883, EBI-1165705;
P07766:CD3E; NbExp=6; IntAct=EBI-389883, EBI-1211297;
P30260:CDC27; NbExp=3; IntAct=EBI-389883, EBI-994813;
Q9NYQ7:CELSR3; NbExp=2; IntAct=EBI-389883, EBI-308417;
Q13111:CHAF1A; NbExp=2; IntAct=EBI-389883, EBI-1020839;
Q14008:CKAP5; NbExp=3; IntAct=EBI-389883, EBI-310585;
P78357:CNTNAP1; NbExp=2; IntAct=EBI-389883, EBI-1751903;
P78329:CYP4F2; NbExp=2; IntAct=EBI-389883, EBI-1752413;
P98082:DAB2; NbExp=2; IntAct=EBI-389883, EBI-1171238;
Q14118:DAG1; NbExp=2; IntAct=EBI-389883, EBI-1755945;
O14490:DLGAP1; NbExp=4; IntAct=EBI-389883, EBI-1753207;
Q9P1A6:DLGAP2; NbExp=4; IntAct=EBI-389883, EBI-1753397;
O95886:DLGAP3; NbExp=2; IntAct=EBI-389883, EBI-1752541;
Q9Y2H0:DLGAP4; NbExp=5; IntAct=EBI-389883, EBI-722139;
Q92988:DLX4; NbExp=3; IntAct=EBI-389883, EBI-1752755;
Q05193:DNM1; NbExp=2; IntAct=EBI-389883, EBI-713135;
Q8IZD9:DOCK3; NbExp=3; IntAct=EBI-389883, EBI-1752361;
Q9H1R2:DUSP15; NbExp=2; IntAct=EBI-389883, EBI-1752795;
Q9H8V3:ECT2; NbExp=3; IntAct=EBI-389883, EBI-1054039;
P00533:EGFR; NbExp=3; IntAct=EBI-389883, EBI-297353;
P41970:ELK3; NbExp=3; IntAct=EBI-389883, EBI-1758534;
P42566:EPS15; NbExp=2; IntAct=EBI-389883, EBI-396684;
O00254:F2RL2; NbExp=2; IntAct=EBI-389883, EBI-1751853;
Q9BQ89:FAM110A; NbExp=2; IntAct=EBI-389883, EBI-1752811;
P48023:FASLG; NbExp=4; IntAct=EBI-15578122, EBI-495538;
P31994:FCGR2B; NbExp=2; IntAct=EBI-389883, EBI-724784;
P31995:FCGR2C; NbExp=2; IntAct=EBI-389883, EBI-1396036;
O75369:FLNB; NbExp=3; IntAct=EBI-389883, EBI-352089;
O75593:FOXH1; NbExp=2; IntAct=EBI-389883, EBI-1759806;
O15117:FYB; NbExp=3; IntAct=EBI-389883, EBI-1753267;
Q13480:GAB1; NbExp=3; IntAct=EBI-389883, EBI-517684;
Q9UBS5:GABBR1; NbExp=3; IntAct=EBI-389883, EBI-724156;
Q99259:GAD1; NbExp=2; IntAct=EBI-389883, EBI-743184;
P10912:GHR; NbExp=3; IntAct=EBI-389883, EBI-286316;
P15586:GNS; NbExp=2; IntAct=EBI-389883, EBI-1752200;
O43708:GSTZ1; NbExp=2; IntAct=EBI-389883, EBI-748043;
P10412:HIST1H1E; NbExp=2; IntAct=EBI-389883, EBI-358163;
O43390:HNRNPR; NbExp=2; IntAct=EBI-389883, EBI-713419;
P47928:ID4; NbExp=3; IntAct=EBI-389883, EBI-1754719;
Q9H9L3:ISG20L2; NbExp=2; IntAct=EBI-389883, EBI-751335;
O60674:JAK2; NbExp=2; IntAct=EBI-389883, EBI-518647;
P35968:KDR; NbExp=3; IntAct=EBI-389883, EBI-1005487;
P10721:KIT; NbExp=3; IntAct=EBI-389883, EBI-1379503;
Q9UMN6:KMT2B; NbExp=2; IntAct=EBI-389883, EBI-765774;
Q13094:LCP2; NbExp=14; IntAct=EBI-389883, EBI-346946;
Q9BY71:LRRC3; NbExp=2; IntAct=EBI-389883, EBI-1761329;
P27816:MAP4; NbExp=2; IntAct=EBI-389883, EBI-715255;
Q92918:MAP4K1; NbExp=4; IntAct=EBI-389883, EBI-881;
Q9Y4K4:MAP4K5; NbExp=2; IntAct=EBI-389883, EBI-1279;
Q9NQ76:MEPE; NbExp=3; IntAct=EBI-389883, EBI-1753293;
P08581:MET; NbExp=2; IntAct=EBI-389883, EBI-1039152;
Q15746:MYLK; NbExp=2; IntAct=EBI-389883, EBI-968482;
Q8WX92:NELFB; NbExp=6; IntAct=EBI-389883, EBI-347721;
P43699:NKX2-1; NbExp=2; IntAct=EBI-389883, EBI-1391923;
O60500:NPHS1; NbExp=3; IntAct=EBI-389883, EBI-996920;
Q13177:PAK2; NbExp=2; IntAct=EBI-389883, EBI-1045887;
Q13087:PDIA2; NbExp=3; IntAct=EBI-389883, EBI-1752525;
O75167:PHACTR2; NbExp=2; IntAct=EBI-389883, EBI-1754409;
O00750:PIK3C2B; NbExp=3; IntAct=EBI-389883, EBI-641107;
Q9UL42:PNMA2; NbExp=2; IntAct=EBI-389883, EBI-302355;
Q9BXM0:PRX; NbExp=2; IntAct=EBI-389883, EBI-1753064;
P29074:PTPN4; NbExp=3; IntAct=EBI-389883, EBI-710431;
P15918:RAG1; NbExp=2; IntAct=EBI-389883, EBI-1755109;
Q13905:RAPGEF1; NbExp=2; IntAct=EBI-389883, EBI-976876;
P20936:RASA1; NbExp=6; IntAct=EBI-389883, EBI-1026476;
Q9UQ26:RIMS2; NbExp=2; IntAct=EBI-389883, EBI-1756749;
Q8TB24:RIN3; NbExp=2; IntAct=EBI-389883, EBI-1570523;
O60942:RNGTT; NbExp=2; IntAct=EBI-15578122, EBI-1237132;
O55236:Rngtt (xeno); NbExp=3; IntAct=EBI-15578122, EBI-16118241;
P26373:RPL13; NbExp=2; IntAct=EBI-389883, EBI-356849;
P78345:RPP38; NbExp=2; IntAct=EBI-389883, EBI-366493;
P10301:RRAS; NbExp=3; IntAct=EBI-389883, EBI-968703;
Q96GP6:SCARF2; NbExp=2; IntAct=EBI-389883, EBI-1752088;
Q9NZV5:SELENON; NbExp=2; IntAct=EBI-389883, EBI-1751965;
O75326:SEMA7A; NbExp=2; IntAct=EBI-389883, EBI-1753538;
Q9UPX8:SHANK2; NbExp=6; IntAct=EBI-389883, EBI-1570571;
Q9BYB0:SHANK3; NbExp=4; IntAct=EBI-389883, EBI-1752330;
Q13796:SHROOM2; NbExp=2; IntAct=EBI-389883, EBI-1644065;
Q9UHI7:SLC23A1; NbExp=2; IntAct=EBI-389883, EBI-1759386;
O60721:SLC24A1; NbExp=3; IntAct=EBI-389883, EBI-1753504;
Q9UMY4:SNX12; NbExp=3; IntAct=EBI-389883, EBI-1752602;
Q15036:SNX17; NbExp=3; IntAct=EBI-389883, EBI-1752620;
Q9Y5X2:SNX8; NbExp=2; IntAct=EBI-389883, EBI-1752557;
Q07889:SOS1; NbExp=5; IntAct=EBI-389883, EBI-297487;
Q07890:SOS2; NbExp=3; IntAct=EBI-389883, EBI-298181;
P08047:SP1; NbExp=2; IntAct=EBI-389883, EBI-298336;
Q96T58:SPEN; NbExp=3; IntAct=EBI-389883, EBI-765739;
Q9H5I1:SUV39H2; NbExp=2; IntAct=EBI-389883, EBI-723127;
O15056:SYNJ2; NbExp=3; IntAct=EBI-389883, EBI-310513;
O43493:TGOLN2; NbExp=3; IntAct=EBI-389883, EBI-1752146;
P42167:TMPO; NbExp=2; IntAct=EBI-389883, EBI-455283;
O54967:Tnk2 (xeno); NbExp=2; IntAct=EBI-15578122, EBI-7780354;
Q15661:TPSAB1; NbExp=2; IntAct=EBI-389883, EBI-1761369;
Q9ULW0:TPX2; NbExp=4; IntAct=EBI-389883, EBI-1037322;
Q9BWF2:TRAIP; NbExp=3; IntAct=EBI-389883, EBI-1756205;
Q9HCM9:TRIM39; NbExp=2; IntAct=EBI-389883, EBI-739510;
O00294:TULP1; NbExp=2; IntAct=EBI-389883, EBI-1756778;
Q96RL7:VPS13A; NbExp=3; IntAct=EBI-389883, EBI-1752583;
O00401:WASL; NbExp=2; IntAct=EBI-389883, EBI-957615;
O43516:WIPF1; NbExp=2; IntAct=EBI-389883, EBI-346356;
-!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Nucleus.
Note=Mostly cytoplasmic, but shuttles between the cytoplasm and
the nucleus. Import into the nucleus requires the interaction with
SOCS7. Predominantly nuclear following genotoxic stresses, such as
UV irradiation, hydroxyurea or mitomycin C treatments.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P16333-1; Sequence=Displayed;
Name=2;
IsoId=P16333-2; Sequence=VSP_043122;
Note=No experimental confirmation available.;
-!- DOMAIN: Only the first and third SH3 domains seem to be involved
in RASA1-binding; the second SH3 domain and the SH2 domains do not
seeem to be involved.
-!- PTM: Phosphorylated on Ser and Tyr residues. Phosphorylated in
response to activation of EGFR and FcERI. Phosphorylated by
activated PDGFRB. {ECO:0000269|PubMed:10026169,
ECO:0000269|PubMed:1333046, ECO:0000269|PubMed:1448108,
ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:7692233}.
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EMBL; X17576; CAA35599.1; -; mRNA.
EMBL; AK301460; BAH13487.1; -; mRNA.
EMBL; AC011597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79105.1; -; Genomic_DNA.
EMBL; CH471052; EAW79108.1; -; Genomic_DNA.
EMBL; CH471052; EAW79109.1; -; Genomic_DNA.
EMBL; BC006403; AAH06403.1; -; mRNA.
CCDS; CCDS3092.1; -. [P16333-1]
CCDS; CCDS54644.1; -. [P16333-2]
PIR; S08636; S08636.
RefSeq; NP_001177725.1; NM_001190796.2. [P16333-2]
RefSeq; NP_001278928.1; NM_001291999.1. [P16333-1]
RefSeq; NP_006144.1; NM_006153.5. [P16333-1]
UniGene; Hs.126889; -.
UniGene; Hs.477693; -.
PDB; 2CI8; X-ray; 1.80 A; A=281-377.
PDB; 2CI9; X-ray; 1.50 A; A/B=281-377.
PDB; 2CUB; NMR; -; A=99-173.
PDB; 2JS0; NMR; -; A=107-165.
PDB; 2JS2; NMR; -; A=1-61.
PDB; 2JW4; NMR; -; A=1-63.
PDBsum; 2CI8; -.
PDBsum; 2CI9; -.
PDBsum; 2CUB; -.
PDBsum; 2JS0; -.
PDBsum; 2JS2; -.
PDBsum; 2JW4; -.
ProteinModelPortal; P16333; -.
SMR; P16333; -.
BioGrid; 110770; 121.
DIP; DIP-639N; -.
ELM; P16333; -.
IntAct; P16333; 216.
MINT; MINT-92747; -.
STRING; 9606.ENSP00000288986; -.
BindingDB; P16333; -.
ChEMBL; CHEMBL4846; -.
iPTMnet; P16333; -.
PhosphoSitePlus; P16333; -.
BioMuta; NCK1; -.
DMDM; 127962; -.
EPD; P16333; -.
MaxQB; P16333; -.
PaxDb; P16333; -.
PeptideAtlas; P16333; -.
PRIDE; P16333; -.
DNASU; 4690; -.
Ensembl; ENST00000288986; ENSP00000288986; ENSG00000158092. [P16333-1]
Ensembl; ENST00000469404; ENSP00000419631; ENSG00000158092. [P16333-2]
Ensembl; ENST00000481752; ENSP00000417273; ENSG00000158092. [P16333-1]
GeneID; 4690; -.
KEGG; hsa:4690; -.
UCSC; uc003erh.3; human. [P16333-1]
CTD; 4690; -.
DisGeNET; 4690; -.
EuPathDB; HostDB:ENSG00000158092.6; -.
GeneCards; NCK1; -.
HGNC; HGNC:7664; NCK1.
HPA; CAB005063; -.
HPA; HPA030766; -.
MIM; 600508; gene.
neXtProt; NX_P16333; -.
OpenTargets; ENSG00000158092; -.
PharmGKB; PA31466; -.
eggNOG; KOG4226; Eukaryota.
eggNOG; ENOG410XRPF; LUCA.
GeneTree; ENSGT00820000126999; -.
HOGENOM; HOG000290684; -.
HOVERGEN; HBG000719; -.
InParanoid; P16333; -.
KO; K07365; -.
OMA; KNYVTIM; -.
OrthoDB; EOG091G0AD0; -.
PhylomeDB; P16333; -.
TreeFam; TF351631; -.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-373753; Nephrin family interactions.
Reactome; R-HSA-418885; DCC mediated attractive signaling.
Reactome; R-HSA-428540; Activation of Rac.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; P16333; -.
SIGNOR; P16333; -.
ChiTaRS; NCK1; human.
EvolutionaryTrace; P16333; -.
GeneWiki; NCK1; -.
GenomeRNAi; 4690; -.
PMAP-CutDB; P16333; -.
PRO; PR:P16333; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000158092; -.
CleanEx; HS_NCK1; -.
ExpressionAtlas; P16333; baseline and differential.
Genevisible; P16333; HS.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005840; C:ribosome; IDA:ParkinsonsUK-UCL.
GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0008093; F:cytoskeletal adaptor activity; NAS:UniProtKB.
GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl.
GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; IPI:ParkinsonsUK-UCL.
GO; GO:0030674; F:protein binding, bridging; IC:ParkinsonsUK-UCL.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0004860; F:protein kinase inhibitor activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0005070; F:SH3/SH2 adaptor activity; NAS:ParkinsonsUK-UCL.
GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:Ensembl.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
GO; GO:0060548; P:negative regulation of cell death; IDA:UniProtKB.
GO; GO:1903912; P:negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:1903898; P:negative regulation of PERK-mediated unfolded protein response; IDA:ParkinsonsUK-UCL.
GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
GO; GO:0070262; P:peptidyl-serine dephosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
GO; GO:1903676; P:positive regulation of cap-dependent translational initiation; IDA:ParkinsonsUK-UCL.
GO; GO:1903679; P:positive regulation of cap-independent translational initiation; IDA:ParkinsonsUK-UCL.
GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0036493; P:positive regulation of translation in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
GO; GO:0051707; P:response to other organism; IEA:Ensembl.
GO; GO:0007172; P:signal complex assembly; NAS:UniProtKB.
GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IEA:Ensembl.
GO; GO:0042110; P:T cell activation; IMP:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd10408; SH2_Nck1; 1.
CDD; cd11900; SH3_Nck1_1; 1.
CDD; cd11901; SH3_Nck1_2; 1.
CDD; cd11904; SH3_Nck1_3; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR017304; NCK.
InterPro; IPR035882; Nck1_SH2.
InterPro; IPR035562; Nck1_SH3_1.
InterPro; IPR035564; Nck1_SH3_2.
InterPro; IPR035565; Nck1_SH3_3.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 2.
Pfam; PF14604; SH3_9; 1.
PIRSF; PIRSF037874; Cytoplasmic_NCK; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 3.
SUPFAM; SSF50044; SSF50044; 3.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH2 domain;
SH3 domain; Translation regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 377 Cytoplasmic protein NCK1.
/FTId=PRO_0000096766.
DOMAIN 2 61 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 115 165 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 190 252 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 282 376 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 105 105 Phosphotyrosine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 76 MAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRV
RNSMNKTGFVPSNYVERKNSARKASIVKNLKDTLG -> MD
WLNVFKDFFS (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043122.
VARIANT 180 180 A -> V (in dbSNP:rs13320485).
/FTId=VAR_051228.
MUTAGEN 38 38 W->K: Small decrease in RASA1-binding.
Almost complete loss of RASA1-binding;
when associated with K-143 and K-229.
{ECO:0000269|PubMed:21664272}.
MUTAGEN 143 143 W->K: No effect on RASA1-binding. Almost
complete loss of RASA1-binding; when
associated with K-38 and K-229.
{ECO:0000269|PubMed:21664272}.
MUTAGEN 229 229 W->K: Small decrease in RASA1-binding.
Almost complete loss of RASA1-binding;
when associated with K-38 and K-229.
{ECO:0000269|PubMed:21664272}.
MUTAGEN 308 308 R->K: No effect on RASA1-binding.
{ECO:0000269|PubMed:21664272}.
STRAND 5 11 {ECO:0000244|PDB:2JS2}.
STRAND 28 33 {ECO:0000244|PDB:2JS2}.
STRAND 35 42 {ECO:0000244|PDB:2JS2}.
STRAND 48 51 {ECO:0000244|PDB:2JS2}.
TURN 53 55 {ECO:0000244|PDB:2JS2}.
STRAND 56 58 {ECO:0000244|PDB:2JS2}.
STRAND 99 101 {ECO:0000244|PDB:2CUB}.
STRAND 109 115 {ECO:0000244|PDB:2CUB}.
STRAND 131 138 {ECO:0000244|PDB:2CUB}.
STRAND 142 148 {ECO:0000244|PDB:2CUB}.
STRAND 151 156 {ECO:0000244|PDB:2CUB}.
HELIX 157 159 {ECO:0000244|PDB:2CUB}.
STRAND 160 162 {ECO:0000244|PDB:2CUB}.
STRAND 168 170 {ECO:0000244|PDB:2CUB}.
HELIX 289 299 {ECO:0000244|PDB:2CI9}.
STRAND 304 309 {ECO:0000244|PDB:2CI9}.
STRAND 311 313 {ECO:0000244|PDB:2CI9}.
STRAND 316 321 {ECO:0000244|PDB:2CI9}.
STRAND 324 326 {ECO:0000244|PDB:2CI9}.
STRAND 328 335 {ECO:0000244|PDB:2CI9}.
STRAND 338 341 {ECO:0000244|PDB:2CI9}.
STRAND 344 348 {ECO:0000244|PDB:2CI9}.
HELIX 349 358 {ECO:0000244|PDB:2CI9}.
STRAND 361 363 {ECO:0000244|PDB:2CI9}.
SEQUENCE 377 AA; 42864 MW; 554E9B1A936AEF30 CRC64;
MAEEVVVVAK FDYVAQQEQE LDIKKNERLW LLDDSKSWWR VRNSMNKTGF VPSNYVERKN
SARKASIVKN LKDTLGIGKV KRKPSVPDSA SPADDSFVDP GERLYDLNMP AYVKFNYMAE
REDELSLIKG TKVIVMEKCS DGWWRGSYNG QVGWFPSNYV TEEGDSPLGD HVGSLSEKLA
AVVNNLNTGQ VLHVVQALYP FSSSNDEELN FEKGDVMDVI EKPENDPEWW KCRKINGMVG
LVPKNYVTVM QNNPLTSGLE PSPPQCDYIR PSLTGKFAGN PWYYGKVTRH QAEMALNERG
HEGDFLIRDS ESSPNDFSVS LKAQGKNKHF KVQLKETVYC IGQRKFSTME ELVEHYKKAP
IFTSEQGEKL YLVKHLS


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