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Protein

Cell division cycle protein 27 homolog

Gene

CDC27

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

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 - Molecular functioni

  • protein phosphatase binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division cycle protein 27 homolog
Alternative name(s):
Anaphase-promoting complex subunit 3
Short name:
APC3
CDC27 homolog
Short name:
CDC27Hs
H-NUC
Gene namesi
Name:CDC27
Synonyms:ANAPC3, D0S1430E, D17S978E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:1728. CDC27.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • centrosome Source: MGI
  • cytoplasm Source: LIFEdb
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
  • nucleus Source: BHF-UCL
  • spindle Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi821 – 8211S → A: Abolishes binding to MCPH1. 1 Publication

Organism-specific databases

PharmGKBiPA26261.

Polymorphism and mutation databases

BioMutaiCDC27.
DMDMi12644198.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 824824Cell division cycle protein 27 homologPRO_0000106273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei205 – 2051Phosphothreonine2 Publications
Modified residuei209 – 2091Phosphothreonine1 Publication
Modified residuei244 – 2441Phosphothreonine1 Publication
Modified residuei291 – 2911Phosphoserine1 Publication
Modified residuei313 – 3131Phosphothreonine1 Publication
Modified residuei339 – 3391Phosphoserine1 Publication
Modified residuei366 – 3661Phosphothreonine1 Publication
Modified residuei386 – 3861Phosphoserine1 Publication
Modified residuei426 – 4261Phosphoserine2 Publications
Modified residuei430 – 4301Phosphothreonine1 Publication
Modified residuei435 – 4351Phosphoserine1 Publication
Modified residuei438 – 4381Phosphoserine1 Publication
Modified residuei446 – 4461Phosphothreonine2 Publications
Modified residuei821 – 8211Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated. Phosphorylation on Ser-426 and Thr-446 occurs specifically during mitosis.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP30260.
PaxDbiP30260.
PRIDEiP30260.

PTM databases

PhosphoSiteiP30260.

Expressioni

Gene expression databases

BgeeiP30260.
CleanExiHS_CDC27.
ExpressionAtlasiP30260. baseline and differential.
GenevisibleiP30260. HS.

Organism-specific databases

HPAiCAB004357.
CAB016315.
HPA028129.
HPA052399.

Interactioni

Subunit structurei

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. Interacts with RB. Interacts with FAM168B/MANI (By similarity). Interacts with MCPH1.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC20Q128347EBI-994813,EBI-367462
CDH1P128302EBI-994813,EBI-727477
COMTP21964-23EBI-994813,EBI-10200977
FBXO5Q9UKT42EBI-994813,EBI-852298
FZR1Q9UM118EBI-994813,EBI-724997
MAD2L2Q9UI952EBI-994813,EBI-77889
NCK1P163333EBI-994813,EBI-389883
NEK2P519552EBI-994813,EBI-633182
PTENP604847EBI-994813,EBI-696162

Protein-protein interaction databases

BioGridi107431. 100 interactions.
DIPiDIP-36422N.
IntActiP30260. 45 interactions.
MINTiMINT-86425.
STRINGi9606.ENSP00000434614.

Structurei

Secondary structure

1
824
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 1710Combined sources
Helixi21 – 3414Combined sources
Helixi38 – 5013Combined sources
Helixi54 – 6310Combined sources
Helixi69 – 8113Combined sources
Helixi85 – 939Combined sources
Beta strandi96 – 983Combined sources
Helixi103 – 1108Combined sources
Helixi111 – 1133Combined sources
Helixi114 – 12714Combined sources
Helixi131 – 14414Combined sources
Helixi149 – 15810Combined sources
Helixi164 – 1674Combined sources
Helixi457 – 47721Combined sources
Helixi481 – 4899Combined sources
Helixi493 – 4975Combined sources
Helixi499 – 51214Combined sources
Helixi515 – 52814Combined sources
Helixi536 – 54611Combined sources
Helixi549 – 56214Combined sources
Helixi567 – 57913Combined sources
Helixi583 – 59614Combined sources
Helixi601 – 61313Combined sources
Helixi617 – 63014Combined sources
Helixi635 – 64814Combined sources
Helixi651 – 66414Combined sources
Helixi668 – 68114Combined sources
Helixi693 – 6986Combined sources
Turni699 – 7013Combined sources
Helixi703 – 71513Combined sources
Helixi719 – 73214Combined sources
Helixi737 – 74812Combined sources
Helixi754 – 76613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T1NX-ray2.60C/D821-824[»]
4RG6X-ray3.30A/B1-824[»]
4RG7X-ray4.25A/B1-824[»]
4RG9X-ray3.25A/B1-824[»]
ProteinModelPortaliP30260.
SMRiP30260. Positions 5-171, 448-768.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati6 – 3530TPR 1Add
BLAST
Repeati38 – 6528TPR 2Add
BLAST
Repeati67 – 9933TPR 3Add
BLAST
Repeati115 – 14531TPR 4Add
BLAST
Repeati465 – 49531TPR 5Add
BLAST
Repeati499 – 52830TPR 6Add
BLAST
Repeati533 – 56331TPR 7Add
BLAST
Repeati567 – 59832TPR 8Add
BLAST
Repeati601 – 63131TPR 9Add
BLAST
Repeati635 – 66733TPR 10Add
BLAST
Repeati670 – 70233TPR 11Add
BLAST
Repeati704 – 73431TPR 12Add
BLAST
Repeati737 – 76832TPR 13Add
BLAST

Sequence similaritiesi

Belongs to the APC3/CDC27 family.Curated
Contains 13 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00550000074887.
HOGENOMiHOG000231056.
HOVERGENiHBG050859.
InParanoidiP30260.
KOiK03350.
OMAiNSCTTQV.
OrthoDBiEOG751NDX.
PhylomeDBiP30260.
TreeFamiTF101058.

Family and domain databases

InterProiIPR013026. TPR-contain_dom.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 4 hits.
PF07719. TPR_2. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
PROSITEiPS50005. TPR. 8 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P30260-1) [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
MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR
60 70 80 90 100
SGKAYKAYRL LKGHSCTTPQ CKYLLAKCCV DLSKLAEGEQ ILSGGVFNKQ
110 120 130 140 150
KSHDDIVTEF GDSACFTLSL LGHVYCKTDR LAKGSECYQK SLSLNPFLWS
160 170 180 190 200
PFESLCEIGE KPDPDQTFKF TSLQNFSNCL PNSCTTQVPN HSLSHRQPET
210 220 230 240 250
VLTETPQDTI ELNRLNLESS NSKYSLNTDS SVSYIDSAVI SPDTVPLGTG
260 270 280 290 300
TSILSKQVQN KPKTGRSLLG GPAALSPLTP SFGILPLETP SPGDGSYLQN
310 320 330 340 350
YTNTPPVIDV PSTGAPSKKS VARIGQTGTK SVFSQSGNSR EVTPILAQTQ
360 370 380 390 400
SSGPQTSTTP QVLSPTITSP PNALPRRSSR LFTSDSSTTK ENSKKLKMKF
410 420 430 440 450
PPKIPNRKTK SKTNKGGITQ PNINDSLEIT KLDSSIISEG KISTITPQIQ
460 470 480 490 500
AFNLQKAAAE GLMSLLREMG KGYLALCSYN CKEAINILSH LPSHHYNTGW
510 520 530 540 550
VLCQIGRAYF ELSEYMQAER IFSEVRRIEN YRVEGMEIYS TTLWHLQKDV
560 570 580 590 600
ALSVLSKDLT DMDKNSPEAW CAAGNCFSLQ REHDIAIKFF QRAIQVDPNY
610 620 630 640 650
AYAYTLLGHE FVLTEELDKA LACFRNAIRV NPRHYNAWYG LGMIYYKQEK
660 670 680 690 700
FSLAEMHFQK ALDINPQSSV LLCHIGVVQH ALKKSEKALD TLNKAIVIDP
710 720 730 740 750
KNPLCKFHRA SVLFANEKYK SALQELEELK QIVPKESLVY FLIGKVYKKL
760 770 780 790 800
GQTHLALMNF SWAMDLDPKG ANNQIKEAID KRYLPDDEEP ITQEEQIMGT
810 820
DESQESSMTD ADDTQLHAAE SDEF
Length:824
Mass (Da):91,867
Last modified:December 1, 2000 - v2
Checksum:iE6C8F59C1EF1DCBA
GO
Isoform 2 (identifier: P30260-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     319-319: K → KTFRVLQ

Note: No experimental confirmation available. May be due to competing acceptor splice site.
Show »
Length:830
Mass (Da):92,612
Checksum:i00CE7174F8165CA1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti403 – 4031K → E in AAH11656 (PubMed:15489334).Curated
Sequence conflicti460 – 4601Missing in AAA60471 (PubMed:8234252).Curated
Sequence conflicti715 – 7151A → R in AAA60471 (PubMed:8234252).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti270 – 2701G → A in a breast cancer sample; somatic mutation. 1 Publication
VAR_035861
Natural varianti320 – 3201S → P.
Corresponds to variant rs3208653 [ dbSNP | Ensembl ].
VAR_052613
Natural varianti496 – 4961Y → H.
Corresponds to variant rs13666 [ dbSNP | Ensembl ].
VAR_014489

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei319 – 3191K → KTFRVLQ in isoform 2. 1 PublicationVSP_047225

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00001 mRNA. Translation: AAA60471.1.
S78234 mRNA. Translation: AAB34378.1.
AY518321 Genomic DNA. Translation: AAR89911.1.
AC002558 Genomic DNA. No translation available.
CH471231 Genomic DNA. Translation: EAW57687.1.
BC011656 mRNA. Translation: AAH11656.1.
CCDSiCCDS11509.1. [P30260-1]
CCDS45720.1. [P30260-2]
PIRiI52835.
RefSeqiNP_001107563.1. NM_001114091.2. [P30260-2]
NP_001247.3. NM_001256.4. [P30260-1]
NP_001280018.1. NM_001293089.1.
UniGeneiHs.463295.
Hs.602766.

Genome annotation databases

EnsembliENST00000066544; ENSP00000066544; ENSG00000004897.
ENST00000531206; ENSP00000434614; ENSG00000004897. [P30260-2]
GeneIDi996.
KEGGihsa:996.
UCSCiuc002ild.4. human. [P30260-1]
uc002ile.4. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00001 mRNA. Translation: AAA60471.1.
S78234 mRNA. Translation: AAB34378.1.
AY518321 Genomic DNA. Translation: AAR89911.1.
AC002558 Genomic DNA. No translation available.
CH471231 Genomic DNA. Translation: EAW57687.1.
BC011656 mRNA. Translation: AAH11656.1.
CCDSiCCDS11509.1. [P30260-1]
CCDS45720.1. [P30260-2]
PIRiI52835.
RefSeqiNP_001107563.1. NM_001114091.2. [P30260-2]
NP_001247.3. NM_001256.4. [P30260-1]
NP_001280018.1. NM_001293089.1.
UniGeneiHs.463295.
Hs.602766.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T1NX-ray2.60C/D821-824[»]
4RG6X-ray3.30A/B1-824[»]
4RG7X-ray4.25A/B1-824[»]
4RG9X-ray3.25A/B1-824[»]
ProteinModelPortaliP30260.
SMRiP30260. Positions 5-171, 448-768.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107431. 100 interactions.
DIPiDIP-36422N.
IntActiP30260. 45 interactions.
MINTiMINT-86425.
STRINGi9606.ENSP00000434614.

PTM databases

PhosphoSiteiP30260.

Polymorphism and mutation databases

BioMutaiCDC27.
DMDMi12644198.

Proteomic databases

MaxQBiP30260.
PaxDbiP30260.
PRIDEiP30260.

Protocols and materials databases

DNASUi996.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000066544; ENSP00000066544; ENSG00000004897.
ENST00000531206; ENSP00000434614; ENSG00000004897. [P30260-2]
GeneIDi996.
KEGGihsa:996.
UCSCiuc002ild.4. human. [P30260-1]
uc002ile.4. human.

Organism-specific databases

CTDi996.
GeneCardsiGC17M045195.
H-InvDBHIX0176461.
HGNCiHGNC:1728. CDC27.
HPAiCAB004357.
CAB016315.
HPA028129.
HPA052399.
MIMi116946. gene.
neXtProtiNX_P30260.
PharmGKBiPA26261.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00550000074887.
HOGENOMiHOG000231056.
HOVERGENiHBG050859.
InParanoidiP30260.
KOiK03350.
OMAiNSCTTQV.
OrthoDBiEOG751NDX.
PhylomeDBiP30260.
TreeFamiTF101058.

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.

Miscellaneous databases

ChiTaRSiCDC27. human.
GeneWikiiCDC27.
GenomeRNAii996.
NextBioi4184.
PROiP30260.
SOURCEiSearch...

Gene expression databases

BgeeiP30260.
CleanExiHS_CDC27.
ExpressionAtlasiP30260. baseline and differential.
GenevisibleiP30260. HS.

Family and domain databases

InterProiIPR013026. TPR-contain_dom.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 4 hits.
PF07719. TPR_2. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
PROSITEiPS50005. TPR. 8 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Linking yeast genetics to mammalian genomes: identification and mapping of the human homolog of CDC27 via the expressed sequence tag (EST) data base."
    Tugendreich S., Boguski M.S., Seldin M., Hieter P.A.
    Proc. Natl. Acad. Sci. U.S.A. 90:10031-10035(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Identification of a human homologue of yeast nuc2 which interacts with the retinoblastoma protein in a specific manner."
    Chen P.L., Ueng Y.C., Durfee T., Chen K.C., Yang-Feng T., Lee W.H.
    Cell Growth Differ. 6:199-210(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. NIEHS SNPs program
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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).
    Tissue: Uterus.
  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 THR-205; THR-209; THR-244; SER-291; THR-313; SER-426; THR-430; SER-435 AND THR-446.
  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: 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; SER-339; SER-426; SER-438 AND THR-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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].
  12. "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 THR-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Structural basis for the subunit assembly of the anaphase-promoting complex."
    Schreiber A., Stengel F., Zhang Z., Enchev R.I., Kong E.H., Morris E.P., Robinson C.V., da Fonseca P.C., Barford D.
    Nature 470:227-232(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TPR REPEATS.
  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 basis for the association of microcephalin (MCPH1) protein with the cell division cycle protein 27 (Cdc27) subunit of the anaphase-promoting complex."
    Singh N., Wiltshire T.D., Thompson J.R., Mer G., Couch F.J.
    J. Biol. Chem. 287:2854-2862(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 821-824 IN COMPLEX WITH MCPH1, PHOSPHORYLATION AT SER-821, MUTAGENESIS OF SER-821.
  18. "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.
  19. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-270.

Entry informationi

Entry nameiCDC27_HUMAN
AccessioniPrimary (citable) accession number: P30260
Secondary accession number(s): G3V1C4, Q16349, Q96F35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 1, 2000
Last modified: July 22, 2015
This is version 163 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.