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Protein

Anaphase-promoting complex subunit 5

Gene

Anapc5

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 5
Short name:
APC5
Alternative name(s):
Cyclosome subunit 5
Gene namesi
Name:Anapc5
ORF Names:MNCb-2778
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1929722. Anapc5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740Anaphase-promoting complex subunit 5PRO_0000064598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BTZ4.
MaxQBiQ8BTZ4.
PaxDbiQ8BTZ4.
PRIDEiQ8BTZ4.

PTM databases

iPTMnetiQ8BTZ4.
PhosphoSiteiQ8BTZ4.

Expressioni

Gene expression databases

BgeeiQ8BTZ4.
CleanExiMM_ANAPC5.
ExpressionAtlasiQ8BTZ4. baseline and differential.
GenevisibleiQ8BTZ4. MM.

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.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi208479. 19 interactions.
IntActiQ8BTZ4. 10 interactions.
STRINGi10090.ENSMUSP00000083393.

Structurei

3D structure databases

ProteinModelPortaliQ8BTZ4.
SMRiQ8BTZ4. Positions 15-740.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati194 – 23441TPR 1Add
BLAST
Repeati235 – 28551TPR 2Add
BLAST
Repeati286 – 32237TPR 3Add
BLAST
Repeati323 – 36341TPR 4Add
BLAST
Repeati364 – 40340TPR 5Add
BLAST
Repeati404 – 45148TPR 6Add
BLAST
Repeati452 – 48534TPR 7Add
BLAST
Repeati486 – 52540TPR 8Add
BLAST
Repeati526 – 56540TPR 9Add
BLAST
Repeati566 – 60540TPR 10Add
BLAST
Repeati606 – 64540TPR 11Add
BLAST
Repeati646 – 68136TPR 12Add
BLAST
Repeati682 – 72140TPR 13Add
BLAST

Sequence similaritiesi

Belongs to the APC5 family.Curated
Contains 13 TPR repeats.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG4322. Eukaryota.
ENOG410YVZN. LUCA.
GeneTreeiENSGT00390000018674.
HOVERGENiHBG001285.
InParanoidiQ8BTZ4.
KOiK03352.
OMAiLYWRSSC.
OrthoDBiEOG7T7GSR.
PhylomeDBiQ8BTZ4.
TreeFamiTF105444.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR026000. Apc5_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF12862. ANAPC5. 2 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q8BTZ4-1) [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
MMTNGVVHAN LFGIKDWVTP YKIAVLVLLN EMGRTGEGAV SLVERRKLNQ
60 70 80 90 100
LLLPLLQGPD ITLSKLYKLI EESCPQLANS VQIRIKLMAE GELKDMEQFF
110 120 130 140 150
DDLSDSFSGT EPEVHKTSVV GLFLRHMILA YSKLSFSQVF KLYTALQQYF
160 170 180 190 200
QNGEKKTVED ADMDREDGEK QMEKEELDVS VREEEVSCSG PLSQKQAEFF
210 220 230 240 250
LSQQAALLKN DETKALTPAS LQKELNNLLK FNPDFAEAHY LSYLNNLRVQ
260 270 280 290 300
DVFSSTHSLL HYFDRLILTG AEGKSNGEEG YGRSLRYAAL NLAALHCRFG
310 320 330 340 350
HYQQAELALQ EAIRIAQESN DHVCLQHCLS WLYVLGQKRA DSYVLLEHSV
360 370 380 390 400
KKAVHFGLPY LASLGIQSLV QQRAFAGKTA NKLMDALKDS DLLHWKHSLS
410 420 430 440 450
ELIDISIAQK TAIWRLYGRS TMALQQAQML LSMNSLESLN AGVQQNNTES
460 470 480 490 500
FAVALCHLAE LHAEQGCFAA AGEVLKHLKD RFPPNSQHAQ LWMLCDQKIQ
510 520 530 540 550
FDRAMNDGKF HLADSLVTGI TALNGIEGVY RKAVVLQAQN QMTEAHKLLQ
560 570 580 590 600
KLLTYCQKLK NTEMVISVLL SVAELYWRSS SPTIAMPVLL EALALSKEYR
610 620 630 640 650
LQYLASETVL NLAYAQLILG IPEQALTLLH MAIEPILADG AVLDKGRAMF
660 670 680 690 700
LVSKCQVASA ASYDPVKKAE ALEAAIQNLS EAKNYFAQVD CRERIRDVAY
710 720 730 740
FQARLYHALG KTQERNHCAM IFRQLHQELP AHGVPLINHL
Length:740
Mass (Da):83,098
Last modified:March 1, 2003 - v1
Checksum:i43CCD0615BCFC184
GO
Isoform 2 (identifier: Q8BTZ4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     360-372: Missing.

Show »
Length:727
Mass (Da):81,696
Checksum:i0B721BC939FC0DE2
GO

Sequence cautioni

The sequence BAA95076.1 differs from that shown. Reason: Frameshift at position 293. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721E → V in BAA95076 (Ref. 1) Curated
Sequence conflicti78 – 781A → E in BAC33891 (PubMed:16141072).Curated
Sequence conflicti248 – 2481R → H in BAA95076 (Ref. 1) Curated
Sequence conflicti501 – 5011F → S in BAA95076 (Ref. 1) Curated
Sequence conflicti511 – 5111H → Y in BAA95076 (Ref. 1) Curated
Sequence conflicti520 – 5201I → V in BAA95076 (Ref. 1) Curated
Sequence conflicti642 – 6421V → I in AAH46566 (PubMed:15489334).Curated
Sequence conflicti662 – 6621S → T in BAC27401 (PubMed:16141072).Curated
Sequence conflicti676 – 6761I → V in AAH46566 (PubMed:15489334).Curated
Sequence conflicti682 – 6821A → T in BAC33891 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei360 – 37213Missing in isoform 2. 1 PublicationVSP_008472Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041593 mRNA. Translation: BAA95076.1. Frameshift.
AK012579 mRNA. Translation: BAB28331.1.
AK013978 mRNA. Translation: BAB29097.1.
AK031432 mRNA. Translation: BAC27401.1.
AK049719 mRNA. Translation: BAC33891.1.
AK088327 mRNA. Translation: BAC40284.1.
AK159916 mRNA. Translation: BAE35479.1.
AK168814 mRNA. Translation: BAE40641.1.
AK169196 mRNA. Translation: BAE40972.1.
BC010339 mRNA. Translation: AAH10339.1.
BC046566 mRNA. Translation: AAH46566.1.
BC046804 mRNA. Translation: AAH46804.1.
CCDSiCCDS39258.1. [Q8BTZ4-1]
CCDS80397.1. [Q8BTZ4-2]
RefSeqiNP_001035956.1. NM_001042491.2. [Q8BTZ4-2]
NP_067480.2. NM_021505.3. [Q8BTZ4-1]
UniGeneiMm.332667.

Genome annotation databases

EnsembliENSMUST00000086216; ENSMUSP00000083393; ENSMUSG00000029472. [Q8BTZ4-1]
ENSMUST00000200645; ENSMUSP00000142922; ENSMUSG00000029472. [Q8BTZ4-2]
GeneIDi59008.
KEGGimmu:59008.
UCSCiuc008zmg.2. mouse. [Q8BTZ4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041593 mRNA. Translation: BAA95076.1. Frameshift.
AK012579 mRNA. Translation: BAB28331.1.
AK013978 mRNA. Translation: BAB29097.1.
AK031432 mRNA. Translation: BAC27401.1.
AK049719 mRNA. Translation: BAC33891.1.
AK088327 mRNA. Translation: BAC40284.1.
AK159916 mRNA. Translation: BAE35479.1.
AK168814 mRNA. Translation: BAE40641.1.
AK169196 mRNA. Translation: BAE40972.1.
BC010339 mRNA. Translation: AAH10339.1.
BC046566 mRNA. Translation: AAH46566.1.
BC046804 mRNA. Translation: AAH46804.1.
CCDSiCCDS39258.1. [Q8BTZ4-1]
CCDS80397.1. [Q8BTZ4-2]
RefSeqiNP_001035956.1. NM_001042491.2. [Q8BTZ4-2]
NP_067480.2. NM_021505.3. [Q8BTZ4-1]
UniGeneiMm.332667.

3D structure databases

ProteinModelPortaliQ8BTZ4.
SMRiQ8BTZ4. Positions 15-740.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208479. 19 interactions.
IntActiQ8BTZ4. 10 interactions.
STRINGi10090.ENSMUSP00000083393.

PTM databases

iPTMnetiQ8BTZ4.
PhosphoSiteiQ8BTZ4.

Proteomic databases

EPDiQ8BTZ4.
MaxQBiQ8BTZ4.
PaxDbiQ8BTZ4.
PRIDEiQ8BTZ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086216; ENSMUSP00000083393; ENSMUSG00000029472. [Q8BTZ4-1]
ENSMUST00000200645; ENSMUSP00000142922; ENSMUSG00000029472. [Q8BTZ4-2]
GeneIDi59008.
KEGGimmu:59008.
UCSCiuc008zmg.2. mouse. [Q8BTZ4-1]

Organism-specific databases

CTDi51433.
MGIiMGI:1929722. Anapc5.

Phylogenomic databases

eggNOGiKOG4322. Eukaryota.
ENOG410YVZN. LUCA.
GeneTreeiENSGT00390000018674.
HOVERGENiHBG001285.
InParanoidiQ8BTZ4.
KOiK03352.
OMAiLYWRSSC.
OrthoDBiEOG7T7GSR.
PhylomeDBiQ8BTZ4.
TreeFamiTF105444.

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

ChiTaRSiAnapc5. mouse.
NextBioi314542.
PROiQ8BTZ4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BTZ4.
CleanExiMM_ANAPC5.
ExpressionAtlasiQ8BTZ4. baseline and differential.
GenevisibleiQ8BTZ4. MM.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR026000. Apc5_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF12862. ANAPC5. 2 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
    Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Brain.
  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] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Embryo, Heart, Kidney, Spinal cord, Testis and Thymus.
  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 2).
    Strain: Czech II.
    Tissue: Brain and Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiAPC5_MOUSE
AccessioniPrimary (citable) accession number: Q8BTZ4
Secondary accession number(s): Q3TGA7
, Q80UJ6, Q80W43, Q8BWW7, Q8C0F7, Q9CRX0, Q9CSL1, Q9JJB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 119 of the entry and version 1 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.