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Protein

Anaphase-promoting complex subunit 4

Gene

ANAPC4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 phosphatase binding Source: BHF-UCL
  2. ubiquitin-protein transferase activity Source: ProtInc

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. cell division Source: UniProtKB-KW
  3. mitotic cell cycle Source: Reactome
  4. mitotic nuclear division Source: UniProtKB-KW
  5. mitotic spindle assembly checkpoint Source: Reactome
  6. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  7. positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition Source: Reactome
  8. protein K11-linked ubiquitination Source: UniProtKB
  9. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
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_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
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.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
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 Componenti: 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.

Polymorphism and mutation databases

BioMutaiANAPC4.
DMDMi205371737.

PTM / Processingi

Molecule processing

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

BgeeiQ9UJX5.
CleanExiHS_ANAPC4.
ExpressionAtlasiQ9UJX5. baseline and differential.
GenevestigatoriQ9UJX5.

Organism-specific databases

HPAiCAB032519.
HPA038395.
HPA038396.

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.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi118982. 56 interactions.
DIPiDIP-56450N.
IntActiQ9UJX5. 26 interactions.
MINTiMINT-4787108.
STRINGi9606.ENSP00000318775.

Structurei

3D structure databases

ProteinModelPortaliQ9UJX5.
SMRiQ9UJX5. Positions 12-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the APC4 family.Curated

Phylogenomic databases

eggNOGiNOG248176.
GeneTreeiENSGT00390000004612.
HOGENOMiHOG000033987.
HOVERGENiHBG044815.
InParanoidiQ9UJX5.
KOiK03351.
OMAiRQVGEKQ.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA
60 70 80 90 100
SFHRVWSFPP NENTGKEVTC LAWRPDGKLL AFALADTKKI VLCDVEKPES
110 120 130 140 150
LHSFSVEAPV SCMHWMEVTV ESSVLTSFYN AEDESNLLLP KLPTLPKNYS
160 170 180 190 200
NTSKIFSEEN SDEIIKLLGD VRLNILVLGG SSGFIELYAY GMFKIARVTG
210 220 230 240 250
IAGTCLALCL SSDLKSLSVV TEVSTNGASE VSYFQLETNL LYSFLPEVTR
260 270 280 290 300
MARKFTHISA LLQYINLSLT CMCEAWEEIL MQMDSRLTKF VQEKNTTTSV
310 320 330 340 350
QDEFMHLLLW GKASAELQTL LMNQLTVKGL KKLGQSIESS YSSIQKLVIS
360 370 380 390 400
HLQSGSESLL YHLSELKGMA SWKQKYEPLG LDAAGIEEAI 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
LQNSSHLKES PLLFPYYPRK SLHFVKRRME NIIDQCLQKP ADVIGKSMNQ
560 570 580 590 600
AICIPLYRDT RSEDSTRRLF KFPFLWNNKT SNLHYLLFTI LEDSLYKMCI
610 620 630 640 650
LRRHTDISQS VSNGLIAIKF GSFTYATTEK VRRSIYSCLD AQFYDDETVT
660 670 680 690 700
VVLKDTVGRE GRDRLLVQLP LSLVYNSEDS AEYQFTGTYS TRLDEQCSAI
710 720 730 740 750
PTRTMHFEKH WRLLESMKAQ YVAGNGFRKV SCVLSSNLRH VRVFEMDIDD
760 770 780 790 800
EWELDESSDE EEEASNKPVK IKEEVLSESE AENQQAGAAA LAPEIVIKVE

KLDPELDS
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
Isoform 3 (identifier: Q9UJX5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     439-439: K → KV

Note: No experimental confirmation available.

Show »
Length:809
Mass (Da):92,216
Checksum:iDD0B4899C6501E09
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti286 – 2861R → C in AAF05752 (PubMed:9469815).Curated
Sequence conflicti293 – 2953EKN → GKD in AAF05752 (PubMed:9469815).Curated
Sequence conflicti756 – 7561E → G in AAH59383 (PubMed:15489334).Curated

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 sequencei439 – 4391K → KV in isoform 3. CuratedVSP_056708
Alternative sequencei542 – 55110DVIGKSMNQA → VSLKEMHVFV in isoform 2. 1 PublicationVSP_008464
Alternative sequencei552 – 808257Missing in isoform 2. 1 PublicationVSP_008465Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS68684.1. [Q9UJX5-3]
PIRiT48682.
RefSeqiNP_001273685.1. NM_001286756.1. [Q9UJX5-3]
NP_037499.2. NM_013367.2. [Q9UJX5-1]
UniGeneiHs.152173.

Genome annotation databases

EnsembliENST00000315368; ENSP00000318775; ENSG00000053900. [Q9UJX5-1]
ENST00000510092; ENSP00000426654; ENSG00000053900. [Q9UJX5-3]
GeneIDi29945.
KEGGihsa:29945.
UCSCiuc003gro.3. human. [Q9UJX5-1]

Polymorphism and mutation databases

BioMutaiANAPC4.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS68684.1. [Q9UJX5-3]
PIRiT48682.
RefSeqiNP_001273685.1. NM_001286756.1. [Q9UJX5-3]
NP_037499.2. NM_013367.2. [Q9UJX5-1]
UniGeneiHs.152173.

3D structure databases

ProteinModelPortaliQ9UJX5.
SMRiQ9UJX5. Positions 12-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118982. 56 interactions.
DIPiDIP-56450N.
IntActiQ9UJX5. 26 interactions.
MINTiMINT-4787108.
STRINGi9606.ENSP00000318775.

PTM databases

PhosphoSiteiQ9UJX5.

Polymorphism and mutation databases

BioMutaiANAPC4.
DMDMi205371737.

Proteomic databases

MaxQBiQ9UJX5.
PaxDbiQ9UJX5.
PRIDEiQ9UJX5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315368; ENSP00000318775; ENSG00000053900. [Q9UJX5-1]
ENST00000510092; ENSP00000426654; ENSG00000053900. [Q9UJX5-3]
GeneIDi29945.
KEGGihsa:29945.
UCSCiuc003gro.3. human. [Q9UJX5-1]

Organism-specific databases

CTDi29945.
GeneCardsiGC04P025379.
HGNCiHGNC:19990. ANAPC4.
HPAiCAB032519.
HPA038395.
HPA038396.
MIMi606947. gene.
neXtProtiNX_Q9UJX5.
PharmGKBiPA134894250.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG248176.
GeneTreeiENSGT00390000004612.
HOGENOMiHOG000033987.
HOVERGENiHBG044815.
InParanoidiQ9UJX5.
KOiK03351.
OMAiRQVGEKQ.
OrthoDBiEOG7S21XB.
PhylomeDBiQ9UJX5.
TreeFamiTF105443.

Enzyme and pathway databases

UniPathwayiUPA00143.
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_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
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.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Miscellaneous databases

ChiTaRSiANAPC4. human.
GeneWikiiANAPC4.
GenomeRNAii29945.
NextBioi35501547.
PROiQ9UJX5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJX5.
CleanExiHS_ANAPC4.
ExpressionAtlasiQ9UJX5. baseline and differential.
GenevestigatoriQ9UJX5.

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.
ProtoNetiSearch...

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. "Molecular architecture and mechanism of the anaphase-promoting complex."
    Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.
    Nature 513:388-393(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, SUBUNIT.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-155.

Entry informationi

Entry nameiAPC4_HUMAN
AccessioniPrimary (citable) accession number: Q9UJX5
Secondary accession number(s): A8K8H1
, E9PCR4, Q6PCC6, Q9NSH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: September 2, 2008
Last modified: April 29, 2015
This is version 122 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

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 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.