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Q8BZQ7

- ANC2_MOUSE

UniProt

Q8BZQ7 - ANC2_MOUSE

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Protein

Anaphase-promoting complex subunit 2

Gene

Anapc2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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. 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.1 Publication

Pathwayi

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
  2. positive regulation of axon extension Source: Ensembl
  3. positive regulation of dendrite morphogenesis Source: Ensembl
  4. positive regulation of synapse maturation Source: UniProtKB
  5. positive regulation of synaptic plasticity Source: UniProtKB
  6. protein K11-linked ubiquitination Source: UniProtKB
  7. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, Mitosis, Neurogenesis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_205250. Phosphorylation of the APC/C.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_207679. Separation of Sister Chromatids.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_215601. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2139135. Anapc2.

Subcellular locationi

GO - Cellular componenti

  1. anaphase-promoting complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 837837Anaphase-promoting complex subunit 2PRO_0000119812Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei233 – 2331PhosphoserineBy similarity
Modified residuei329 – 3291PhosphoserineBy similarity
Modified residuei485 – 4851PhosphoserineBy similarity
Modified residuei549 – 5491PhosphoserineBy similarity
Modified residuei825 – 8251Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BZQ7.
PaxDbiQ8BZQ7.
PRIDEiQ8BZQ7.

PTM databases

PhosphoSiteiQ8BZQ7.

Expressioni

Gene expression databases

BgeeiQ8BZQ7.
CleanExiMM_ANAPC2.
ExpressionAtlasiQ8BZQ7. baseline and differential.
GenevestigatoriQ8BZQ7.

Interactioni

Subunit structurei

The APC/C is composed of at least 12 subunits (By similarity). Interacts with NEUROD2.By similarity1 Publication

Protein-protein interaction databases

BioGridi221196. 13 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8BZQ7.
SMRiQ8BZQ7. Positions 495-711.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5647.
GeneTreeiENSGT00390000016127.
HOVERGENiHBG045327.
InParanoidiQ8BZQ7.
KOiK03349.
OMAiELLVAWN.
OrthoDBiEOG76MK7Q.
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]

Sequencei

Sequence statusi: Complete.

Q8BZQ7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEAEGVAVAA AAAAAAAAAT IIASDDCDSR PGQELLVAWN TVSTGLVPPA
60 70 80 90 100
ALGLASSRTS GAVPPKEEEL RAAVEVLRGH GLHSVLEEWF VEVLQNDLQG
110 120 130 140 150
NIATEFWNAI ALRENSVDEP QCLGLLLDAF GLLESRLDPY LHSLELLEKW
160 170 180 190 200
TRLGLLMGAG AQGLREKVHT MLRGVLFFST PRTFQEMVQR LYGRFLRVYM
210 220 230 240 250
QSKRKGEGGT DPELEGELDS RYARRRYYRL LQSPLCAGCG SDKQQCWCRQ
260 270 280 290 300
ALEQFNQLSQ VLHRLSLLER VCAEAVTTTL HQVTRERMED RCRGEYERSF
310 320 330 340 350
LREFHKWIER VVGWLGKVFL QDNPTRPTSP EAGNTLRRWR CHVQRFFYRI
360 370 380 390 400
YATLRIEELF SIIRDFPDSR PAIEDLKYCL ERTDQRQQLL VSLKVALETR
410 420 430 440 450
LLHPGVNTCD IITLYISAIK ALRVLDPSMV ILEVACEPIR RYLRTREDTV
460 470 480 490 500
RQIVAGLTGD SDGTGDLAVE LSKTDPACLE TGQDSEDDSG EPEDWVPDPV
510 520 530 540 550
DADPVKSSSK RRSSDIISLL VSIYGSKDLF INEYRSLLAD RLLHQFSFSP
560 570 580 590 600
EREIRNVELL KLRFGEAPMH FCEVMLKDMA DSRRINANIR EEDEKRPVEE
610 620 630 640 650
QPPFGVYAVI LSSEFWPPFK DEKLEVPEDI RAALDVYCKK YEKLKAMRTL
660 670 680 690 700
SWKHTLGLVT MDVELADRTL SVAVTPVQAV VLLYFQNQAS WTLEELSKVV
710 720 730 740 750
KMPVALLRRR MSVWLQQGVL REEPPGTFSV IEEERPQDRD NMVLIDSDDE
760 770 780 790 800
SDSGMASQAD QKEEELLLFW AYIQAMLTNL ESLSLERIYS MLRMFVMTGP
810 820 830
ALAEIDLQEL QGYLQKKVRD QQLIYSAGVY RLPKNSN
Length:837
Mass (Da):95,307
Last modified:July 27, 2011 - v2
Checksum:i02E62B928C0E20B3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti680 – 6801V → L in BAC28472. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK033784 mRNA. Translation: BAC28472.1.
AK170676 mRNA. Translation: BAE41951.1.
AL732309 Genomic DNA. Translation: CAM14680.1.
BC027351 mRNA. Translation: AAH27351.1.
BC137583 mRNA. Translation: AAI37584.1.
CCDSiCCDS15761.1.
RefSeqiNP_780509.2. NM_175300.4.
UniGeneiMm.291624.

Genome annotation databases

EnsembliENSMUST00000028341; ENSMUSP00000028341; ENSMUSG00000026965.
GeneIDi99152.
KEGGimmu:99152.
UCSCiuc008ird.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK033784 mRNA. Translation: BAC28472.1 .
AK170676 mRNA. Translation: BAE41951.1 .
AL732309 Genomic DNA. Translation: CAM14680.1 .
BC027351 mRNA. Translation: AAH27351.1 .
BC137583 mRNA. Translation: AAI37584.1 .
CCDSi CCDS15761.1.
RefSeqi NP_780509.2. NM_175300.4.
UniGenei Mm.291624.

3D structure databases

ProteinModelPortali Q8BZQ7.
SMRi Q8BZQ7. Positions 495-711.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 221196. 13 interactions.

PTM databases

PhosphoSitei Q8BZQ7.

Proteomic databases

MaxQBi Q8BZQ7.
PaxDbi Q8BZQ7.
PRIDEi Q8BZQ7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028341 ; ENSMUSP00000028341 ; ENSMUSG00000026965 .
GeneIDi 99152.
KEGGi mmu:99152.
UCSCi uc008ird.2. mouse.

Organism-specific databases

CTDi 29882.
MGIi MGI:2139135. Anapc2.

Phylogenomic databases

eggNOGi COG5647.
GeneTreei ENSGT00390000016127.
HOVERGENi HBG045327.
InParanoidi Q8BZQ7.
KOi K03349.
OMAi ELLVAWN.
OrthoDBi EOG76MK7Q.
TreeFami TF105442.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_205250. Phosphorylation of the APC/C.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_207679. Separation of Sister Chromatids.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_215601. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.

Miscellaneous databases

NextBioi 353811.
PROi Q8BZQ7.
SOURCEi Search...

Gene expression databases

Bgeei Q8BZQ7.
CleanExi MM_ANAPC2.
ExpressionAtlasi Q8BZQ7. baseline and differential.
Genevestigatori Q8BZQ7.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR014786. APC_su2_C.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF08672. APC2. 1 hit.
PF00888. Cullin. 1 hit.
[Graphical view ]
SMARTi SM01013. APC2. 1 hit.
SM00182. CULLIN. 1 hit.
[Graphical view ]
SUPFAMi SSF75632. SSF75632. 1 hit.
PROSITEi PS50069. CULLIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J and NOD.
    Tissue: Epididymis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
  4. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  5. "A Cdc20-APC ubiquitin signaling pathway regulates presynaptic differentiation."
    Yang Y., Kim A.H., Yamada T., Wu B., Bilimoria P.M., Ikeuchi Y., de la Iglesia N., Shen J., Bonni A.
    Science 326:575-578(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NEUROD2.

Entry informationi

Entry nameiANC2_MOUSE
AccessioniPrimary (citable) accession number: Q8BZQ7
Secondary accession number(s): Q3TCK5, Q8R2Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 90 of the entry and version 2 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

External Data

Dasty 3