ZC3C1_HUMAN
ID ZC3C1_HUMAN Reviewed; 502 AA.
AC Q86WB0; A6NH66; Q75MF3; Q75MF4; Q8N330; Q96F75; Q9HA34; Q9NVX4; Q9P0R0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Zinc finger C3HC-type protein 1;
DE AltName: Full=Nuclear-interacting partner of ALK;
DE Short=hNIPA;
DE AltName: Full=Nuclear-interacting partner of anaplastic lymphoma kinase;
GN Name=ZC3HC1; Synonyms=NIPA; ORFNames=HSPC216;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH NPM-ALK FUSION
RP PROTEIN, PHOSPHORYLATION AT SER-354, AND MUTAGENESIS OF TYR-105; TYR-137;
RP SER-354; LYS-399 AND 398-ARG--LYS-401.
RX PubMed=12748172; DOI=10.1074/jbc.m300883200;
RA Ouyang T., Bai R.-Y., Bassermann F., von Klitzing C., Klumpen S.,
RA Miething C., Morris S.W., Peschel C., Duyster J.;
RT "Identification and characterization of a nuclear interacting partner of
RT anaplastic lymphoma kinase (NIPA).";
RL J. Biol. Chem. 278:30028-30036(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-271
RP AND HIS-363.
RC TISSUE=Kidney, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, PHOSPHORYLATION, DEVELOPMENTAL STAGE, DOMAIN, INTERACTION WITH
RP SKP1 AND CCNB1, IDENTIFICATION IN SCF(NIPA) COMPLEX WITH SKP1; CUL1 AND
RP RBX1, AND MUTAGENESIS OF 170-LEU-PRO-171 AND SER-354.
RX PubMed=16009132; DOI=10.1016/j.cell.2005.04.034;
RA Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H.,
RA Morris S.W., Peschel C., Duyster J.;
RT "NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic
RT entry.";
RL Cell 122:45-57(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND THR-28, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND THR-28, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333; SER-335; SER-338;
RP SER-344; SER-354; SER-370; THR-384; THR-387 AND SER-395, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-62; SER-335; SER-338;
RP SER-344; SER-354; SER-359; SER-370; THR-387 AND SER-395, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-321; SER-335 AND
RP SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-62; SER-321; SER-329;
RP SER-335; SER-344 AND SER-354, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; THR-28; SER-58; SER-62;
RP THR-84; SER-321; SER-329; SER-335; SER-344; SER-354; SER-381; THR-387;
RP SER-395 AND SER-483, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-344; SER-354 AND
RP SER-407, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Essential component of a SCF-type E3 ligase complex,
CC SCF(NIPA), a complex that controls mitotic entry by mediating
CC ubiquitination and subsequent degradation of cyclin B1 (CCNB1). Its
CC cell-cycle-dependent phosphorylation regulates the assembly of the
CC SCF(NIPA) complex, restricting CCNB1 ubiquitination activity to
CC interphase. Its inactivation results in nuclear accumulation of CCNB1
CC in interphase and premature mitotic entry. May have an antiapoptotic
CC role in NPM-ALK-mediated signaling events.
CC {ECO:0000269|PubMed:16009132}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the NPM-ALK fusion protein in a tyrosine
CC phosphorylation-dependent manner. Interacts with SKP1. Component of a
CC SCF(NIPA) E3 complex with SKP1, RBX1 and CUL1 when not phosphorylated
CC on Ser-354. Interacts with CCNB1. {ECO:0000269|PubMed:12748172,
CC ECO:0000269|PubMed:16009132}.
CC -!- INTERACTION:
CC Q86WB0-2; P54253: ATXN1; NbExp=6; IntAct=EBI-25894765, EBI-930964;
CC Q86WB0-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25894765, EBI-5235340;
CC Q86WB0-2; P09936: UCHL1; NbExp=3; IntAct=EBI-25894765, EBI-714860;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12748172}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86WB0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86WB0-2; Sequence=VSP_015217;
CC Name=3;
CC IsoId=Q86WB0-3; Sequence=VSP_015218;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart,
CC skeletal muscle and testis. Expressed in brain, placenta, lung, kidney,
CC liver, pancreas, spleen, thymus, prostate, ovary small intestine and
CC colon. Weakly or not expressed in leukocytes.
CC {ECO:0000269|PubMed:12748172}.
CC -!- DEVELOPMENTAL STAGE: Weakly expressed in G0/G1 phases, abundant during
CC S and G2/M phases, and strongly decreases thereafter.
CC {ECO:0000269|PubMed:16009132}.
CC -!- DOMAIN: The F-box-like region is required for the interaction with
CC SKP1. {ECO:0000269|PubMed:16009132}.
CC -!- PTM: Phosphorylated. Phosphorylated on Ser residues at G2/M phase, but
CC not during S and G0 phases. May also be weakly phosphorylated on Tyr
CC residues. Ser-354 phosphorylation, a major site during the course of
CC cell-cycle-dependent phosphorylation, results in its dissociation from
CC the SCF(NIPA) complex, thereby preventing CCNB1 degradation leading to
CC mitotic entry. {ECO:0000269|PubMed:12748172,
CC ECO:0000269|PubMed:16009132}.
CC -!- CAUTION: Reported to contain a F-box domain (PubMed:16009132). Such
CC domain is however not predicted by any detection method.
CC {ECO:0000305|PubMed:16009132}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36136.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH28917.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS07546.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAS07547.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ537494; CAD61161.1; -; mRNA.
DR EMBL; AF151050; AAF36136.1; ALT_FRAME; mRNA.
DR EMBL; AK001317; BAA91619.1; -; mRNA.
DR EMBL; AK022373; BAB14024.1; -; mRNA.
DR EMBL; AC073320; AAS07546.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC073320; AAS07547.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC087071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011551; AAH11551.1; -; mRNA.
DR EMBL; BC028917; AAH28917.1; ALT_INIT; mRNA.
DR CCDS; CCDS34753.1; -. [Q86WB0-1]
DR CCDS; CCDS64767.1; -. [Q86WB0-2]
DR CCDS; CCDS75659.1; -. [Q86WB0-3]
DR RefSeq; NP_001269119.1; NM_001282190.1. [Q86WB0-2]
DR RefSeq; NP_001269120.1; NM_001282191.1. [Q86WB0-3]
DR RefSeq; NP_057562.3; NM_016478.4. [Q86WB0-1]
DR AlphaFoldDB; Q86WB0; -.
DR BioGRID; 119592; 123.
DR CORUM; Q86WB0; -.
DR IntAct; Q86WB0; 21.
DR MINT; Q86WB0; -.
DR STRING; 9606.ENSP00000351052; -.
DR iPTMnet; Q86WB0; -.
DR MetOSite; Q86WB0; -.
DR PhosphoSitePlus; Q86WB0; -.
DR SwissPalm; Q86WB0; -.
DR BioMuta; ZC3HC1; -.
DR DMDM; 73921220; -.
DR EPD; Q86WB0; -.
DR jPOST; Q86WB0; -.
DR MassIVE; Q86WB0; -.
DR MaxQB; Q86WB0; -.
DR PaxDb; Q86WB0; -.
DR PeptideAtlas; Q86WB0; -.
DR PRIDE; Q86WB0; -.
DR ProteomicsDB; 70140; -. [Q86WB0-1]
DR ProteomicsDB; 70141; -. [Q86WB0-2]
DR ProteomicsDB; 70142; -. [Q86WB0-3]
DR Antibodypedia; 17928; 267 antibodies from 31 providers.
DR DNASU; 51530; -.
DR Ensembl; ENST00000311873.9; ENSP00000309301.5; ENSG00000091732.17. [Q86WB0-2]
DR Ensembl; ENST00000358303.9; ENSP00000351052.4; ENSG00000091732.17. [Q86WB0-1]
DR Ensembl; ENST00000360708.9; ENSP00000353933.5; ENSG00000091732.17. [Q86WB0-3]
DR GeneID; 51530; -.
DR KEGG; hsa:51530; -.
DR MANE-Select; ENST00000358303.9; ENSP00000351052.4; NM_016478.5; NP_057562.3.
DR UCSC; uc003vpi.4; human. [Q86WB0-1]
DR CTD; 51530; -.
DR DisGeNET; 51530; -.
DR GeneCards; ZC3HC1; -.
DR HGNC; HGNC:29913; ZC3HC1.
DR HPA; ENSG00000091732; Low tissue specificity.
DR MIM; 619746; gene.
DR neXtProt; NX_Q86WB0; -.
DR OpenTargets; ENSG00000091732; -.
DR PharmGKB; PA134931869; -.
DR VEuPathDB; HostDB:ENSG00000091732; -.
DR eggNOG; KOG4765; Eukaryota.
DR GeneTree; ENSGT00390000006086; -.
DR InParanoid; Q86WB0; -.
DR OMA; YSCLKWA; -.
DR OrthoDB; 1626741at2759; -.
DR PhylomeDB; Q86WB0; -.
DR TreeFam; TF314674; -.
DR PathwayCommons; Q86WB0; -.
DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer.
DR SignaLink; Q86WB0; -.
DR SIGNOR; Q86WB0; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 51530; 58 hits in 1090 CRISPR screens.
DR ChiTaRS; ZC3HC1; human.
DR GeneWiki; ZC3HC1; -.
DR GenomeRNAi; 51530; -.
DR Pharos; Q86WB0; Tbio.
DR PRO; PR:Q86WB0; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q86WB0; protein.
DR Bgee; ENSG00000091732; Expressed in tibialis anterior and 171 other tissues.
DR ExpressionAtlas; Q86WB0; baseline and differential.
DR Genevisible; Q86WB0; HS.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR InterPro; IPR013909; NIPA/Rsm1.
DR InterPro; IPR012935; Znf_C3HC-like.
DR Pfam; PF08600; Rsm1; 1.
DR Pfam; PF07967; zf-C3HC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Metal-binding; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..502
FT /note="Zinc finger C3HC-type protein 1"
FT /id="PRO_0000096849"
FT ZN_FING 102..156
FT /note="C3HC-type"
FT REGION 36..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..210
FT /note="F-box-like"
FT REGION 302..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 396..402
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:12748172"
FT COMPBIAS 50..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 28
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:23186163"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12748172,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 384
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 387
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..49
FT /note="MAAPCEGQAFAVGVEKNWGAVVRSPEGTPQKIRQLIDEGIAPEEGGVDA ->
FT MRGLPRKREAWTQPHPLEALYESLRVLE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015217"
FT VAR_SEQ 341..411
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11042152"
FT /id="VSP_015218"
FT VARIANT 271
FT /note="T -> A (in dbSNP:rs1464890)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_023312"
FT VARIANT 363
FT /note="R -> H (in dbSNP:rs11556924)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_023313"
FT MUTAGEN 105
FT /note="Y->F: Does not strongly affect phosphorylation
FT status; when associated with F-137."
FT /evidence="ECO:0000269|PubMed:12748172"
FT MUTAGEN 137
FT /note="Y->F: Does not strongly affect phosphorylation
FT status; when associated with F-105."
FT /evidence="ECO:0000269|PubMed:12748172"
FT MUTAGEN 170..171
FT /note="LP->FM: Abolishes interaction with SKP1."
FT /evidence="ECO:0000269|PubMed:16009132"
FT MUTAGEN 354
FT /note="S->A: Strongly reduces phosphorylation and induces
FT the formation of a constitutive SCF(NIPA) E3 complex that
FT degrades CCNB1 at G2/M phase and delays mitotic entry."
FT /evidence="ECO:0000269|PubMed:12748172,
FT ECO:0000269|PubMed:16009132"
FT MUTAGEN 398..401
FT /note="RKAK->AAAA: Induces a complete cytoplasmic
FT redistribution."
FT /evidence="ECO:0000269|PubMed:12748172"
FT MUTAGEN 399
FT /note="K->P: Induces a partial cytoplasmic redistribution."
FT /evidence="ECO:0000269|PubMed:12748172"
FT CONFLICT 179
FT /note="V -> I (in Ref. 3; BAB14024)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="K -> R (in Ref. 2; AAF36136)"
FT /evidence="ECO:0000305"
SQ 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
