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Hematopoietic lineage cell-specific protein (Hematopoietic cell-specific LYN substrate 1) (LckBP1) (p75)

 HCLS1_HUMAN             Reviewed;         486 AA.
P14317; B4DQ69; Q53Y93; Q6IBK9; Q9UDK0;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
22-NOV-2017, entry version 189.
RecName: Full=Hematopoietic lineage cell-specific protein;
AltName: Full=Hematopoietic cell-specific LYN substrate 1;
AltName: Full=LckBP1;
AltName: Full=p75;
Name=HCLS1; Synonyms=HS1;
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), AND VARIANTS ALA-235 AND
LEU-436.
PubMed=2587259;
Kitamura D., Kaneko H., Miyagoe Y., Ariyasu T., Watanabe T.;
"Isolation and characterization of a novel human gene expressed
specifically in the cells of hematopoietic lineage.";
Nucleic Acids Res. 17:9367-9379(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-235 AND LEU-436.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS ALA-235 AND LEU-436.
TISSUE=Spleen;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-235 AND LEU-436.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-235 AND LEU-436.
TISSUE=Lymph;
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).
[7]
PROTEIN SEQUENCE OF 4-26; 79-95; 134-146; 208-223 AND 274-289,
INTERACTION WITH LYN, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
TISSUE=B-cell lymphoma;
PubMed=7682714; DOI=10.1073/pnas.90.8.3631;
Yamanashi Y., Okada M., Semba T., Yamori T., Umemori H., Tsunasawa S.,
Toyoshima K., Kitamura D., Watanabe T., Yamamoto T.;
"Identification of HS1 protein as a major substrate of protein-
tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling.";
Proc. Natl. Acad. Sci. U.S.A. 90:3631-3635(1993).
[8]
PROTEIN SEQUENCE OF 97-108; 193-201 AND 240-248.
PubMed=8713105; DOI=10.1006/bbrc.1996.1082;
Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.;
"Identification of the 70kD heat shock cognate protein (Hsc70) and
alpha-actinin-1 as novel phosphotyrosine-containing proteins in T
lymphocytes.";
Biochem. Biophys. Res. Commun. 224:666-674(1996).
[9]
PHOSPHORYLATION AT TYR-222 AND TYR-397, AND PHOSPHORYLATION BY SYK;
LYN; FYN AND FGR.
PubMed=8611520; DOI=10.1021/bi9528614;
Ruzzene M., Brunati A.M., Marin O., Donella-Deana A., Pinna L.A.;
"SH2 domains mediate the sequential phosphorylation of HS1 protein by
p72syk and Src-related protein tyrosine kinases.";
Biochemistry 35:5327-5332(1996).
[10]
INTERACTION WITH HAX1.
PubMed=9058808;
Suzuki Y., Demoliere C., Kitamura D., Takeshita H., Deuschle U.,
Watanabe T.;
"HAX-1, a novel intracellular protein, localized on mitochondria,
directly associates with HS1, a substrate of Src family tyrosine
kinases.";
J. Immunol. 158:2736-2744(1997).
[11]
PHOSPHORYLATION AT TYR-222 AND TYR-397, IDENTIFICATION BY MASS
SPECTROMETRY, AND INTERACTION WITH FGR.
PubMed=10066823; DOI=10.1074/jbc.274.11.7557;
Brunati A.M., Donella-Deana A., James P., Quadroni M., Contri A.,
Marin O., Pinna L.A.;
"Molecular features underlying the sequential phosphorylation of HS1
protein and its association with c-Fgr protein-tyrosine kinase.";
J. Biol. Chem. 274:7557-7564(1999).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-198, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=12522270; DOI=10.1073/pnas.2436191100;
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,
Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
"Profiling of tyrosine phosphorylation pathways in human cells using
mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-198, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND THR-308, 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).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41; LYS-123; LYS-192 AND
LYS-241, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND THR-308, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, 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).
-!- FUNCTION: Substrate of the antigen receptor-coupled tyrosine
kinase. Plays a role in antigen receptor signaling for both clonal
expansion and deletion in lymphoid cells. May also be involved in
the regulation of gene expression.
-!- SUBUNIT: Associates with the SH2 and SH3 domains of LCK. Binding
to he LCK SH3 domain occurs constitutively, while binding to the
LCK SH2 domain occurs only upon TCR stimulation. A similar binding
pattern was observed with LYN, but not with FYN in which the FYN
SH2 region associates upon TCR stimulation but the FYN SH3 region
does not associate regardless of TCR stimulation. Directly
associates with HAX1, through binding to its C-terminal region.
Interacts with HS1BP3. Interacts with FES/FPS (By similarity).
Interacts (via SH2 domain) with FGR. Forms a multiprotein complex
with LYN and ANKRD54 (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q9H788:SH2D4A; NbExp=6; IntAct=EBI-750369, EBI-747035;
P54274:TERF1; NbExp=2; IntAct=EBI-750369, EBI-710997;
O43516:WIPF1; NbExp=2; IntAct=EBI-750369, EBI-346356;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7682714};
Peripheral membrane protein {ECO:0000269|PubMed:7682714}.
Cytoplasm {ECO:0000269|PubMed:7682714}. Mitochondrion
{ECO:0000305|PubMed:7682714}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P14317-1; Sequence=Displayed;
Name=2;
IsoId=P14317-2; Sequence=VSP_056429, VSP_056430;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed only in tissues and cells of
hematopoietic origin.
-!- DEVELOPMENTAL STAGE: Expressed in early stage of myeloid and
erythroid differentiation.
-!- PTM: Phosphorylated by FES (By similarity). Phosphorylated by LYN,
FYN and FGR after cross-linking of surface IgM on B-cells.
Phosphorylation by LYN, FYN and FGR requires prior phosphorylation
by SYK or FES. {ECO:0000250, ECO:0000269|PubMed:10066823,
ECO:0000269|PubMed:7682714, ECO:0000269|PubMed:8611520}.
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EMBL; X16663; CAA34651.1; -; mRNA.
EMBL; BT006824; AAP35470.1; -; mRNA.
EMBL; AK298663; BAG60831.1; -; mRNA.
EMBL; AK312750; BAG35617.1; -; mRNA.
EMBL; CR456794; CAG33075.1; -; mRNA.
EMBL; AC133750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC016758; AAH16758.1; -; mRNA.
CCDS; CCDS3003.1; -. [P14317-1]
PIR; S07633; S07633.
RefSeq; NP_001278970.1; NM_001292041.1.
RefSeq; NP_005326.2; NM_005335.5.
UniGene; Hs.14601; -.
ProteinModelPortal; P14317; -.
SMR; P14317; -.
BioGrid; 109309; 26.
IntAct; P14317; 17.
MINT; MINT-1343660; -.
STRING; 9606.ENSP00000320176; -.
iPTMnet; P14317; -.
PhosphoSitePlus; P14317; -.
BioMuta; HCLS1; -.
DMDM; 317373440; -.
EPD; P14317; -.
MaxQB; P14317; -.
PaxDb; P14317; -.
PeptideAtlas; P14317; -.
PRIDE; P14317; -.
DNASU; 3059; -.
Ensembl; ENST00000314583; ENSP00000320176; ENSG00000180353. [P14317-1]
Ensembl; ENST00000495491; ENSP00000418299; ENSG00000180353. [P14317-2]
GeneID; 3059; -.
KEGG; hsa:3059; -.
UCSC; uc003eeh.5; human. [P14317-1]
CTD; 3059; -.
DisGeNET; 3059; -.
EuPathDB; HostDB:ENSG00000180353.10; -.
GeneCards; HCLS1; -.
HGNC; HGNC:4844; HCLS1.
HPA; HPA019143; -.
MIM; 601306; gene.
neXtProt; NX_P14317; -.
OpenTargets; ENSG00000180353; -.
PharmGKB; PA29220; -.
eggNOG; ENOG410IFV2; Eukaryota.
eggNOG; ENOG410XTAK; LUCA.
GeneTree; ENSGT00530000062953; -.
HOGENOM; HOG000006523; -.
HOVERGEN; HBG005994; -.
InParanoid; P14317; -.
KO; K06106; -.
OMA; YEDVEEM; -.
OrthoDB; EOG091G0CPX; -.
PhylomeDB; P14317; -.
TreeFam; TF318935; -.
SIGNOR; P14317; -.
ChiTaRS; HCLS1; human.
GenomeRNAi; 3059; -.
PMAP-CutDB; P14317; -.
PRO; PR:P14317; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000180353; -.
CleanEx; HS_HCLS1; -.
ExpressionAtlas; P14317; baseline and differential.
Genevisible; P14317; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
GO; GO:0003779; F:actin binding; IEA:InterPro.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:BHF-UCL.
GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:2000107; P:negative regulation of leukocyte apoptotic process; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IC:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0030854; P:positive regulation of granulocyte differentiation; IMP:BHF-UCL.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:BHF-UCL.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
GO; GO:0030833; P:regulation of actin filament polymerization; IMP:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
InterPro; IPR028534; HS1.
InterPro; IPR003134; Hs1_Cortactin.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR10829:SF5; PTHR10829:SF5; 2.
Pfam; PF02218; HS1_rep; 4.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS51090; CORTACTIN; 4.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Membrane; Mitochondrion; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; SH3 domain.
CHAIN 1 486 Hematopoietic lineage cell-specific
protein.
/FTId=PRO_0000083921.
REPEAT 79 115 Cortactin 1.
REPEAT 116 152 Cortactin 2.
REPEAT 153 189 Cortactin 3.
REPEAT 190 212 Cortactin 4; truncated.
DOMAIN 428 486 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 27 66 Involved in HAX-1 binding.
MOD_RES 41 41 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 123 123 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 140 140 Phosphotyrosine.
{ECO:0000250|UniProtKB:P49710}.
MOD_RES 192 192 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 198 198 Phosphotyrosine.
{ECO:0000244|PubMed:12522270,
ECO:0000244|PubMed:15144186}.
MOD_RES 222 222 Phosphotyrosine; by FGR.
{ECO:0000269|PubMed:10066823,
ECO:0000269|PubMed:8611520}.
MOD_RES 241 241 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 308 308 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 378 378 Phosphotyrosine; by SYK and FES.
{ECO:0000250}.
MOD_RES 397 397 Phosphotyrosine; by SYK and FES.
{ECO:0000250}.
VAR_SEQ 134 209 SAVGFDYKGEVEKHTSQKDYSRGFGGRYGVEKDKWDKAALG
YDYKGETEKHESQRDYAKGFGGQYGIQKDRVDKSA -> IT
LVALVAGTGWRRINGTKQLWDMTTRERRRNTSPREIMPRAL
VASMESRRTEWIRALSASMKWRPRPQLIRRRRP (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056429.
VAR_SEQ 210 486 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056430.
VARIANT 235 235 T -> A (in dbSNP:rs2070179).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2587259,
ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
/FTId=VAR_055006.
VARIANT 361 361 E -> K (in dbSNP:rs2070180).
/FTId=VAR_055007.
VARIANT 436 436 V -> L (in dbSNP:rs9869984).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2587259,
ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
/FTId=VAR_056910.
CONFLICT 241 242 KF -> FK (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 486 486 E -> D (in Ref. 4; CAG33075).
{ECO:0000305}.
SEQUENCE 486 AA; 54014 MW; 20AE72A28DA33DFB CRC64;
MWKSVVGHDV SVSVETQGDD WDTDPDFVND ISEKEQRWGA KTIEGSGRTE HINIHQLRNK
VSEEHDVLRK KEMESGPKAS HGYGGRFGVE RDRMDKSAVG HEYVAEVEKH SSQTDAAKGF
GGKYGVERDR ADKSAVGFDY KGEVEKHTSQ KDYSRGFGGR YGVEKDKWDK AALGYDYKGE
TEKHESQRDY AKGFGGQYGI QKDRVDKSAV GFNEMEAPTT AYKKTTPIEA ASSGTRGLKA
KFESMAEEKR KREEEEKAQQ VARRQQERKA VTKRSPEAPQ PVIAMEEPAV PAPLPKKISS
EAWPPVGTPP SSESEPVRTS REHPVPLLPI RQTLPEDNEE PPALPPRTLE GLQVEEEPVY
EAEPEPEPEP EPEPENDYED VEEMDRHEQE DEPEGDYEEV LEPEDSSFSS ALAGSSGCPA
GAGAGAVALG ISAVAVYDYQ GEGSDELSFD PDDVITDIEM VDEGWWRGRC HGHFGLFPAN
YVKLLE


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