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Nuclear-interacting partner of ALK (Nuclear-interacting partner of anaplastic lymphoma kinase) (hNIPA) (Zinc finger C3HC-type protein 1)

 NIPA_HUMAN              Reviewed;         502 AA.
Q86WB0; A6NH66; Q75MF3; Q75MF4; Q8N330; Q96F75; Q9HA34; Q9NVX4;
Q9P0R0;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
18-JUL-2018, entry version 136.
RecName: Full=Nuclear-interacting partner of ALK;
AltName: Full=Nuclear-interacting partner of anaplastic lymphoma kinase;
Short=hNIPA;
AltName: Full=Zinc finger C3HC-type protein 1;
Name=ZC3HC1; Synonyms=NIPA; ORFNames=HSPC216;
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), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH NPM-ALK
FUSION PROTEIN, PHOSPHORYLATION AT SER-354, AND MUTAGENESIS OF
TYR-105; TYR-137; SER-354; LYS-399 AND 398-ARG--LYS-401.
PubMed=12748172; DOI=10.1074/jbc.M300883200;
Ouyang T., Bai R.-Y., Bassermann F., von Klitzing C., Klumpen S.,
Miething C., Morris S.W., Peschel C., Duyster J.;
"Identification and characterization of a nuclear interacting partner
of anaplastic lymphoma kinase (NIPA).";
J. Biol. Chem. 278:30028-30036(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Mammary gland;
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 GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-271 AND HIS-363.
TISSUE=Kidney, and Mammary gland;
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]
FUNCTION, PHOSPHORYLATION, DEVELOPMENTAL STAGE, DOMAIN, INTERACTION
WITH SKP1 AND CCNB1, IDENTIFICATION IN SCF(NIPA) COMPLEX WITH SKP1;
CUL1 AND RBX1, AND MUTAGENESIS OF 170-LEU-PRO-171 AND SER-354.
PubMed=16009132; DOI=10.1016/j.cell.2005.04.034;
Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H.,
Morris S.W., Peschel C., Duyster J.;
"NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic
entry.";
Cell 122:45-57(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND THR-28, AND
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND THR-28, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333; SER-335; SER-338;
SER-344; SER-354; SER-370; THR-384; THR-387 AND SER-395, 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).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-62; SER-335;
SER-338; SER-344; SER-354; SER-359; SER-370; THR-387 AND SER-395, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-321; SER-335 AND
SER-344, 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).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-62; SER-321;
SER-329; SER-335; SER-344 AND SER-354, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; THR-28; SER-58;
SER-62; THR-84; SER-321; SER-329; SER-335; SER-344; SER-354; SER-381;
THR-387; SER-395 AND SER-483, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-344; SER-354
AND SER-407, 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: Essential component of a SCF-type E3 ligase complex,
SCF(NIPA), a complex that controls mitotic entry by mediating
ubiquitination and subsequent degradation of cyclin B1 (CCNB1).
Its cell-cycle-dependent phosphorylation regulates the assembly of
the SCF(NIPA) complex, restricting CCNB1 ubiquitination activity
to interphase. Its inactivation results in nuclear accumulation of
CCNB1 in interphase and premature mitotic entry. May have an
antiapoptotic role in NPM-ALK-mediated signaling events.
{ECO:0000269|PubMed:16009132}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with the NPM-ALK fusion protein in a tyrosine
phosphorylation-dependent manner. Interacts with SKP1. Component
of a SCF(NIPA) E3 complex with SKP1, RBX1 and CUL1 when not
phosphorylated on Ser-354. Interacts with CCNB1.
{ECO:0000269|PubMed:12748172, ECO:0000269|PubMed:16009132}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12748172}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q86WB0-1; Sequence=Displayed;
Name=2;
IsoId=Q86WB0-2; Sequence=VSP_015217;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q86WB0-3; Sequence=VSP_015218;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart,
skeletal muscle and testis. Expressed in brain, placenta, lung,
kidney, liver, pancreas, spleen, thymus, prostate, ovary small
intestine and colon. Weakly or not expressed in leukocytes.
{ECO:0000269|PubMed:12748172}.
-!- DEVELOPMENTAL STAGE: Weakly expressed in G0/G1 phases, abundant
during S and G2/M phases, and strongly decreases thereafter.
{ECO:0000269|PubMed:16009132}.
-!- DOMAIN: The F-box-like region is required for the interaction with
SKP1. {ECO:0000269|PubMed:16009132}.
-!- PTM: Phosphorylated. Phosphorylated on Ser residues at G2/M phase,
but not during S and G0 phases. May also be weakly phosphorylated
on Tyr residues. Ser-354 phosphorylation, a major site during the
course of cell-cycle-dedendent phosphorylation, results in its
dissociation from the SCF(NIPA) complex, thereby preventing CCNB1
degradation leading to mitotic entry.
{ECO:0000269|PubMed:12748172, ECO:0000269|PubMed:16009132}.
-!- CAUTION: Reported to contain a F-box domain (PubMed:16009132).
Such domain is however not predicted by any detection method.
{ECO:0000305|PubMed:16009132}.
-!- SEQUENCE CAUTION:
Sequence=AAF36136.1; Type=Frameshift; Positions=93, 187, 220; Evidence={ECO:0000305};
Sequence=AAH28917.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAS07546.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAS07547.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AJ537494; CAD61161.1; -; mRNA.
EMBL; AF151050; AAF36136.1; ALT_FRAME; mRNA.
EMBL; AK001317; BAA91619.1; -; mRNA.
EMBL; AK022373; BAB14024.1; -; mRNA.
EMBL; AC073320; AAS07546.1; ALT_SEQ; Genomic_DNA.
EMBL; AC073320; AAS07547.1; ALT_SEQ; Genomic_DNA.
EMBL; AC087071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011551; AAH11551.1; -; mRNA.
EMBL; BC028917; AAH28917.1; ALT_INIT; mRNA.
CCDS; CCDS34753.1; -. [Q86WB0-1]
CCDS; CCDS64767.1; -. [Q86WB0-2]
CCDS; CCDS75659.1; -. [Q86WB0-3]
RefSeq; NP_001269119.1; NM_001282190.1. [Q86WB0-2]
RefSeq; NP_001269120.1; NM_001282191.1. [Q86WB0-3]
RefSeq; NP_057562.3; NM_016478.4. [Q86WB0-1]
UniGene; Hs.194157; -.
ProteinModelPortal; Q86WB0; -.
BioGrid; 119592; 37.
CORUM; Q86WB0; -.
IntAct; Q86WB0; 5.
MINT; Q86WB0; -.
STRING; 9606.ENSP00000351052; -.
iPTMnet; Q86WB0; -.
PhosphoSitePlus; Q86WB0; -.
SwissPalm; Q86WB0; -.
BioMuta; ZC3HC1; -.
DMDM; 73921220; -.
EPD; Q86WB0; -.
MaxQB; Q86WB0; -.
PaxDb; Q86WB0; -.
PeptideAtlas; Q86WB0; -.
PRIDE; Q86WB0; -.
ProteomicsDB; 70140; -.
ProteomicsDB; 70141; -. [Q86WB0-2]
ProteomicsDB; 70142; -. [Q86WB0-3]
DNASU; 51530; -.
Ensembl; ENST00000311873; ENSP00000309301; ENSG00000091732. [Q86WB0-2]
Ensembl; ENST00000358303; ENSP00000351052; ENSG00000091732. [Q86WB0-1]
Ensembl; ENST00000360708; ENSP00000353933; ENSG00000091732. [Q86WB0-3]
GeneID; 51530; -.
KEGG; hsa:51530; -.
UCSC; uc003vpi.4; human. [Q86WB0-1]
CTD; 51530; -.
DisGeNET; 51530; -.
EuPathDB; HostDB:ENSG00000091732.15; -.
GeneCards; ZC3HC1; -.
H-InvDB; HIX0007070; -.
HGNC; HGNC:29913; ZC3HC1.
HPA; HPA019089; -.
HPA; HPA024023; -.
neXtProt; NX_Q86WB0; -.
OpenTargets; ENSG00000091732; -.
PharmGKB; PA134931869; -.
eggNOG; KOG4765; Eukaryota.
eggNOG; ENOG410ZQX4; LUCA.
GeneTree; ENSGT00390000006086; -.
HOVERGEN; HBG082030; -.
InParanoid; Q86WB0; -.
OMA; RYKERCA; -.
OrthoDB; EOG091G0HKR; -.
PhylomeDB; Q86WB0; -.
TreeFam; TF314674; -.
SIGNOR; Q86WB0; -.
UniPathway; UPA00143; -.
ChiTaRS; ZC3HC1; human.
GeneWiki; ZC3HC1; -.
GenomeRNAi; 51530; -.
PRO; PR:Q86WB0; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000091732; -.
CleanEx; HS_ZC3HC1; -.
ExpressionAtlas; Q86WB0; baseline and differential.
Genevisible; Q86WB0; HS.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:LIFEdb.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
InterPro; IPR013909; NIPA/Rsm1.
InterPro; IPR012935; Znf_C3HC-like.
Pfam; PF08600; Rsm1; 1.
Pfam; PF07967; zf-C3HC; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell cycle; Cell division;
Complete proteome; Metal-binding; Mitosis; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation pathway; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CHAIN 2 502 Nuclear-interacting partner of ALK.
/FTId=PRO_0000096849.
ZN_FING 102 156 C3HC-type.
REGION 170 210 F-box-like.
MOTIF 396 402 Nuclear localization signal.
{ECO:0000269|PubMed:12748172}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 28 28 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 84 84 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 333 333 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:12748172}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 381 381 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 384 384 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 387 387 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 49 MAAPCEGQAFAVGVEKNWGAVVRSPEGTPQKIRQLIDEGIA
PEEGGVDA -> MRGLPRKREAWTQPHPLEALYESLRVLE
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_015217.
VAR_SEQ 341 411 Missing (in isoform 3).
{ECO:0000303|PubMed:11042152}.
/FTId=VSP_015218.
VARIANT 271 271 T -> A (in dbSNP:rs1464890).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_023312.
VARIANT 363 363 R -> H (in dbSNP:rs11556924).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_023313.
MUTAGEN 105 105 Y->F: Does not strongly affect
phosphorylation status; when associated
with F-137.
{ECO:0000269|PubMed:12748172}.
MUTAGEN 137 137 Y->F: Does not strongly affect
phosphorylation status; when associated
with F-105.
{ECO:0000269|PubMed:12748172}.
MUTAGEN 170 171 LP->FM: Abolishes interaction with SKP1.
{ECO:0000269|PubMed:16009132}.
MUTAGEN 354 354 S->A: Strongly reduces phosphorylation
and induces the formation of a
constitutive SCF(NIPA) E3 complex that
degrades CCNB1 at G2/M phase and delays
mitotic entry.
{ECO:0000269|PubMed:12748172,
ECO:0000269|PubMed:16009132}.
MUTAGEN 398 401 RKAK->AAAA: Induces a complete
cytoplasmic redistribution.
{ECO:0000269|PubMed:12748172}.
MUTAGEN 399 399 K->P: Induces a partial cytoplasmic
redistribution.
{ECO:0000269|PubMed:12748172}.
CONFLICT 179 179 V -> I (in Ref. 3; BAB14024).
{ECO:0000305}.
CONFLICT 278 278 K -> R (in Ref. 2; AAF36136).
{ECO:0000305}.
SEQUENCE 502 AA; 55262 MW; D5DEDF9E30070586 CRC64;
MAAPCEGQAF AVGVEKNWGA VVRSPEGTPQ KIRQLIDEGI APEEGGVDAK DTSATSQSVN
GSPQAEQPSL ESTSKEAFFS RVETFSSLKW AGKPFELSPL VCAKYGWVTV ECDMLKCSSC
QAFLCASLQP AFDFDRYKQR CAELKKALCT AHEKFCFWPD SPSPDRFGML PLDEPAILVS
EFLDRFQSLC HLDLQLPSLR PEDLKTMCLT EDKISLLLHL LEDELDHRTD ERKTTIKLGS
DIQVHVTACI LSVCGWACSS SLESMQLSLI TCSQCMRKVG LWGFQQIESS MTDLDASFGL
TSSPIPGLEG RPERLPLVPE SPRRMMTRSQ DATFSPGSEQ AEKSPGPIVS RTRSWDSSSP
VDRPEPEAAS PTTRTRPVTR SMGTGDTPGL EVPSSPLRKA KRARLCSSSS SDTSSRSFFD
PTSQHRDWCP WVNITLGKES RENGGTEPDA SAPAEPGWKA VLTILLAHKQ SSQPAETDSM
SLSEKSRKVF RIFRQWESLC SC


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