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Q9UJX5

- APC4_HUMAN

UniProt

Q9UJX5 - APC4_HUMAN

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Protein
Anaphase-promoting complex subunit 4
Gene
ANAPC4, APC4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.1 Publication

Pathwayi

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein phosphatase binding Source: BHF-UCL
  3. ubiquitin-protein transferase activity Source: ProtInc

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: ProtInc
  2. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  3. mitotic anaphase Source: ProtInc
  4. mitotic cell cycle Source: Reactome
  5. mitotic nuclear division Source: ProtInc
  6. mitotic spindle assembly checkpoint Source: Reactome
  7. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  8. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  9. protein K11-linked ubiquitination Source: UniProtKB
  10. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  11. ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
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:APC4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:19990. ANAPC4.

Subcellular locationi

GO - Cellular componenti

  1. anaphase-promoting complex Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134894250.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 808808Anaphase-promoting complex subunit 4
PRO_0000064595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei469 – 4691Phosphotyrosine1 Publication
Modified residuei757 – 7571Phosphoserine1 Publication
Modified residuei758 – 7581Phosphoserine1 Publication
Modified residuei777 – 7771Phosphoserine1 Publication
Modified residuei779 – 7791Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UJX5.
PaxDbiQ9UJX5.
PRIDEiQ9UJX5.

PTM databases

PhosphoSiteiQ9UJX5.

Expressioni

Gene expression databases

ArrayExpressiQ9UJX5.
BgeeiQ9UJX5.
CleanExiHS_ANAPC4.
GenevestigatoriQ9UJX5.

Organism-specific databases

HPAiCAB032519.
HPA038395.
HPA038396.

Interactioni

Subunit structurei

The APC/C is composed of at least 12 subunits.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KIF18AQ8NI772EBI-2554854,EBI-355426
NEK2P519556EBI-2554854,EBI-633182

Protein-protein interaction databases

BioGridi118982. 49 interactions.
DIPiDIP-56450N.
IntActiQ9UJX5. 26 interactions.
MINTiMINT-4787108.
STRINGi9606.ENSP00000318775.

Structurei

3D structure databases

ProteinModelPortaliQ9UJX5.
SMRiQ9UJX5. Positions 175-215, 721-749.

Family & Domainsi

Sequence similaritiesi

Belongs to the APC4 family.

Phylogenomic databases

eggNOGiNOG248176.
HOGENOMiHOG000033987.
HOVERGENiHBG044815.
InParanoidiQ9UJX5.
KOiK03351.
OrthoDBiEOG7S21XB.
PhylomeDBiQ9UJX5.
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. Apc4. 1 hit.
PF12894. Apc4_WD40. 1 hit.
[Graphical view]
PIRSFiPIRSF037303. APC4. 1 hit.
SUPFAMiSSF50978. SSF50978. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UJX5-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA    50
SFHRVWSFPP NENTGKEVTC LAWRPDGKLL AFALADTKKI VLCDVEKPES 100
LHSFSVEAPV SCMHWMEVTV ESSVLTSFYN AEDESNLLLP KLPTLPKNYS 150
NTSKIFSEEN SDEIIKLLGD VRLNILVLGG SSGFIELYAY GMFKIARVTG 200
IAGTCLALCL SSDLKSLSVV TEVSTNGASE VSYFQLETNL LYSFLPEVTR 250
MARKFTHISA LLQYINLSLT CMCEAWEEIL MQMDSRLTKF VQEKNTTTSV 300
QDEFMHLLLW GKASAELQTL LMNQLTVKGL KKLGQSIESS YSSIQKLVIS 350
HLQSGSESLL YHLSELKGMA SWKQKYEPLG LDAAGIEEAI TAVGSFILKA 400
NELLQVIDSS MKNFKAFFRW LYVAMLRMTE DHVLPELNKM TQKDITFVAE 450
FLTEHFNEAP DLYNRKGKYF NVERVGQYLK DEDDDLVSPP NTEGNQWYDF 500
LQNSSHLKES PLLFPYYPRK SLHFVKRRME NIIDQCLQKP ADVIGKSMNQ 550
AICIPLYRDT RSEDSTRRLF KFPFLWNNKT SNLHYLLFTI LEDSLYKMCI 600
LRRHTDISQS VSNGLIAIKF GSFTYATTEK VRRSIYSCLD AQFYDDETVT 650
VVLKDTVGRE GRDRLLVQLP LSLVYNSEDS AEYQFTGTYS TRLDEQCSAI 700
PTRTMHFEKH WRLLESMKAQ YVAGNGFRKV SCVLSSNLRH VRVFEMDIDD 750
EWELDESSDE EEEASNKPVK IKEEVLSESE AENQQAGAAA LAPEIVIKVE 800
KLDPELDS 808
Length:808
Mass (Da):92,116
Last modified:September 2, 2008 - v2
Checksum:i80362CC8D8B2063F
GO
Isoform 2 (identifier: Q9UJX5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     542-551: DVIGKSMNQA → VSLKEMHVFV
     552-808: Missing.

Note: No experimental confirmation available.

Show »
Length:551
Mass (Da):62,639
Checksum:i16829B75DE9987DF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551I → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035792
Natural varianti465 – 4651R → Q.
Corresponds to variant rs34811474 [ dbSNP | Ensembl ].
VAR_054044
Natural varianti800 – 8001E → G.
Corresponds to variant rs11550697 [ dbSNP | Ensembl ].
VAR_054045

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei542 – 55110DVIGKSMNQA → VSLKEMHVFV in isoform 2.
VSP_008464
Alternative sequencei552 – 808257Missing in isoform 2.
VSP_008465Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti286 – 2861R → C in AAF05752. 1 Publication
Sequence conflicti293 – 2953EKN → GKD in AAF05752. 1 Publication
Sequence conflicti756 – 7561E → G in AAH59383. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF191338 mRNA. Translation: AAF05752.1.
AK292336 mRNA. Translation: BAF85025.1.
CH471069 Genomic DNA. Translation: EAW92839.1.
BC059383 mRNA. Translation: AAH59383.1.
AL353932 mRNA. Translation: CAB89245.1.
CCDSiCCDS3434.1. [Q9UJX5-1]
PIRiT48682.
RefSeqiNP_001273685.1. NM_001286756.1.
NP_037499.2. NM_013367.2. [Q9UJX5-1]
UniGeneiHs.152173.

Genome annotation databases

EnsembliENST00000315368; ENSP00000318775; ENSG00000053900. [Q9UJX5-1]
GeneIDi29945.
KEGGihsa:29945.
UCSCiuc003gro.3. human. [Q9UJX5-1]

Polymorphism databases

DMDMi205371737.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF191338 mRNA. Translation: AAF05752.1 .
AK292336 mRNA. Translation: BAF85025.1 .
CH471069 Genomic DNA. Translation: EAW92839.1 .
BC059383 mRNA. Translation: AAH59383.1 .
AL353932 mRNA. Translation: CAB89245.1 .
CCDSi CCDS3434.1. [Q9UJX5-1 ]
PIRi T48682.
RefSeqi NP_001273685.1. NM_001286756.1.
NP_037499.2. NM_013367.2. [Q9UJX5-1 ]
UniGenei Hs.152173.

3D structure databases

ProteinModelPortali Q9UJX5.
SMRi Q9UJX5. Positions 175-215, 721-749.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118982. 49 interactions.
DIPi DIP-56450N.
IntActi Q9UJX5. 26 interactions.
MINTi MINT-4787108.
STRINGi 9606.ENSP00000318775.

PTM databases

PhosphoSitei Q9UJX5.

Polymorphism databases

DMDMi 205371737.

Proteomic databases

MaxQBi Q9UJX5.
PaxDbi Q9UJX5.
PRIDEi Q9UJX5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315368 ; ENSP00000318775 ; ENSG00000053900 . [Q9UJX5-1 ]
GeneIDi 29945.
KEGGi hsa:29945.
UCSCi uc003gro.3. human. [Q9UJX5-1 ]

Organism-specific databases

CTDi 29945.
GeneCardsi GC04P025462.
HGNCi HGNC:19990. ANAPC4.
HPAi CAB032519.
HPA038395.
HPA038396.
MIMi 606947. gene.
neXtProti NX_Q9UJX5.
PharmGKBi PA134894250.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG248176.
HOGENOMi HOG000033987.
HOVERGENi HBG044815.
InParanoidi Q9UJX5.
KOi K03351.
OrthoDBi EOG7S21XB.
PhylomeDBi Q9UJX5.
TreeFami TF105443.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSi ANAPC4. human.
GeneWikii ANAPC4.
GenomeRNAii 29945.
NextBioi 52611.
PROi Q9UJX5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UJX5.
Bgeei Q9UJX5.
CleanExi HS_ANAPC4.
Genevestigatori Q9UJX5.

Family and domain databases

Gene3Di 2.130.10.10. 2 hits.
InterProi IPR024789. APC4.
IPR024790. APC4_long_dom.
IPR017169. APC4_metazoa.
IPR024977. Apc4_WD40_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view ]
PANTHERi PTHR13260. PTHR13260. 1 hit.
Pfami PF12896. Apc4. 1 hit.
PF12894. Apc4_WD40. 1 hit.
[Graphical view ]
PIRSFi PIRSF037303. APC4. 1 hit.
SUPFAMi SSF50978. SSF50978. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a cullin homology region in a subunit of the anaphase-promoting complex."
    Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W.
    Science 279:1219-1222(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Tissue: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-808 (ISOFORM 2).
    Tissue: Amygdala.
  6. "Mitotic regulation of the human anaphase-promoting complex by phosphorylation."
    Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J., Peters J.-M.
    EMBO J. 22:6598-6609(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-469 AND SER-779.
  7. "Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex."
    Jin L., Williamson A., Banerjee S., Philipp I., Rape M.
    Cell 133:653-665(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE APC/C.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757; SER-758; SER-777 AND SER-779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C."
    Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A., Engel A., Peters J.-M., Stark H.
    Mol. Cell 20:867-879(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY OF THE APC/C.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-155.

Entry informationi

Entry nameiAPC4_HUMAN
AccessioniPrimary (citable) accession number: Q9UJX5
Secondary accession number(s): A8K8H1, Q6PCC6, Q9NSH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: September 2, 2008
Last modified: September 3, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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