Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Anaphase-promoting complex subunit 7

Gene

Anapc7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit 7
Short name:
APC7
Alternative name(s):
Cyclosome subunit 7
Prediabetic NOD sera-reactive autoantigen
Gene namesi
Name:Anapc7
Synonyms:Apc7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1929711. Anapc7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 565565Anaphase-promoting complex subunit 7PRO_0000106262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei229 – 2291N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9WVM3.
MaxQBiQ9WVM3.
PaxDbiQ9WVM3.
PRIDEiQ9WVM3.

PTM databases

iPTMnetiQ9WVM3.
PhosphoSiteiQ9WVM3.

Expressioni

Gene expression databases

BgeeiQ9WVM3.
CleanExiMM_ANAPC7.
ExpressionAtlasiQ9WVM3. baseline and differential.
GenevisibleiQ9WVM3. MM.

Interactioni

Subunit structurei

V-shaped homodimer. 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.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207898. 6 interactions.
IntActiQ9WVM3. 3 interactions.
MINTiMINT-1746955.
STRINGi10090.ENSMUSP00000031422.

Structurei

3D structure databases

ProteinModelPortaliQ9WVM3.
SMRiQ9WVM3. Positions 2-518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati101 – 13434TPR 1Add
BLAST
Repeati169 – 20234TPR 2Add
BLAST
Repeati203 – 23634TPR 3Add
BLAST
Repeati237 – 27034TPR 4Add
BLAST
Repeati339 – 37234TPR 5Add
BLAST
Repeati373 – 40634TPR 6Add
BLAST
Repeati407 – 43933TPR 7Add
BLAST
Repeati442 – 47433TPR 8Add
BLAST
Repeati475 – 50834TPR 9Add
BLAST
Repeati509 – 53123TPR 10Add
BLAST

Sequence similaritiesi

Belongs to the APC7 family.Curated
Contains 10 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1174. Eukaryota.
ENOG410XS2B. LUCA.
GeneTreeiENSGT00390000005482.
HOGENOMiHOG000007393.
HOVERGENiHBG050529.
InParanoidiQ9WVM3.
KOiK03354.
OMAiSIPNLDW.
OrthoDBiEOG71VSS4.
PhylomeDBiQ9WVM3.
TreeFamiTF105445.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WVM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVIDHVRDM AAAGLHSNVR LLSSLLLTMS NNNPELFSPS QKYQLLVYHA
60 70 80 90 100
DSLFHDKEYR NAVSKYAMAL QQKKALSKTS KVRPSTGNSA STPQSQCLPS
110 120 130 140 150
EIEVKYKMAE CYTMLKLDKD AIAVLDGIPS RQRTPKINMM LANLYKKAGQ
160 170 180 190 200
ERPSVTSYKE VLRQCPLALD AILGLLSLSV KGAEVASMTM NVIQTVPNLD
210 220 230 240 250
WLSVWIKAYA FVHTGDNSRA INTICSLEKK SLLRDNVDLL GSLADLYFRA
260 270 280 290 300
GDSKNSVLKF EQAQMLDPYL IRGMDVYGYL LAREGRLEDV ENLGCRLFNI
310 320 330 340 350
SDQHAEPWVV SGCHSFYSKR YSRALYLGAK AIQLNSNSVQ ALLLKGAALR
360 370 380 390 400
NMGRVQEAII HFREAIRLAP CRLDCYEGLI ECYLASNSIR EAMVMANNVY
410 420 430 440 450
KTLGANAQTL TLLATVCLED PVTQEKAKTL LDKALAQRPD YVKAVVKKAE
460 470 480 490 500
LLSREQKYED GIALLRNALA NQSDCVLHRI LGDFLVAVNE YQEAMDQYSI
510 520 530 540 550
ALSLDPNDQK SLEGMQKMEK EESPTDATQE EDVDDMEGSG EEGDLEGSDS
560
EAAQWADQEQ WFGMQ
Length:565
Mass (Da):63,021
Last modified:October 3, 2003 - v3
Checksum:iF7DFB8D45FDCD639
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561T → A in AAD39343 (PubMed:10515598).Curated
Sequence conflicti188 – 1881M → T in AAD39343 (PubMed:10515598).Curated
Sequence conflicti288 – 2881E → K in BAC27131 (PubMed:16141072).Curated
Sequence conflicti340 – 3401Q → K in BAC27131 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076607 mRNA. Translation: AAD39343.2.
AK030775 mRNA. Translation: BAC27131.1.
AK150764 mRNA. Translation: BAE29831.1.
AK150891 mRNA. Translation: BAE29937.1.
AK153114 mRNA. Translation: BAE31731.1.
AK159523 mRNA. Translation: BAE35152.1.
AK164202 mRNA. Translation: BAE37680.1.
BC006635 mRNA. Translation: AAH06635.1.
CCDSiCCDS19649.1.
RefSeqiNP_062779.3. NM_019805.4.
UniGeneiMm.37341.

Genome annotation databases

EnsembliENSMUST00000031422; ENSMUSP00000031422; ENSMUSG00000029466.
ENSMUST00000122010; ENSMUSP00000113928; ENSMUSG00000029466.
GeneIDi56317.
KEGGimmu:56317.
UCSCiuc008zlh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076607 mRNA. Translation: AAD39343.2.
AK030775 mRNA. Translation: BAC27131.1.
AK150764 mRNA. Translation: BAE29831.1.
AK150891 mRNA. Translation: BAE29937.1.
AK153114 mRNA. Translation: BAE31731.1.
AK159523 mRNA. Translation: BAE35152.1.
AK164202 mRNA. Translation: BAE37680.1.
BC006635 mRNA. Translation: AAH06635.1.
CCDSiCCDS19649.1.
RefSeqiNP_062779.3. NM_019805.4.
UniGeneiMm.37341.

3D structure databases

ProteinModelPortaliQ9WVM3.
SMRiQ9WVM3. Positions 2-518.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207898. 6 interactions.
IntActiQ9WVM3. 3 interactions.
MINTiMINT-1746955.
STRINGi10090.ENSMUSP00000031422.

PTM databases

iPTMnetiQ9WVM3.
PhosphoSiteiQ9WVM3.

Proteomic databases

EPDiQ9WVM3.
MaxQBiQ9WVM3.
PaxDbiQ9WVM3.
PRIDEiQ9WVM3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031422; ENSMUSP00000031422; ENSMUSG00000029466.
ENSMUST00000122010; ENSMUSP00000113928; ENSMUSG00000029466.
GeneIDi56317.
KEGGimmu:56317.
UCSCiuc008zlh.2. mouse.

Organism-specific databases

CTDi51434.
MGIiMGI:1929711. Anapc7.

Phylogenomic databases

eggNOGiKOG1174. Eukaryota.
ENOG410XS2B. LUCA.
GeneTreeiENSGT00390000005482.
HOGENOMiHOG000007393.
HOVERGENiHBG050529.
InParanoidiQ9WVM3.
KOiK03354.
OMAiSIPNLDW.
OrthoDBiEOG71VSS4.
PhylomeDBiQ9WVM3.
TreeFamiTF105445.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi312272.
PROiQ9WVM3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVM3.
CleanExiMM_ANAPC7.
ExpressionAtlasiQ9WVM3. baseline and differential.
GenevisibleiQ9WVM3. MM.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new autoantigen reactive with prediabetic nonobese diabetic mice sera."
    Kang Y., Choi K.S., Kim K.H., Kim K.S., Choi S.E., Ko I.Y., Kim H.M., Yoon J.W.
    Mol. Cells 9:358-364(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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.
    Tissue: Bone marrow and Hippocampus.
  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].
    Tissue: Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiAPC7_MOUSE
AccessioniPrimary (citable) accession number: Q9WVM3
Secondary accession number(s): Q3UBM7, Q8BSR2, Q91W13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: May 11, 2016
This is version 128 of the entry and version 3 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

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.