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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: 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

  • protein phosphatase binding Source: BHF-UCL
  • ubiquitin-protein transferase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-983168. 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 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:19990. ANAPC4.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • 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 – 7571PhosphoserineCombined sources
Modified residuei758 – 7581PhosphoserineCombined sources
Modified residuei777 – 7771PhosphoserineCombined sources
Modified residuei779 – 7791Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UJX5.
PaxDbiQ9UJX5.
PRIDEiQ9UJX5.

PTM databases

iPTMnetiQ9UJX5.
PhosphoSiteiQ9UJX5.

Expressioni

Gene expression databases

BgeeiQ9UJX5.
CleanExiHS_ANAPC4.
ExpressionAtlasiQ9UJX5. baseline and differential.
GenevisibleiQ9UJX5. HS.

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. 32 interactions.
MINTiMINT-4787108.
STRINGi9606.ENSP00000318775.

Structurei

Secondary structure

1
808
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187Combined sources
Beta strandi23 – 286Combined sources
Beta strandi30 – 3910Combined sources
Beta strandi44 – 496Combined sources
Helixi50 – 523Combined sources
Beta strandi54 – 585Combined sources
Beta strandi62 – 643Combined sources
Beta strandi68 – 736Combined sources
Beta strandi77 – 8711Combined sources
Beta strandi89 – 10517Combined sources
Beta strandi112 – 1176Combined sources
Turni120 – 1223Combined sources
Helixi133 – 1364Combined sources
Beta strandi155 – 1606Combined sources
Helixi162 – 1698Combined sources
Beta strandi174 – 1796Combined sources
Beta strandi183 – 1897Combined sources
Turni190 – 1923Combined sources
Beta strandi193 – 1997Combined sources
Beta strandi203 – 2108Combined sources
Beta strandi214 – 22310Combined sources
Beta strandi228 – 23710Combined sources
Helixi239 – 2435Combined sources
Helixi245 – 28440Combined sources
Turni320 – 3245Combined sources
Helixi327 – 35024Combined sources
Helixi352 – 37019Combined sources
Helixi373 – 3764Combined sources
Helixi383 – 42644Combined sources
Turni427 – 4293Combined sources
Helixi448 – 4569Combined sources
Helixi474 – 4785Combined sources
Helixi526 – 54722Combined sources
Beta strandi551 – 56010Combined sources
Turni561 – 5633Combined sources
Beta strandi573 – 5786Combined sources
Turni579 – 5824Combined sources
Beta strandi583 – 60624Combined sources
Beta strandi614 – 62411Combined sources
Beta strandi636 – 64510Combined sources
Beta strandi648 – 65710Combined sources
Turni659 – 6613Combined sources
Beta strandi664 – 6707Combined sources
Helixi671 – 6733Combined sources
Helixi679 – 6824Combined sources
Beta strandi702 – 7076Combined sources
Beta strandi709 – 7135Combined sources
Beta strandi721 – 7244Combined sources
Beta strandi726 – 7283Combined sources
Beta strandi730 – 7345Combined sources
Beta strandi738 – 7458Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60I1-808[»]
5A31electron microscopy4.30I1-808[»]
5BPWX-ray3.40A1-808[»]
ProteinModelPortaliQ9UJX5.
SMRiQ9UJX5. Positions 6-757.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the APC4 family.Curated

Phylogenomic databases

eggNOGiKOG4640. Eukaryota.
ENOG410XPXK. LUCA.
GeneTreeiENSGT00390000004612.
HOGENOMiHOG000033987.
HOVERGENiHBG044815.
InParanoidiQ9UJX5.
KOiK03351.
OMAiTLDQKSF.
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. ANAPC4. 1 hit.
PF12894. ANAPC4_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]

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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60I1-808[»]
5A31electron microscopy4.30I1-808[»]
5BPWX-ray3.40A1-808[»]
ProteinModelPortaliQ9UJX5.
SMRiQ9UJX5. Positions 6-757.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118982. 56 interactions.
DIPiDIP-56450N.
IntActiQ9UJX5. 32 interactions.
MINTiMINT-4787108.
STRINGi9606.ENSP00000318775.

PTM databases

iPTMnetiQ9UJX5.
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.
GeneCardsiANAPC4.
HGNCiHGNC:19990. ANAPC4.
HPAiCAB032519.
HPA038395.
HPA038396.
MIMi606947. gene.
neXtProtiNX_Q9UJX5.
PharmGKBiPA134894250.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4640. Eukaryota.
ENOG410XPXK. LUCA.
GeneTreeiENSGT00390000004612.
HOGENOMiHOG000033987.
HOVERGENiHBG044815.
InParanoidiQ9UJX5.
KOiK03351.
OMAiTLDQKSF.
OrthoDBiEOG7S21XB.
PhylomeDBiQ9UJX5.
TreeFamiTF105443.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

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

Gene expression databases

BgeeiQ9UJX5.
CleanExiHS_ANAPC4.
ExpressionAtlasiQ9UJX5. baseline and differential.
GenevisibleiQ9UJX5. HS.

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

« 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 AND SER-777, 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: January 20, 2016
This is version 130 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.