LOCUS NP_037499 808 aa linear PRI 31-AUG-2020
DEFINITION anaphase-promoting complex subunit 4 isoform 2 [Homo sapiens].
ACCESSION NP_037499
VERSION NP_037499.2
DBSOURCE REFSEQ: accession NM_013367.3
KEYWORDS RefSeq; MANE Select.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 808)
AUTHORS Lee CC, Li B, Yu H and Matunis MJ.
TITLE Sumoylation promotes optimal APC/C Activation and Timely Anaphase
JOURNAL Elife 7, e29539 (2018)
PUBMED 29517484
REMARK GeneRIF: We have also identified a functionally important SUMO
interacting motif in the cullin-homology domain of APC2 located
near the APC4 sumoylation sites and APC/C catalytic core. Our
findings provide evidence of an important regulatory role for SUMO
modification and binding in affecting APC/C activation and mitotic
exit.
Publication Status: Online-Only
REFERENCE 2 (residues 1 to 808)
AUTHORS Hein MY, Hubner NC, Poser I, Cox J, Nagaraj N, Toyoda Y, Gak IA,
Weisswange I, Mansfeld J, Buchholz F, Hyman AA and Mann M.
TITLE A human interactome in three quantitative dimensions organized by
stoichiometries and abundances
JOURNAL Cell 163 (3), 712-723 (2015)
PUBMED 26496610
REFERENCE 3 (residues 1 to 808)
AUTHORS Chang L, Zhang Z, Yang J, McLaughlin SH and Barford D.
TITLE Atomic structure of the APC/C and its mechanism of protein
ubiquitination
JOURNAL Nature 522 (7557), 450-454 (2015)
PUBMED 26083744
REFERENCE 4 (residues 1 to 808)
AUTHORS Izawa D and Pines J.
TITLE The mitotic checkpoint complex binds a second CDC20 to inhibit
active APC/C
JOURNAL Nature 517 (7536), 631-634 (2015)
PUBMED 25383541
REFERENCE 5 (residues 1 to 808)
AUTHORS Sedgwick GG, Hayward DG, Di Fiore B, Pardo M, Yu L, Pines J and
Nilsson J.
TITLE Mechanisms controlling the temporal degradation of Nek2A and Kif18A
by the APC/C-Cdc20 complex
JOURNAL EMBO J. 32 (2), 303-314 (2013)
PUBMED 23288039
REFERENCE 6 (residues 1 to 808)
AUTHORS Lukas C, Sorensen CS, Kramer E, Santoni-Rugiu E, Lindeneg C, Peters
JM, Bartek J and Lukas J.
TITLE Accumulation of cyclin B1 requires E2F and cyclin-A-dependent
rearrangement of the anaphase-promoting complex
JOURNAL Nature 401 (6755), 815-818 (1999)
PUBMED 10548110
REFERENCE 7 (residues 1 to 808)
AUTHORS Gieffers C, Peters BH, Kramer ER, Dotti CG and Peters JM.
TITLE Expression of the CDH1-associated form of the anaphase-promoting
complex in postmitotic neurons
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 96 (20), 11317-11322 (1999)
PUBMED 10500174
REFERENCE 8 (residues 1 to 808)
AUTHORS Grossberger R, Gieffers C, Zachariae W, Podtelejnikov AV,
Schleiffer A, Nasmyth K, Mann M and Peters JM.
TITLE Characterization of the DOC1/APC10 subunit of the yeast and the
human anaphase-promoting complex
JOURNAL J. Biol. Chem. 274 (20), 14500-14507 (1999)
PUBMED 10318877
REFERENCE 9 (residues 1 to 808)
AUTHORS Yu H, Peters JM, King RW, Page AM, Hieter P and Kirschner MW.
TITLE Identification of a cullin homology region in a subunit of the
anaphase-promoting complex
JOURNAL Science 279 (5354), 1219-1222 (1998)
PUBMED 9469815
REFERENCE 10 (residues 1 to 808)
AUTHORS Tekolf,W.A., Biddison,W.E., Aster,R.D. and Shaw,S.
TITLE Two subgroups of HLA Bw44 defined by cell-mediated lympholysis that
differ in Bw44 expression on platelets and in patterns of genetic
linkage disequilibrium
JOURNAL J. Immunol. 129 (4), 1474-1478 (1982)
PUBMED 6180011
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from BI546948.1, BC059383.1 and
CA312572.1.
On Jan 26, 2004 this sequence version replaced NP_037499.1.
Summary: A large protein complex, termed the anaphase-promoting
complex (APC), or the cyclosome, promotes metaphase-anaphase
transition by ubiquitinating its specific substrates such as
mitotic cyclins and anaphase inhibitor, which are subsequently
degraded by the 26S proteasome. Biochemical studies have shown that
the vertebrate APC contains eight subunits. The composition of the
APC is highly conserved in organisms from yeast to humans. The
exact function of this gene product is not known. Two transcript
variants encoding different isoforms have been found for this gene.
[provided by RefSeq, Nov 2013].
Transcript Variant: This variant (2) uses an alternate in-frame
splice junction at the 3' end of an exon compared to variant 1. The
resulting isoform (2) has the same N- and C-termini but is 1 aa
shorter compared to isoform 1.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: BC059383.1, SRR1803612.59956.1
[ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMEA1965299, SAMEA1966682
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
MANE Ensembl match :: ENST00000315368.8/ ENSP00000318775.3
RefSeq Select criteria :: based on conservation, expression
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..808
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="4"
/map="4p15.2"
Protein 1..808
/product="anaphase-promoting complex subunit 4 isoform 2"
/note="cyclosome subunit 4"
/calculated_mol_wt=91986
Region 10..57
/region_name="ANAPC4_WD40"
/note="Anaphase-promoting complex subunit 4 WD40 domain;
pfam12894"
/db_xref="CDD:289649"
Region 24..59
/region_name="WD40 repeat"
/note="WD40 repeat [structural motif]"
/db_xref="CDD:293791"
Region <26..115
/region_name="WD40"
/note="WD40 domain, found in a number of eukaryotic
proteins that cover a wide variety of functions including
adaptor/regulatory modules in signal transduction,
pre-mRNA processing and cytoskeleton assembly; typically
contains a GH dipeptide 11-24 residues from...; cl02567"
/db_xref="CDD:295369"
Region 68..102
/region_name="WD40 repeat"
/note="WD40 repeat [structural motif]"
/db_xref="CDD:293791"
Region 232..431
/region_name="ANAPC4"
/note="Anaphase-promoting complex, cyclosome, subunit 4;
pfam12896"
/db_xref="CDD:289651"
Site 469
/site_type="phosphorylation"
/note="Phosphotyrosine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (Q9UJX5.2)"
Site 757
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000244|PubMed:19690332; propagated from
UniProtKB/Swiss-Prot (Q9UJX5.2)"
Site 758
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000244|PubMed:19690332; propagated from
UniProtKB/Swiss-Prot (Q9UJX5.2)"
Site 777
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q9UJX5.2)"
Site 779
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:14657031; propagated from
UniProtKB/Swiss-Prot (Q9UJX5.2)"
CDS 1..808
/gene="ANAPC4"
/gene_synonym="APC4"
/coded_by="NM_013367.3:93..2519"
/note="isoform 2 is encoded by transcript variant 2"
/db_xref="CCDS:CCDS3434.1"
/db_xref="GeneID:29945"
/db_xref="HGNC:HGNC:19990"
/db_xref="MIM:606947"
ORIGIN
1 mlrfptcfps frvvgekqlp qeiiflvwsp krdlialant agevllhrla sfhrvwsfpp
61 nentgkevtc lawrpdgkll afaladtkki vlcdvekpes lhsfsveapv scmhwmevtv
121 essvltsfyn aedesnlllp klptlpknys ntskifseen sdeiikllgd vrlnilvlgg
181 ssgfielyay gmfkiarvtg iagtclalcl ssdlkslsvv tevstngase vsyfqletnl
241 lysflpevtr markfthisa llqyinlslt cmceaweeil mqmdsrltkf vqekntttsv
301 qdefmhlllw gkasaelqtl lmnqltvkgl kklgqsiess yssiqklvis hlqsgsesll
361 yhlselkgma swkqkyeplg ldaagieeai tavgsfilka nellqvidss mknfkaffrw
421 lyvamlrmte dhvlpelnkm tqkditfvae fltehfneap dlynrkgkyf nvervgqylk
481 dedddlvspp ntegnqwydf lqnsshlkes pllfpyyprk slhfvkrrme niidqclqkp
541 advigksmnq aiciplyrdt rsedstrrlf kfpflwnnkt snlhyllfti ledslykmci
601 lrrhtdisqs vsngliaikf gsftyattek vrrsiyscld aqfyddetvt vvlkdtvgre
661 grdrllvqlp lslvynseds aeyqftgtys trldeqcsai ptrtmhfekh wrllesmkaq
721 yvagngfrkv scvlssnlrh vrvfemdidd eweldessde eeeasnkpvk ikeevlsese
781 aenqqagaaa lapeivikve kldpelds
//
