Reviewed, UniProtKB/Swiss-Prot Q13042 (CDC16_HUMAN)

Names and origin

Protein names

Recommended name:
    Cell division cycle protein 16 homolog
Alternative name(s):
    CDC16Hs
    Anaphase-promoting complex subunit 6
      Short name=APC6
    Cyclosome subunit 6

Gene names

Name:	CDC16
Synonyms:	ANAPC6

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	620 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	The APC/C is composed of at least 12 subunits. Interacts with PPP5C and CDC20.
Subcellular location	Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle. Note: Colocalizes with CDC27 to the centrosome at all stages of the cell cycle and to the mitotic spindle. Ref.1
Post-translational modification	Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis. Ref.9 Ref.13 Ref.14 Ref.15 Ref.10 Ref.11
Sequence similarities	Belongs to the APC6/CDC16 family. Contains 7 TPR repeats.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Ubl conjugation pathway
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	Repeat TPR repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Ref.1 Traceable author statement. Source: ProtInc mitosis Ref.1 Traceable author statement. Source: ProtInc negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome protein K11-linked ubiquitination Ref.12 Inferred from direct assay. Source: UniProtKB regulation of mitosis Ref.1 Traceable author statement. Source: ProtInc
Cellular component	anaphase-promoting complex Ref.17 Inferred from direct assay. Source: UniProtKB centrosome Ref.1 Inferred from direct assay. Source: MGI cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome spindle microtubule Ref.1 Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13042-1)

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.

Isoform 2 (identifier: Q13042-2)

The sequence of this isoform differs from the canonical sequence as follows:
     36-36: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q13042-3)

The sequence of this isoform differs from the canonical sequence as follows:
     36-36: Missing.
     367-417: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 620	620	Cell division cycle protein 16 homolog		PRO_0000106267
Regions
	Repeat	130 – 163	34	TPR 1
	Repeat	299 – 333	35	TPR 2
	Repeat	334 – 367	34	TPR 3
	Repeat	368 – 401	34	TPR 4
	Repeat	403 – 435	33	TPR 5
	Repeat	445 – 478	34	TPR 6
	Repeat	479 – 512	34	TPR 7
Amino acid modifications
	Modified residue	112	1	Phosphoserine Ref.9
	Modified residue	490	1	Phosphoserine Ref.9
	Modified residue	560	1	Phosphoserine Ref.9 Ref.13 Ref.14 Ref.15 Ref.10 Ref.11
	Modified residue	581	1	Phosphothreonine Ref.9 Ref.14 Ref.10 Ref.11
	Modified residue	595	1	Phosphoserine Ref.9
	Modified residue	599	1	Phosphothreonine Ref.9
Natural variations
	Alternative sequence	36	1	Missing in isoform 2 and isoform 3.		VSP_008427
	Alternative sequence	367 – 417	51	Missing in isoform 3.		VSP_008428
Experimental info
	Sequence conflict	138	1	K → Q in AAC50200. Ref.1
	Sequence conflict	299	1	P → L in AAD45156. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2003. Version 2. Checksum: A9C4F24615DF17EB	FASTA	620	71,656
	10 20 30 40 50 60 MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREEPQDI YWLAQCLYLT AQYHRAAHAL 70 80 90 100 110 120 RSRKLDKLYE ACRYLAARCH YAAKEHQQAL DVLDMEEPIN KRLFEKYLKD ESGFKDPSSD 130 140 150 160 170 180 WEMSQSSIKS SICLLRGKIY DALDNRTLAT YSYKEALKLD VYCFEAFDLL TSHHMLTAQE 190 200 210 220 230 240 EKELLESLPL SKLCNEEQEL LRFLFENKLK KYNKPSETVI PESVDGLQEN LDVVVSLAER 250 260 270 280 290 300 HYYNCDFKMC YKLTSVVMEK DPFHASCLPV HIGTLVELNK ANELFYLSHK LVDLYPSNPV 310 320 330 340 350 360 SWFAVGCYYL MVGHKNEHAR RYLSKATTLE KTYGPAWIAY GHSFAVESEH DQAMAAYFTA 370 380 390 400 410 420 AQLMKGCHLP MLYIGLEYGL TNNSKLAERF FSQALSIAPE DPFVMHEVGV VAFQNGEWKT 430 440 450 460 470 480 AEKWFLDALE KIKAIGNEVT VDKWEPLLNN LGHVCRKLKK YAEALDYHRQ ALVLIPQNAS 490 500 510 520 530 540 TYSAIGYIHS LMGNFENAVD YFHTALGLRR DDTFSVTMLG HCIEMYIGDS EAYIGADIKD 550 560 570 580 590 600 KLKCYDFDVH TMKTLKNIIS PPWDFREFEV EKQTAEETGL TPLETSRKTP DSRPSLEETF 610 620 EIEMNESDMM LETSMSDHST
	Isoform 2. Checksum: 87D5542D21C14CD6	FASTA	619	71,527
	10 20 30 40 50 60 MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREPQDIY WLAQCLYLTA QYHRAAHALR 70 80 90 100 110 120 SRKLDKLYEA CRYLAARCHY AAKEHQQALD VLDMEEPINK RLFEKYLKDE SGFKDPSSDW 130 140 150 160 170 180 EMSQSSIKSS ICLLRGKIYD ALDNRTLATY SYKEALKLDV YCFEAFDLLT SHHMLTAQEE 190 200 210 220 230 240 KELLESLPLS KLCNEEQELL RFLFENKLKK YNKPSETVIP ESVDGLQENL DVVVSLAERH 250 260 270 280 290 300 YYNCDFKMCY KLTSVVMEKD PFHASCLPVH IGTLVELNKA NELFYLSHKL VDLYPSNPVS 310 320 330 340 350 360 WFAVGCYYLM VGHKNEHARR YLSKATTLEK TYGPAWIAYG HSFAVESEHD QAMAAYFTAA 370 380 390 400 410 420 QLMKGCHLPM LYIGLEYGLT NNSKLAERFF SQALSIAPED PFVMHEVGVV AFQNGEWKTA 430 440 450 460 470 480 EKWFLDALEK IKAIGNEVTV DKWEPLLNNL GHVCRKLKKY AEALDYHRQA LVLIPQNAST 490 500 510 520 530 540 YSAIGYIHSL MGNFENAVDY FHTALGLRRD DTFSVTMLGH CIEMYIGDSE AYIGADIKDK 550 560 570 580 590 600 LKCYDFDVHT MKTLKNIISP PWDFREFEVE KQTAEETGLT PLETSRKTPD SRPSLEETFE 610 IEMNESDMML ETSMSDHST
	Isoform 3. Checksum: 0B5B3A3B468B3109	FASTA	568	65,860
	10 20 30 40 50 60 MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREPQDIY WLAQCLYLTA QYHRAAHALR 70 80 90 100 110 120 SRKLDKLYEA CRYLAARCHY AAKEHQQALD VLDMEEPINK RLFEKYLKDE SGFKDPSSDW 130 140 150 160 170 180 EMSQSSIKSS ICLLRGKIYD ALDNRTLATY SYKEALKLDV YCFEAFDLLT SHHMLTAQEE 190 200 210 220 230 240 KELLESLPLS KLCNEEQELL RFLFENKLKK YNKPSETVIP ESVDGLQENL DVVVSLAERH 250 260 270 280 290 300 YYNCDFKMCY KLTSVVMEKD PFHASCLPVH IGTLVELNKA NELFYLSHKL VDLYPSNPVS 310 320 330 340 350 360 WFAVGCYYLM VGHKNEHARR YLSKATTLEK TYGPAWIAYG HSFAVESEHD QAMAAYFTAA 370 380 390 400 410 420 QLMKGWKTAE KWFLDALEKI KAIGNEVTVD KWEPLLNNLG HVCRKLKKYA EALDYHRQAL 430 440 450 460 470 480 VLIPQNASTY SAIGYIHSLM GNFENAVDYF HTALGLRRDD TFSVTMLGHC IEMYIGDSEA 490 500 510 520 530 540 YIGADIKDKL KCYDFDVHTM KTLKNIISPP WDFREFEVEK QTAEETGLTP LETSRKTPDS 550 560 RPSLEETFEI EMNESDMMLE TSMSDHST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic spindle and is essential for the metaphase to anaphase transition." Tugendreich S., Tomkiel J., Earnshaw W., Hieter P. Cell 81:261-268(1995) [PubMed: 7736578] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION. Tissue: Brain.
[2]	"The differential splicing variants of human CDC16 mRNA." Zhou P.K., Rigaud O. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 3).
[3]	NIEHS SNPs program Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[7]	"The serine/threonine phosphatase PP5 interacts with CDC16 and CDC27, two tetratricopeptide repeat-containing subunits of the anaphase-promoting complex." Ollendorff V., Donoghue D.J. J. Biol. Chem. 272:32011-32018(1997) [PubMed: 9405394] [Abstract] Cited for: INTERACTION WITH PPP5C.
[8]	"Mammalian p55CDC mediates association of the spindle checkpoint protein Mad2 with the cyclosome/anaphase-promoting complex, and is involved in regulating anaphase onset and late mitotic events." Kallio M., Weinstein J., Daum J.R., Burke D.J., Gorbsky G.J. J. Cell Biol. 141:1393-1406(1998) [PubMed: 9628895] [Abstract] Cited for: INTERACTION WITH CDC20.
[9]	"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: 14657031] [Abstract] Cited for: PHOSPHORYLATION AT SER-112; SER-490; SER-560; THR-581; SER-595 AND THR-599.
[10]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND THR-581, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND THR-581, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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: 18485873] [Abstract] Cited for: FUNCTION OF THE APC/C.
[13]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, MASS SPECTROMETRY.
[14]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND THR-581, MASS SPECTROMETRY.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, MASS SPECTROMETRY.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-581, MASS SPECTROMETRY. Tissue: T-cell.
[17]	"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: 16364912] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE APC/C.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

U18291 mRNA. Translation: AAC50200.1.
AF164598 mRNA. Translation: AAD45156.1.
AY599074 Genomic DNA. Translation: AAS94323.1.
AL160396 Genomic DNA. Translation: CAI15810.1.
AL160396 Genomic DNA. Translation: CAM22287.1.
CH471085 Genomic DNA. Translation: EAX09237.1.
CH471085 Genomic DNA. Translation: EAX09244.1.
BC017244 mRNA. Translation: AAH17244.1.

IPI

IPI00022091.
IPI00376312.
IPI00376313.

PIR

A56519.

RefSeq

NP_001072113.1.
NP_003894.3.

UniGene

Hs.374127

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HYM	X-ray	2.80	B/D/F/H/J/L	212-539	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q13042.

PTM databases

PhosphoSite

Q13042.

Proteomic databases

PRIDE

Q13042.

Genome annotation databases

Ensembl

ENST00000356221; ENSP00000348554; ENSG00000130177; Homo sapiens. [Genome view]
ENST00000360383; ENSP00000353549; ENSG00000130177; Homo sapiens. [Genome view]

GeneID

8881.

KEGG

hsa:8881.

UCSC

uc001vuk.1. human.

Organism-specific databases

CTD

8881.

GeneCards

GC13P114018.

H-InvDB

HIX0011483.

HGNC

HGNC:1720. CDC16.

MIM

603461. gene.

PharmGKB

PA142672176.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG559313.

HOVERGEN

Q13042.

InParanoid

Q13042.

OMA

HFLFENK.

OrthoDB

EOG922D52.

Enzyme and pathway databases

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.
REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.

Gene expression databases

ArrayExpress

Q13042.

Bgee

Q13042.

CleanEx

HS_CDC16.

Genevestigator

Q13042.

GermOnline

ENSG00000130177. Homo sapiens.

Family and domain databases

InterPro

IPR001440. TPR-1.
IPR011990. TPR-like_helical.
IPR013026. TPR_region.
IPR019734. TPR_repeat.
[Graphical view]

Gene3D

G3DSA:1.25.40.10. TPR-like_helical. 1 hit.

Pfam

PF00515. TPR_1. 4 hits.
[Graphical view]

SMART

SM00028. TPR. 4 hits.
[Graphical view]

PROSITE

PS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

33347.

SOURCE

Search...

Entry information

Entry name

CDC16_HUMAN

Accession

Primary (citable) accession number: Q13042
Secondary accession number(s): A2A365 , Q5T8C8, Q96AE6, Q9Y564

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	October 3, 2003
Last modified:	December 15, 2009
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.