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   27-MAR-2024, entry version 149.
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.ENSMUSP00000079627; -.
DR   iPTMnet; Q80YV2; -.
DR   PhosphoSitePlus; Q80YV2; -.
DR   EPD; Q80YV2; -.
DR   jPOST; Q80YV2; -.
DR   MaxQB; Q80YV2; -.
DR   PaxDb; 10090-ENSMUSP00000100057; -.
DR   PeptideAtlas; Q80YV2; -.
DR   ProteomicsDB; 253069; -. [Q80YV2-1]
DR   ProteomicsDB; 253070; -. [Q80YV2-2]
DR   Pumba; Q80YV2; -.
DR   Antibodypedia; 17928; 317 antibodies from 31 providers.
DR   DNASU; 232679; -.
DR   Ensembl; ENSMUST00000080812.14; ENSMUSP00000079627.8; ENSMUSG00000039130.19. [Q80YV2-1]
DR   Ensembl; ENSMUST00000102992.10; ENSMUSP00000100057.4; ENSMUSG00000039130.19. [Q80YV2-2]
DR   GeneID; 232679; -.
DR   KEGG; mmu:232679; -.
DR   UCSC; uc009bfc.1; mouse. [Q80YV2-1]
DR   UCSC; uc009bfd.1; mouse. [Q80YV2-2]
DR   AGR; MGI:1916023; -.
DR   CTD; 51530; -.
DR   MGI; MGI:1916023; Zc3hc1.
DR   VEuPathDB; HostDB:ENSMUSG00000039130; -.
DR   eggNOG; KOG4765; Eukaryota.
DR   GeneTree; ENSGT00390000006086; -.
DR   InParanoid; Q80YV2; -.
DR   OMA; EWCPWIS; -.
DR   OrthoDB; 1041481at2759; -.
DR   PhylomeDB; Q80YV2; -.
DR   TreeFam; TF314674; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 232679; 12 hits in 63 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 259 other cell types or tissues.
DR   ExpressionAtlas; Q80YV2; baseline and differential.
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_C.
DR   InterPro; IPR012935; Znf_C3HC-like.
DR   PANTHER; PTHR15835; NUCLEAR-INTERACTING PARTNER OF ALK; 1.
DR   PANTHER; PTHR15835:SF6; ZINC FINGER C3HC-TYPE PROTEIN 1; 1.
DR   Pfam; PF08600; Rsm1; 1.
DR   Pfam; PF07967; zf-C3HC; 1.
DR   Genevisible; Q80YV2; MM.
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
//