ZC3C1_MOUSE
ID ZC3C1_MOUSE Reviewed; 501 AA.
AC Q80YV2; Q3TJE6; Q80Z11; Q8BTW5; Q8CI56; Q8R3U7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Zinc finger C3HC-type protein 1;
DE AltName: Full=Nuclear-interacting partner of ALK;
DE Short=mNIPA;
DE AltName: Full=Nuclear-interacting partner of anaplastic lymphoma kinase;
GN Name=Zc3hc1; Synonyms=Nipa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND POSSIBLE FUNCTION.
RC STRAIN=Swiss Webster;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Placenta, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, FVB/N, and FVB/N-3; TISSUE=Embryo, and Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-68; SER-334; SER-337;
RP SER-343; SER-353; SER-358; SER-369 AND SER-406, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC Overexpression may be able to protect from apoptosis induced by IL-3
CC withdrawal. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with SKP1. Component of a SCF(NIPA) E3 complex with
CC SKP1, RBX1 and CUL1 when not phosphorylated on Ser-353. Interacts with
CC CCNB1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80YV2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80YV2-2; Sequence=VSP_015219;
CC -!- DOMAIN: The F-box-like region is required for the interaction with
CC SKP1. {ECO:0000250}.
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-353 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 (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37445.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ537495; CAD61162.1; -; mRNA.
DR EMBL; AK088527; BAC40404.1; -; mRNA.
DR EMBL; AK151694; BAE30618.1; -; mRNA.
DR EMBL; AK167465; BAE39549.1; -; mRNA.
DR EMBL; BC024560; AAH24560.1; -; mRNA.
DR EMBL; BC037445; AAH37445.1; ALT_INIT; mRNA.
DR EMBL; BC050141; AAH50141.1; -; mRNA.
DR CCDS; CCDS19970.1; -. [Q80YV2-2]
DR CCDS; CCDS80508.1; -. [Q80YV2-1]
DR RefSeq; NP_001298015.1; NM_001311086.1. [Q80YV2-1]
DR RefSeq; NP_766323.1; NM_172735.2. [Q80YV2-2]
DR RefSeq; XP_017177060.1; XM_017321571.1. [Q80YV2-2]
DR AlphaFoldDB; Q80YV2; -.
DR IntAct; Q80YV2; 2.
DR MINT; Q80YV2; -.
DR STRING; 10090.ENSMUSP00000100057; -.
DR iPTMnet; Q80YV2; -.
DR PhosphoSitePlus; Q80YV2; -.
DR EPD; Q80YV2; -.
DR jPOST; Q80YV2; -.
DR MaxQB; Q80YV2; -.
DR PaxDb; Q80YV2; -.
DR PeptideAtlas; Q80YV2; -.
DR PRIDE; Q80YV2; -.
DR ProteomicsDB; 253069; -. [Q80YV2-1]
DR ProteomicsDB; 253070; -. [Q80YV2-2]
DR Antibodypedia; 17928; 267 antibodies from 31 providers.
DR DNASU; 232679; -.
DR Ensembl; ENSMUST00000080812; ENSMUSP00000079627; ENSMUSG00000039130. [Q80YV2-1]
DR Ensembl; ENSMUST00000102992; ENSMUSP00000100057; ENSMUSG00000039130. [Q80YV2-2]
DR GeneID; 232679; -.
DR KEGG; mmu:232679; -.
DR UCSC; uc009bfc.1; mouse. [Q80YV2-1]
DR UCSC; uc009bfd.1; mouse. [Q80YV2-2]
DR CTD; 51530; -.
DR MGI; MGI:1916023; Zc3hc1.
DR VEuPathDB; HostDB:ENSMUSG00000039130; -.
DR eggNOG; KOG4765; Eukaryota.
DR GeneTree; ENSGT00390000006086; -.
DR InParanoid; Q80YV2; -.
DR OMA; YSCLKWA; -.
DR OrthoDB; 1626741at2759; -.
DR PhylomeDB; Q80YV2; -.
DR TreeFam; TF314674; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 232679; 12 hits in 60 CRISPR screens.
DR ChiTaRS; Zc3hc1; mouse.
DR PRO; PR:Q80YV2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80YV2; protein.
DR Bgee; ENSMUSG00000039130; Expressed in otic placode and 255 other tissues.
DR ExpressionAtlas; Q80YV2; baseline and differential.
DR Genevisible; Q80YV2; MM.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
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; IDA:MGI.
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:0000250|UniProtKB:Q86WB0"
FT CHAIN 2..501
FT /note="Zinc finger C3HC-type protein 1"
FT /id="PRO_0000096850"
FT ZN_FING 102..156
FT /note="C3HC-type"
FT REGION 21..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..210
FT /note="F-box-like"
FT REGION 302..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 395..401
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 30..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 28
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 332
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 383
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT VAR_SEQ 480..501
FT /note="SLSEKSRKVFRIFRQWESSSSS -> LK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015219"
FT CONFLICT 65
FT /note="A -> S (in Ref. 1; CAD61162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 55196 MW; 1FB522C93F8A8178 CRC64;
MAATSEGPLF AASIEKTWGS VVRSPEGTPQ KVRELIDEGI VPEEGGTEPK DTAATFQSVD
GSPQAEQSPL ESTSKEAFFH RVETFSSLKW AGKPPELSPL ICAKYGWVTV ECDMLKCSSC
QAFLCASLQP TFDFGRYKER CAELKKSLCS AHEKFCFWPD SPSPDRFGML PLGEPAVLIS
EFLDRFQSLC HLDLQLPSLR PEDLKTMCLT EDAVSALLHL LEDELDFHAD DRKTTSKLGS
DVQVQATACV LSLCGWACSS LEPTQLSLIT CYQCMRKVGL WGFQQIESSM TDLEASFGLT
SSPIPGVEGR PEHFPLVPES PRRMMTRSQD ATVSPGSEQS EKSPGPIVSR TRSWESSSPV
DRPELEAASP TTRSRPVTRS MGTGDSAGVE VPSSPLRRTK RARLCSSSSS DTSPRSFFDP
TSQHRDWCPW VNITLVKETK ENGETEVDAC TPAEPGWKAV LTILLAHKRS NQPAETDSMS
LSEKSRKVFR IFRQWESSSS S
