Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Anaphase-promoting complex subunit 4

Gene

Anapc4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-MMU-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-MMU-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-MMU-176412. Phosphorylation of the APC/C.
R-MMU-179409. APC-Cdc20 mediated degradation of Nek2A.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit 4
Short name:
APC4
Alternative name(s):
Cyclosome subunit 4
Gene namesi
Name:Anapc4
Synonyms:D5Ertd249e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1098673. Anapc4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 807807Anaphase-promoting complex subunit 4PRO_0000064596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei469 – 4691PhosphotyrosineBy similarity
Modified residuei757 – 7571PhosphoserineBy similarity
Modified residuei758 – 7581PhosphoserineBy similarity
Modified residuei777 – 7771PhosphoserineCombined sources
Modified residuei779 – 7791PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ91W96.
MaxQBiQ91W96.
PaxDbiQ91W96.
PRIDEiQ91W96.

PTM databases

iPTMnetiQ91W96.
PhosphoSiteiQ91W96.

Expressioni

Gene expression databases

BgeeiQ91W96.
CleanExiMM_ANAPC4.
ExpressionAtlasiQ91W96. baseline and differential.
GenevisibleiQ91W96. MM.

Interactioni

Subunit structurei

The mammalian APC/C is composed of 14 distinct subunits that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031072.

Structurei

3D structure databases

ProteinModelPortaliQ91W96.
SMRiQ91W96. Positions 6-757.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the APC4 family.Curated

Phylogenomic databases

eggNOGiKOG4640. Eukaryota.
ENOG410XPXK. LUCA.
GeneTreeiENSGT00390000004612.
HOGENOMiHOG000033987.
HOVERGENiHBG044815.
InParanoidiQ91W96.
KOiK03351.
OMAiVISHLQX.
OrthoDBiEOG7S21XB.
PhylomeDBiQ91W96.
TreeFamiTF105443.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR024789. APC4.
IPR024790. APC4_long_dom.
IPR017169. APC4_metazoa.
IPR024977. Apc4_WD40_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR13260. PTHR13260. 1 hit.
PfamiPF12896. ANAPC4. 1 hit.
PF12894. ANAPC4_WD40. 1 hit.
[Graphical view]
PIRSFiPIRSF037303. APC4. 1 hit.
SUPFAMiSSF50978. SSF50978. 2 hits.

Sequencei

Sequence statusi: Complete.

Q91W96-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRFPTCFPS FRVVGEKQLP QEIIFLAWSP KRDLIALANT TGEVLLHRLA
60 70 80 90 100
SFHRVWSFPP NESTGKEVTC LAWRPDGKLL AFALADTKKI ILCDVEKPES
110 120 130 140 150
LHSFSVEAPV SCMHWTEVTV ESSVLTSFYN AEDESNLLLP KLPTLPKNYN
160 170 180 190 200
STSKIFSEEN SDEIIKLLGD VRLNILVLGG SSGFIELYAY GMFKIARVTG
210 220 230 240 250
IAGTCIALCL SSDLKSLSVV TEVSSGGESE VSYFQLETNL LYSFLPEVTR
260 270 280 290 300
MARKFTHISA LLQYINLSLT CMCEAWEEIL MQMDSRLTKF VQEKPTTTSV
310 320 330 340 350
QDEFMHLLLW GKASAELQTL LMNQLTVKGL KKLGQSIESS YSSIQKLVIS
360 370 380 390 400
HLQSGSESLL YHLSELKGMA SWKQKYEPLG LDAAGIEDAI TAVGSFILKA
410 420 430 440 450
NELLQVIDSS MKNFKAFFRW LYVAMLRMTE DHVLPELNKM TQKDITFVAE
460 470 480 490 500
FLTEHFNEAP DLYNRKGKYF NVERVGQYLK DEDDDLVSPP NTEGNQWYDF
510 520 530 540 550
LQNSTHLKES PLLFPYYPRK SLHFVKRRME NVIDQCLQKP ADVIGRSMNQ
560 570 580 590 600
AICIPLYKDA RSMDCARRLL KFPFLWNNKT SNLHYLLFTI LEDSVYKMCI
610 620 630 640 650
LRRHTDISQS VSNGLIGIKF GSFTSASADK VRRSSYSCLD AQFYDDETVT
660 670 680 690 700
VILKDSMGRE GRDRILVQLS LSLVYNSEDS DEYEFTGSYS TRLDEQGSII
710 720 730 740 750
PTRTMHFEKH WRLLESMRAQ YVAGNGLRKV SCVLSSNLRH VRVFEMDIDD
760 770 780 790 800
EWEIDESSDD EEEAGGKPVK IKEEVLSESE TEAHQDAAAL DPDVVIKVEK

LDPELDS
Length:807
Mass (Da):91,708
Last modified:December 1, 2001 - v1
Checksum:i1F99C8824BCCC7FC
GO

Sequence cautioni

The sequence BAB27965.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC002259 mRNA. Translation: AAH02259.1.
BC016237 mRNA. Translation: AAH16237.1.
BC024870 mRNA. Translation: AAH24870.1.
AK011994 mRNA. Translation: BAB27965.1. Different initiation.
CCDSiCCDS19290.1.
RefSeqiNP_077175.1. NM_024213.2.
UniGeneiMm.272568.

Genome annotation databases

EnsembliENSMUST00000031072; ENSMUSP00000031072; ENSMUSG00000029176.
GeneIDi52206.
KEGGimmu:52206.
UCSCiuc008xkw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC002259 mRNA. Translation: AAH02259.1.
BC016237 mRNA. Translation: AAH16237.1.
BC024870 mRNA. Translation: AAH24870.1.
AK011994 mRNA. Translation: BAB27965.1. Different initiation.
CCDSiCCDS19290.1.
RefSeqiNP_077175.1. NM_024213.2.
UniGeneiMm.272568.

3D structure databases

ProteinModelPortaliQ91W96.
SMRiQ91W96. Positions 6-757.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031072.

PTM databases

iPTMnetiQ91W96.
PhosphoSiteiQ91W96.

Proteomic databases

EPDiQ91W96.
MaxQBiQ91W96.
PaxDbiQ91W96.
PRIDEiQ91W96.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031072; ENSMUSP00000031072; ENSMUSG00000029176.
GeneIDi52206.
KEGGimmu:52206.
UCSCiuc008xkw.1. mouse.

Organism-specific databases

CTDi29945.
MGIiMGI:1098673. Anapc4.

Phylogenomic databases

eggNOGiKOG4640. Eukaryota.
ENOG410XPXK. LUCA.
GeneTreeiENSGT00390000004612.
HOGENOMiHOG000033987.
HOVERGENiHBG044815.
InParanoidiQ91W96.
KOiK03351.
OMAiVISHLQX.
OrthoDBiEOG7S21XB.
PhylomeDBiQ91W96.
TreeFamiTF105443.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-MMU-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-MMU-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-MMU-176412. Phosphorylation of the APC/C.
R-MMU-179409. APC-Cdc20 mediated degradation of Nek2A.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).

Miscellaneous databases

ChiTaRSiAnapc4. mouse.
PROiQ91W96.
SOURCEiSearch...

Gene expression databases

BgeeiQ91W96.
CleanExiMM_ANAPC4.
ExpressionAtlasiQ91W96. baseline and differential.
GenevisibleiQ91W96. MM.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR024789. APC4.
IPR024790. APC4_long_dom.
IPR017169. APC4_metazoa.
IPR024977. Apc4_WD40_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR13260. PTHR13260. 1 hit.
PfamiPF12896. ANAPC4. 1 hit.
PF12894. ANAPC4_WD40. 1 hit.
[Graphical view]
PIRSFiPIRSF037303. APC4. 1 hit.
SUPFAMiSSF50978. SSF50978. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye and Retina.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 439-807.
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777 AND SER-779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiAPC4_MOUSE
AccessioniPrimary (citable) accession number: Q91W96
Secondary accession number(s): Q99LR5, Q9CZZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.