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Protein

Anaphase-promoting complex subunit 2

Gene

ANAPC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Together with the RING-H2 protein ANAPC11, constitutes the catalytic 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. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 drives presynaptic differentiation.2 Publications

Pathway:iprotein 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 - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, Mitosis, Neurogenesis, 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.
SignaLinkiQ9UJX6.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit 2
Short name:
APC2
Alternative name(s):
Cyclosome subunit 2
Gene namesi
Name:ANAPC2
Synonyms:APC2, KIAA1406
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:19989. ANAPC2.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134884359.

Polymorphism and mutation databases

BioMutaiANAPC2.
DMDMi37537863.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 822822Anaphase-promoting complex subunit 2PRO_0000119811Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei218 – 2181Phosphoserine3 Publications
Modified residuei314 – 3141Phosphoserine2 Publications
Modified residuei470 – 4701Phosphoserine2 Publications
Modified residuei534 – 5341Phosphoserine2 Publications
Modified residuei810 – 8101PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UJX6.
PaxDbiQ9UJX6.
PRIDEiQ9UJX6.

PTM databases

PhosphoSiteiQ9UJX6.

Expressioni

Gene expression databases

BgeeiQ9UJX6.
CleanExiHS_ANAPC2.
HS_APC2.
GenevisibleiQ9UJX6. HS.

Organism-specific databases

HPAiCAB018692.

Interactioni

Subunit structurei

Interacts with NEUROD2 (By similarity). 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. Interacts through the cullin domain with ANAPC11 and with UBCH10.By similarity3 Publications

Protein-protein interaction databases

BioGridi118937. 53 interactions.
DIPiDIP-32957N.
IntActiQ9UJX6. 21 interactions.
MINTiMINT-1196367.
STRINGi9606.ENSP00000314004.

Structurei

Secondary structure

1
822
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi748 – 76518Combined sources
Helixi770 – 78011Combined sources
Helixi792 – 80413Combined sources
Beta strandi807 – 8115Combined sources
Beta strandi814 – 8163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YIIX-ray1.80A735-822[»]
ProteinModelPortaliQ9UJX6.
SMRiQ9UJX6. Positions 508-696.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni502 – 700199Cullin homology1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5647.
GeneTreeiENSGT00390000016127.
HOGENOMiHOG000033936.
HOVERGENiHBG045327.
InParanoidiQ9UJX6.
KOiK03349.
OMAiKVHTMLR.
OrthoDBiEOG76MK7Q.
PhylomeDBiQ9UJX6.
TreeFamiTF105442.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR014786. APC_su2_C.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08672. APC2. 1 hit.
PF00888. Cullin. 1 hit.
[Graphical view]
SMARTiSM01013. APC2. 1 hit.
SM00182. CULLIN. 1 hit.
[Graphical view]
SUPFAMiSSF75632. SSF75632. 1 hit.
PROSITEiPS50069. CULLIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UJX6-1) [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
MAAAVVVAEG DSDSRPGQEL LVAWNTVSTG LVPPAALGLV SSRTSGAVPP
60 70 80 90 100
KEEELRAAVE VLRGHGLHSV LEEWFVEVLQ NDLQANISPE FWNAISQCEN
110 120 130 140 150
SADEPQCLLL LLDAFGLLES RLDPYLRSLE LLEKWTRLGL LMGTGAQGLR
160 170 180 190 200
EEVHTMLRGV LFFSTPRTFQ EMIQRLYGCF LRVYMQSKRK GEGGTDPELE
210 220 230 240 250
GELDSRYARR RYYRLLQSPL CAGCSSDKQQ CWCRQALEQF HQLSQVLHRL
260 270 280 290 300
SLLERVSAEA VTTTLHQVTR ERMEDRCRGE YERSFLREFH KWIERVVGWL
310 320 330 340 350
GKVFLQDGPA RPASPEAGNT LRRWRCHVQR FFYRIYASLR IEELFSIVRD
360 370 380 390 400
FPDSRPAIED LKYCLERTDQ RQQLLVSLKA ALETRLLHPG VNTCDIITLY
410 420 430 440 450
ISAIKALRVL DPSMVILEVA CEPIRRYLRT REDTVRQIVA GLTGDSDGTG
460 470 480 490 500
DLAVELSKTD PASLETGQDS EDDSGEPEDW VPDPVDADPG KSSSKRRSSD
510 520 530 540 550
IISLLVSIYG SKDLFINEYR SLLADRLLHQ FSFSPEREIR NVELLKLRFG
560 570 580 590 600
EAPMHFCEVM LKDMADSRRI NANIREEDEK RPAEEQPPFG VYAVILSSEF
610 620 630 640 650
WPPFKDEKLE VPEDIRAALE AYCKKYEQLK AMRTLSWKHT LGLVTMDVEL
660 670 680 690 700
ADRTLSVAVT PVQAVILLYF QDQASWTLEE LSKAVKMPVA LLRRRMSVWL
710 720 730 740 750
QQGVLREEPP GTFSVIEEER PQDRDNMVLI DSDDESDSGM ASQADQKEEE
760 770 780 790 800
LLLFWTYIQA MLTNLESLSL DRIYNMLRMF VVTGPALAEI DLQELQGYLQ
810 820
KKVRDQQLVY SAGVYRLPKN CS
Length:822
Mass (Da):93,828
Last modified:May 1, 2000 - v1
Checksum:i94A2B1D015805573
GO
Isoform 2 (identifier: Q9UJX6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     350-352: Missing.

Note: No experimental confirmation available.
Show »
Length:819
Mass (Da):93,469
Checksum:iE3FC0627ECE9C324
GO

Sequence cautioni

The sequence AAH09487.2 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei350 – 3523Missing in isoform 2. 1 PublicationVSP_008463

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191337 mRNA. Translation: AAF05751.1.
AL929554 Genomic DNA. Translation: CAH72881.1.
BC032503 mRNA. Translation: AAH32503.1.
BC001579 mRNA. Translation: AAH01579.1.
BC009487 mRNA. Translation: AAH09487.2. Sequence problems.
AB037827 mRNA. Translation: BAA92644.1.
CCDSiCCDS7033.1. [Q9UJX6-1]
RefSeqiNP_037498.1. NM_013366.3. [Q9UJX6-1]
UniGeneiHs.533262.

Genome annotation databases

EnsembliENST00000323927; ENSP00000314004; ENSG00000176248.
GeneIDi29882.
KEGGihsa:29882.
UCSCiuc004clq.1. human. [Q9UJX6-2]
uc004clr.1. human. [Q9UJX6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191337 mRNA. Translation: AAF05751.1.
AL929554 Genomic DNA. Translation: CAH72881.1.
BC032503 mRNA. Translation: AAH32503.1.
BC001579 mRNA. Translation: AAH01579.1.
BC009487 mRNA. Translation: AAH09487.2. Sequence problems.
AB037827 mRNA. Translation: BAA92644.1.
CCDSiCCDS7033.1. [Q9UJX6-1]
RefSeqiNP_037498.1. NM_013366.3. [Q9UJX6-1]
UniGeneiHs.533262.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YIIX-ray1.80A735-822[»]
ProteinModelPortaliQ9UJX6.
SMRiQ9UJX6. Positions 508-696.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118937. 53 interactions.
DIPiDIP-32957N.
IntActiQ9UJX6. 21 interactions.
MINTiMINT-1196367.
STRINGi9606.ENSP00000314004.

PTM databases

PhosphoSiteiQ9UJX6.

Polymorphism and mutation databases

BioMutaiANAPC2.
DMDMi37537863.

Proteomic databases

MaxQBiQ9UJX6.
PaxDbiQ9UJX6.
PRIDEiQ9UJX6.

Protocols and materials databases

DNASUi29882.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323927; ENSP00000314004; ENSG00000176248.
GeneIDi29882.
KEGGihsa:29882.
UCSCiuc004clq.1. human. [Q9UJX6-2]
uc004clr.1. human. [Q9UJX6-1]

Organism-specific databases

CTDi29882.
GeneCardsiGC09M140069.
HGNCiHGNC:19989. ANAPC2.
HPAiCAB018692.
MIMi606946. gene.
neXtProtiNX_Q9UJX6.
PharmGKBiPA134884359.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5647.
GeneTreeiENSGT00390000016127.
HOGENOMiHOG000033936.
HOVERGENiHBG045327.
InParanoidiQ9UJX6.
KOiK03349.
OMAiKVHTMLR.
OrthoDBiEOG76MK7Q.
PhylomeDBiQ9UJX6.
TreeFamiTF105442.

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.
SignaLinkiQ9UJX6.

Miscellaneous databases

ChiTaRSiANAPC2. human.
GeneWikiiANAPC2.
GenomeRNAii29882.
NextBioi52411.
PROiQ9UJX6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJX6.
CleanExiHS_ANAPC2.
HS_APC2.
GenevisibleiQ9UJX6. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR014786. APC_su2_C.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08672. APC2. 1 hit.
PF00888. Cullin. 1 hit.
[Graphical view]
SMARTiSM01013. APC2. 1 hit.
SM00182. CULLIN. 1 hit.
[Graphical view]
SUPFAMiSSF75632. SSF75632. 1 hit.
PROSITEiPS50069. CULLIN_2. 1 hit.
[Graphical view]
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), CULLIN HOMOLOGY REGION, SUBUNIT.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 243-822 (ISOFORM 2).
    Tissue: Brain, Cervix and Ovary.
  4. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-822 (ISOFORM 1).
    Tissue: Brain.
  5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. "APC2 cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex."
    Tang Z., Li B., Bharadwaj R., Zhu H., Oezkan E., Hakala K., Deisenhofer J., Yu H.
    Mol. Biol. Cell 12:3839-3851(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ANAPC11 AND UBCH10.
  7. "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 SER-314 AND SER-534.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-470 AND SER-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "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.
  17. "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.

Entry informationi

Entry nameiANC2_HUMAN
AccessioniPrimary (citable) accession number: Q9UJX6
Secondary accession number(s): Q5VSG1
, Q96DG5, Q96GG4, Q9P2E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: May 1, 2000
Last modified: July 22, 2015
This is version 139 of the entry and version 1 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.