ZC3C1_PONAB
ID ZC3C1_PONAB Reviewed; 502 AA.
AC Q5R8V9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Zinc finger C3HC-type protein 1;
DE AltName: Full=Nuclear-interacting partner of ALK;
DE AltName: Full=Nuclear-interacting partner of anaplastic lymphoma kinase;
GN Name=ZC3HC1; Synonyms=NIPA;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 {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-354. Interacts with
CC CCNB1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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-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 (By similarity). {ECO:0000250}.
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DR EMBL; CR859639; CAH91801.1; -; mRNA.
DR RefSeq; NP_001127464.1; NM_001133992.1.
DR AlphaFoldDB; Q5R8V9; -.
DR STRING; 9601.ENSPPYP00000020193; -.
DR GeneID; 100174537; -.
DR KEGG; pon:100174537; -.
DR CTD; 51530; -.
DR eggNOG; KOG4765; Eukaryota.
DR InParanoid; Q5R8V9; -.
DR OrthoDB; 1626741at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Metal-binding; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT CHAIN 2..502
FT /note="Zinc finger C3HC-type protein 1"
FT /id="PRO_0000096851"
FT ZN_FING 102..156
FT /note="C3HC-type"
FT REGION 35..74
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:0000250"
FT COMPBIAS 49..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..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: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:0000250|UniProtKB:Q86WB0"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 384
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WB0"
SQ SEQUENCE 502 AA; 55255 MW; 96F6D916C6507D53 CRC64;
MAAPCEGQAF AVGVEKNWGA VVRSPEGTPQ KIRQLIDEGI APEEGGVDAQ DTSATSQSVN
GSPQAEQPSL ESTSKEAFFS RVETFSSLKW AGKPPELSPL VCAKYGWVTV ECDMLKCSSC
QAFLCASLQP AFDFDRYKQR CAELKKALCT AHEKFCFWPD SPSPDRFGML PLEEPAILVS
EFLDRFQSLC HLDLQLPSLR PEDLKTMCLT EDKISLLLHL LEDELDHRTD ERKTTTKLGS
DIQVHVTACI LSVCGWACSS SLEPMQLSLI TCSQCMRKVG LWGFQQIESS MTDLDASFGL
TSSPIPGLEG RPERLPLVPE SPRRMMTRSQ DATFFPGSEQ AEKSPGPIVS RTRSWDSSSP
VDRPEPEAAS PTTRTRPVTR SMGTGDPSGL EVPSSPLRKA KRARLCSSSS SDTSSRSFFD
PTSQHRDWCP WVNVTLGKES RENGGTEPDA SAPAEPGWKA VLTILLAHKQ SSQPAETDSM
SLSEKSRKVF RIFRQWESLC SC
