Q13042 (CDC16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell division cycle protein 16 homolog

Alternative name(s):
Anaphase-promoting complex subunit 6
Short name=APC6
CDC16 homolog
Short name=CDC16Hs
Cyclosome subunit 6

Gene names

Name:	CDC16
Synonyms:	ANAPC6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	620 AA.
Sequence status	Complete.
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. Ref.11
Pathway	Protein modification; protein ubiquitination.
Subunit structure	The APC/C is composed of at least 12 subunits. Interacts with PPP5C and CDC20. Ref.7 Ref.8
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
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 Reference proteome
Gene Ontology (GO)
Biological_process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Traceable author statement Ref.1. Source: ProtInc mitosis Traceable author statement Ref.1. Source: ProtInc mitotic spindle assembly checkpoint Traceable author statement. Source: Reactome negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein K11-linked ubiquitination Inferred from direct assay Ref.11. Source: UniProtKB
Cellular_component	anaphase-promoting complex Inferred from direct assay Ref.17PubMed 21926987. Source: UniProtKB centrosome Inferred from direct assay Ref.1. Source: MGI cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome spindle microtubule Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC26	Q8NHZ8	3	EBI-994830,EBI-2555941

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.12 Ref.15

Modified residue

581

1

Phosphothreonine Ref.9 Ref.10 Ref.12 Ref.14 Ref.15

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

Secondary structure

1

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620

Helix Strand Turn

Details...

Helix

234 – 243

10

Helix

247 – 260

14

Turn

265 – 267

3

Helix

268 – 278

11

Helix

281 – 294

14

Helix

300 – 311

12

Helix

316 – 327

12

Helix

335 – 347

13

Helix

350 – 363

14

Turn

364 – 366

3

Helix

369 – 380

12

Helix

384 – 395

12

Helix

402 – 414

13

Helix

418 – 432

15

Turn

433 – 435

3

Turn

440 – 443

4

Helix

446 – 457

12

Helix

461 – 474

14

Helix

480 – 492

13

Helix

495 – 503

9

Turn

504 – 508

5

Helix

513 – 524

12

Turn

525 – 528

4

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 [UniParc]. 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 [UniParc]. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-581, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND THR-581, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"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-581, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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-560 AND THR-581, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE APC/C.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_001078645.1.
NP_003894.3. NM_003903.3.

UniGene

Hs.374127.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q13042.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36423N.

IntAct

Q13042. 37 interactions.

STRING

9606.ENSP00000348554.

PTM databases

PhosphoSite

Q13042.

Polymorphism databases

DMDM

37537763.

Proteomic databases

PaxDb

Q13042.

PRIDE

Q13042.

Protocols and materials databases

DNASU

8881.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000252457; ENSP00000252457; ENSG00000130177.
ENST00000356221; ENSP00000348554; ENSG00000130177.
ENST00000360383; ENSP00000353549; ENSG00000130177.

GeneID

8881.

KEGG

hsa:8881.

UCSC

uc001vuk.1. human.
uc001vun.1. human.
uc001vuo.1. human.

Organism-specific databases

CTD

8881.

GeneCards

GC13P115000.

HGNC

HGNC:1720. CDC16.

HPA

HPA042826.

MIM

603461. gene.

neXtProt

NX_Q13042.

PharmGKB

PA26256.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0457.

HOGENOM

HOG000230908.

HOVERGEN

HBG050857.

InParanoid

Q13042.

KO

K03353.

OMA

HFLFENK.

OrthoDB

EOG4DBTD7.

PhylomeDB

Q13042.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q13042.

Bgee

Q13042.

CleanEx

HS_CDC16.

Genevestigator

Q13042.

GermOnline

ENSG00000130177. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 2 hits.

InterPro

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

Pfam

PF00515. TPR_1. 2 hits.
PF13181. TPR_8. 1 hit.
[Graphical view]

SMART

SM00028. TPR. 4 hits.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other

ChiTaRS

CDC16. human.

EvolutionaryTrace

Q13042.

GenomeRNAi

8881.

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:	May 1, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.