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Q9UJX4

- APC5_HUMAN

UniProt

Q9UJX4 - APC5_HUMAN

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Protein

Anaphase-promoting complex subunit 5

Gene

ANAPC5

Organism
Homo sapiens (Human)
Status
Reviewed - 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

GO - Molecular functioni

  1. protein phosphatase binding Source: BHF-UCL

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. mitotic cell cycle Source: Reactome
  3. mitotic nuclear division Source: UniProtKB-KW
  4. mitotic spindle assembly checkpoint Source: Reactome
  5. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  6. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  7. protein K11-linked ubiquitination Source: UniProtKB
  8. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, 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_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.
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
Synonyms:APC5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:15713. ANAPC5.

Subcellular locationi

GO - Cellular componenti

  1. anaphase-promoting complex Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24788.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 755755Anaphase-promoting complex subunit 5PRO_0000064597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei195 – 1951Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UJX4.
PaxDbiQ9UJX4.
PeptideAtlasiQ9UJX4.
PRIDEiQ9UJX4.

PTM databases

PhosphoSiteiQ9UJX4.

Expressioni

Gene expression databases

BgeeiQ9UJX4.
CleanExiHS_ANAPC5.
ExpressionAtlasiQ9UJX4. baseline and differential.
GenevestigatoriQ9UJX4.

Organism-specific databases

HPAiHPA039457.

Interactioni

Subunit structurei

The APC/C is composed of at least 12 subunits.1 Publication

Protein-protein interaction databases

BioGridi119537. 59 interactions.
DIPiDIP-32945N.
IntActiQ9UJX4. 28 interactions.
MINTiMINT-1391095.
STRINGi9606.ENSP00000261819.

Structurei

3D structure databases

ProteinModelPortaliQ9UJX4.
SMRiQ9UJX4. Positions 304-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati301 – 33434TPR 1Add
BLAST
Repeati522 – 55534TPR 2Add
BLAST
Repeati581 – 61434TPR 3Add
BLAST
Repeati678 – 71134TPR 4Add
BLAST

Sequence similaritiesi

Belongs to the APC5 family.Curated
Contains 4 TPR repeats.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiNOG320252.
GeneTreeiENSGT00390000018674.
HOGENOMiHOG000033988.
HOVERGENiHBG001285.
InParanoidiQ9UJX4.
KOiK03352.
OMAiLYWRSSC.
OrthoDBiEOG7T7GSR.
PhylomeDBiQ9UJX4.
TreeFamiTF105444.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR026000. Apc5/TPR19_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF12862. Apc5. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UJX4-1) [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
MASVHESLYF NPMMTNGVVH ANVFGIKDWV TPYKIAVLVL LNEMSRTGEG
60 70 80 90 100
AVSLMERRRL NQLLLPLLQG PDITLSKLYK LIEESCPQLA NSVQIRIKLM
110 120 130 140 150
AEGELKDMEQ FFDDLSDSFS GTEPEVHKTS VVGLFLRHMI LAYSKLSFSQ
160 170 180 190 200
VFKLYTALQQ YFQNGEKKTV EDADMELTSR DEGERKMEKE ELDVSVREEE
210 220 230 240 250
VSCSGPLSQK QAEFFLSQQA SLLKNDETKA LTPASLQKEL NNLLKFNPDF
260 270 280 290 300
AEAHYLSYLN NLRVQDVFSS THSLLHYFDR LILTGAESKS NGEEGYGRSL
310 320 330 340 350
RYAALNLAAL HCRFGHYQQA ELALQEAIRI AQESNDHVCL QHCLSWLYVL
360 370 380 390 400
GQKRSDSYVL LEHSVKKAVH FGLPYLASLG IQSLVQQRAF AGKTANKLMD
410 420 430 440 450
ALKDSDLLHW KHSLSELIDI SIAQKTAIWR LYGRSTMALQ QAQMLLSMNS
460 470 480 490 500
LEAVNAGVQQ NNTESFAVAL CHLAELHAEQ GCFAAASEVL KHLKERFPPN
510 520 530 540 550
SQHAQLWMLC DQKIQFDRAM NDGKYHLADS LVTGITALNS IEGVYRKAVV
560 570 580 590 600
LQAQNQMSEA HKLLQKLLVH CQKLKNTEMV ISVLLSVAEL YWRSSSPTIA
610 620 630 640 650
LPMLLQALAL SKEYRLQYLA SETVLNLAFA QLILGIPEQA LSLLHMAIEP
660 670 680 690 700
ILADGAILDK GRAMFLVAKC QVASAASYDQ PKKAEALEAA IENLNEAKNY
710 720 730 740 750
FAKVDCKERI RDVVYFQARL YHTLGKTQER NRCAMLFRQL HQELPSHGVP

LINHL
Length:755
Mass (Da):85,077
Last modified:October 3, 2003 - v2
Checksum:i174F68EAB44760EB
GO
Isoform 2 (identifier: Q9UJX4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-121: Missing.
     122-131: TEPEVHKTSV → MLSPCLSSYF
     318-340: QQAELALQEAIRIAQESNDHVCL → TSPPWEYSPLFNRELLLGRRQTS
     341-755: Missing.

Note: No experimental confirmation available.

Show »
Length:219
Mass (Da):25,147
Checksum:iE74D54AFF6C8744E
GO
Isoform 3 (identifier: Q9UJX4-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: Missing.
     375-387: Missing.

Note: No experimental confirmation available.

Show »
Length:643
Mass (Da):72,526
Checksum:i6245611F5812F7CC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241F → L in AAF05753. (PubMed:9469815)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti617 – 6171Q → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_035793

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 121121Missing in isoform 2. 1 PublicationVSP_008466Add
BLAST
Alternative sequencei1 – 9999Missing in isoform 3. 1 PublicationVSP_044878Add
BLAST
Alternative sequencei122 – 13110TEPEVHKTSV → MLSPCLSSYF in isoform 2. 1 PublicationVSP_008467
Alternative sequencei318 – 34023QQAEL…DHVCL → TSPPWEYSPLFNRELLLGRR QTS in isoform 2. 1 PublicationVSP_008468Add
BLAST
Alternative sequencei341 – 755415Missing in isoform 2. 1 PublicationVSP_008469Add
BLAST
Alternative sequencei375 – 38713Missing in isoform 3. 1 PublicationVSP_044879Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF191339 mRNA. Translation: AAF05753.1.
AK025614 mRNA. No translation available.
BX537687 mRNA. Translation: CAD97812.1.
AC048337 Genomic DNA. No translation available.
AC069209 Genomic DNA. No translation available.
BC001081 mRNA. Translation: AAH01081.1.
BC001950 mRNA. Translation: AAH01950.1.
BC006301 mRNA. Translation: AAH06301.1.
BC034243 mRNA. Translation: AAH34243.1.
CCDSiCCDS45000.1. [Q9UJX4-3]
CCDS9220.1. [Q9UJX4-1]
RefSeqiNP_001131031.1. NM_001137559.1. [Q9UJX4-3]
NP_057321.2. NM_016237.4. [Q9UJX4-1]
UniGeneiHs.7101.

Genome annotation databases

EnsembliENST00000261819; ENSP00000261819; ENSG00000089053. [Q9UJX4-1]
ENST00000441917; ENSP00000415061; ENSG00000089053. [Q9UJX4-3]
GeneIDi51433.
KEGGihsa:51433.
UCSCiuc001uag.3. human. [Q9UJX4-1]
uc001uah.3. human.

Polymorphism databases

DMDMi37537861.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF191339 mRNA. Translation: AAF05753.1 .
AK025614 mRNA. No translation available.
BX537687 mRNA. Translation: CAD97812.1 .
AC048337 Genomic DNA. No translation available.
AC069209 Genomic DNA. No translation available.
BC001081 mRNA. Translation: AAH01081.1 .
BC001950 mRNA. Translation: AAH01950.1 .
BC006301 mRNA. Translation: AAH06301.1 .
BC034243 mRNA. Translation: AAH34243.1 .
CCDSi CCDS45000.1. [Q9UJX4-3 ]
CCDS9220.1. [Q9UJX4-1 ]
RefSeqi NP_001131031.1. NM_001137559.1. [Q9UJX4-3 ]
NP_057321.2. NM_016237.4. [Q9UJX4-1 ]
UniGenei Hs.7101.

3D structure databases

ProteinModelPortali Q9UJX4.
SMRi Q9UJX4. Positions 304-330.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119537. 59 interactions.
DIPi DIP-32945N.
IntActi Q9UJX4. 28 interactions.
MINTi MINT-1391095.
STRINGi 9606.ENSP00000261819.

PTM databases

PhosphoSitei Q9UJX4.

Polymorphism databases

DMDMi 37537861.

Proteomic databases

MaxQBi Q9UJX4.
PaxDbi Q9UJX4.
PeptideAtlasi Q9UJX4.
PRIDEi Q9UJX4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261819 ; ENSP00000261819 ; ENSG00000089053 . [Q9UJX4-1 ]
ENST00000441917 ; ENSP00000415061 ; ENSG00000089053 . [Q9UJX4-3 ]
GeneIDi 51433.
KEGGi hsa:51433.
UCSCi uc001uag.3. human. [Q9UJX4-1 ]
uc001uah.3. human.

Organism-specific databases

CTDi 51433.
GeneCardsi GC12M121746.
HGNCi HGNC:15713. ANAPC5.
HPAi HPA039457.
MIMi 606948. gene.
neXtProti NX_Q9UJX4.
PharmGKBi PA24788.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG320252.
GeneTreei ENSGT00390000018674.
HOGENOMi HOG000033988.
HOVERGENi HBG001285.
InParanoidi Q9UJX4.
KOi K03352.
OMAi LYWRSSC.
OrthoDBi EOG7T7GSR.
PhylomeDBi Q9UJX4.
TreeFami TF105444.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_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_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.

Miscellaneous databases

ChiTaRSi ANAPC5. human.
GeneWikii ANAPC5.
GenomeRNAii 51433.
NextBioi 55001.
PROi Q9UJX4.
SOURCEi Search...

Gene expression databases

Bgeei Q9UJX4.
CleanExi HS_ANAPC5.
ExpressionAtlasi Q9UJX4. baseline and differential.
Genevestigatori Q9UJX4.

Family and domain databases

Gene3Di 1.25.40.10. 4 hits.
InterProi IPR026000. Apc5/TPR19_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view ]
Pfami PF12862. Apc5. 2 hits.
[Graphical view ]
ProtoNeti Search...

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 3).
    Tissue: Hepatoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Esophagus.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Brain, Cervix and Lung.
  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 SER-195.
  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. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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.
  11. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-617.

Entry informationi

Entry nameiAPC5_HUMAN
AccessioniPrimary (citable) accession number: Q9UJX4
Secondary accession number(s): E9PFB2, Q8N4H7, Q9BQD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: October 29, 2014
This is version 128 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families

External Data

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