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Protein

Cell division cycle-associated protein 2

Gene

CDCA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulator of chromosome structure during mitosis required for condensin-depleted chromosomes to retain their compact architecture through anaphase. Acts by mediating the recruitment of phopsphatase PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the following interphase. At anaphase onset, its association with chromatin targets a pool of PPP1CC to dephosphorylate substrates.2 Publications

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: Ensembl
  • mitotic nuclear division Source: UniProtKB-KW
  • positive regulation of protein dephosphorylation Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division cycle-associated protein 2
Alternative name(s):
Recruits PP1 onto mitotic chromatin at anaphase protein
Short name:
Repo-Man
Gene namesi
Name:CDCA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:14623. CDCA2.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Excluded from the nucleolus. Present in nucleoplasm throughout the G1, S and G2 stages of the cell cycle. During M phase, it becomes diffuse throughout the cell as the nuclear membrane breaks down, and faintly accumulates later on metaphase chromatin. As the cell progresses to anaphase, it accumulates on chromatin.

GO - Cellular componenti

  • chromosome Source: MGI
  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi393 – 3953VTF → ATA: Abolishes interaction with PPP1CC but not subcellular location. 1 Publication

Organism-specific databases

PharmGKBiPA26275.

Polymorphism and mutation databases

BioMutaiCDCA2.
DMDMi308153420.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10231023Cell division cycle-associated protein 2PRO_0000287695Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981PhosphoserineCombined sources
Modified residuei120 – 1201PhosphoserineCombined sources
Modified residuei126 – 1261PhosphoserineCombined sources
Modified residuei131 – 1311PhosphoserineCombined sources
Modified residuei210 – 2101PhosphoserineCombined sources
Modified residuei291 – 2911PhosphoserineCombined sources
Modified residuei309 – 3091PhosphoserineCombined sources
Modified residuei312 – 3121PhosphothreonineCombined sources
Modified residuei400 – 4001PhosphoserineCombined sources
Modified residuei407 – 4071PhosphoserineCombined sources
Modified residuei412 – 4121PhosphothreonineCombined sources
Modified residuei437 – 4371PhosphoserineCombined sources
Modified residuei591 – 5911PhosphoserineCombined sources
Modified residuei614 – 6141PhosphoserineCombined sources
Modified residuei710 – 7101Phosphoserine; in variant Ile-717Combined sources
Modified residuei756 – 7561PhosphoserineCombined sources
Modified residuei936 – 9361PhosphoserineCombined sources
Modified residuei977 – 9771PhosphoserineCombined sources
Modified residuei1000 – 10001PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CDK1. May regulate its subcellular location.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ69YH5.
MaxQBiQ69YH5.
PaxDbiQ69YH5.
PeptideAtlasiQ69YH5.
PRIDEiQ69YH5.

PTM databases

iPTMnetiQ69YH5.
PhosphoSiteiQ69YH5.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ69YH5.
CleanExiHS_CDCA2.
ExpressionAtlasiQ69YH5. baseline and differential.
GenevisibleiQ69YH5. HS.

Organism-specific databases

HPAiHPA026293.
HPA030049.

Interactioni

Subunit structurei

Interacts with PPP1CC.1 Publication

Protein-protein interaction databases

BioGridi127593. 23 interactions.
IntActiQ69YH5. 9 interactions.
MINTiMINT-4994212.
STRINGi9606.ENSP00000328228.

Structurei

3D structure databases

ProteinModelPortaliQ69YH5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi392 – 3954PP1-binding motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi533 – 57543Lys-richAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IU6S. Eukaryota.
ENOG410YZZ3. LUCA.
GeneTreeiENSGT00390000013098.
HOGENOMiHOG000111496.
HOVERGENiHBG107632.
InParanoidiQ69YH5.
KOiK17590.
OMAiQSAFHSI.
OrthoDBiEOG76QFGJ.
PhylomeDBiQ69YH5.
TreeFamiTF336000.

Family and domain databases

InterProiIPR033064. CDCA2.
IPR029334. PP1-bd.
[Graphical view]
PANTHERiPTHR21603:SF16. PTHR21603:SF16. 1 hit.
PfamiPF15276. PP1_bind. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q69YH5-1) [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
MDANSKDKPP ETKESAMNNA GNASFILGTG KIVTPQKHAE LPPNPCTPDT
60 70 80 90 100
FKSPLNFSTV TVEQLGITPE SFVRNSAGKS SSYLKKCRRR SAVGARGSPE
110 120 130 140 150
TNHLIRFIAR QQNIKNARKS PLAQDSPSQG SPALYRNVNT LRERISAFQS
160 170 180 190 200
AFHSIKENEK MTGCLEFSEA GKESEMTDLT RKEGLSACQQ SGFPAVLSSK
210 220 230 240 250
RRRISYQRDS DENLTDAEGK VIGLQIFNID TDRACAVETS VDLSEISSKL
260 270 280 290 300
GSTQSGFLVE ESLPLSELTE TSNALKVADC VVGKGSSDAV SPDTFTAEVS
310 320 330 340 350
SDAVPDVRSP ATPACRRDLP TPKTFVLRSV LKKPSVKMCL ESLQEHCNNL
360 370 380 390 400
YDDDGTHPSL ISNLPNCCKE KEAEDEENFE APAFLNMRKR KRVTFGEDLS
410 420 430 440 450
PEVFDESLPA NTPLRKGGTP VCKKDFSGLS SLLLEQSPVP EPLPQPDFDD
460 470 480 490 500
KGENLENIEP LQVSFAVLSS PNKSSISETL SGTDTFSSSN NHEKISSPKV
510 520 530 540 550
GRITRTSNRR NQLVSVVEES VCNLLNTEVQ PCKEKKINRR KSQETKCTKR
560 570 580 590 600
ALPKKSQVLK SCRKKKGKGK KSVQKSLYGE RDIASKKPLL SPIPELPEVP
610 620 630 640 650
EMTPSIPSIR RLGSGYFSSN GKLEEVKTPK NPVKRKDLLR HDPDLHMHQG
660 670 680 690 700
YDKYDVSEFC SYIKSSSSLG NATSDEDPNT NIMNINENKN IPKAKNKSES
710 720 730 740 750
ENEPKAGTDS PVSCASVTEE RVASDSPKPA LTLQQGQEFS AGGQNAENLC
760 770 780 790 800
QFFKISPDLN IKCERKDDFL GAAEGKLQCN RLMPNSQKDC HCLGDVLIEN
810 820 830 840 850
TKESKSQSED LGRKPMESSS VVSCRDRKDR RRSMCYSDGR SLHLEKNGNH
860 870 880 890 900
TPSSSVGSSV EISLENSELF KDLSDAIEQT FQRRNSETKV RRSTRLQKDL
910 920 930 940 950
ENEGLVWISL PLPSTSQKAK RRTICTFDSS GFESMSPIKE TVSSRQKPQM
960 970 980 990 1000
APPVSDPENS QGPAAGSSDE PGKRRKSFCI STLANTKATS QFKGYRRRSS
1010 1020
LNGKGESSLT ALERIEHNGE RKQ
Length:1,023
Mass (Da):112,676
Last modified:October 5, 2010 - v2
Checksum:i2A073D6DD928B1E5
GO
Isoform 2 (identifier: Q69YH5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-68: T → N
     69-1023: Missing.

Note: No experimental confirmation available.
Show »
Length:68
Mass (Da):7,241
Checksum:i93DB1640A846E0C2
GO

Sequence cautioni

The sequence AAH36214.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC05374.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAH10577.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti662 – 6621Y → D in BG354575 (PubMed:12188893).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti717 – 7171V → I.Combined sources3 Publications
Corresponds to variant rs4872318 [ dbSNP | Ensembl ].
VAR_032350
Natural varianti884 – 8841R → S.1 Publication
Corresponds to variant rs3829009 [ dbSNP | Ensembl ].
VAR_032351

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei68 – 681T → N in isoform 2. 1 PublicationVSP_025598
Alternative sequencei69 – 1023955Missing in isoform 2. 1 PublicationVSP_025599Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL833396 mRNA. Translation: CAH10585.1.
AL833627 mRNA. Translation: CAH10577.1. Sequence problems.
AC103779 Genomic DNA. No translation available.
BC036214 mRNA. Translation: AAH36214.1. Different initiation.
BC063651 mRNA. Translation: AAH63651.1.
BC085609 mRNA. Translation: AAH85609.1.
BC104451 mRNA. Translation: AAI04452.1.
BC104450 mRNA. Translation: AAI04451.1.
BG354575 mRNA. No translation available.
AK098670 mRNA. Translation: BAC05374.1. Different initiation.
CCDSiCCDS6049.1. [Q69YH5-1]
RefSeqiNP_001304835.1. NM_001317906.1.
NP_001304836.1. NM_001317907.1.
NP_689775.2. NM_152562.3. [Q69YH5-1]
UniGeneiHs.33366.

Genome annotation databases

EnsembliENST00000330560; ENSP00000328228; ENSG00000184661. [Q69YH5-1]
GeneIDi157313.
KEGGihsa:157313.
UCSCiuc003xep.2. human. [Q69YH5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL833396 mRNA. Translation: CAH10585.1.
AL833627 mRNA. Translation: CAH10577.1. Sequence problems.
AC103779 Genomic DNA. No translation available.
BC036214 mRNA. Translation: AAH36214.1. Different initiation.
BC063651 mRNA. Translation: AAH63651.1.
BC085609 mRNA. Translation: AAH85609.1.
BC104451 mRNA. Translation: AAI04452.1.
BC104450 mRNA. Translation: AAI04451.1.
BG354575 mRNA. No translation available.
AK098670 mRNA. Translation: BAC05374.1. Different initiation.
CCDSiCCDS6049.1. [Q69YH5-1]
RefSeqiNP_001304835.1. NM_001317906.1.
NP_001304836.1. NM_001317907.1.
NP_689775.2. NM_152562.3. [Q69YH5-1]
UniGeneiHs.33366.

3D structure databases

ProteinModelPortaliQ69YH5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127593. 23 interactions.
IntActiQ69YH5. 9 interactions.
MINTiMINT-4994212.
STRINGi9606.ENSP00000328228.

PTM databases

iPTMnetiQ69YH5.
PhosphoSiteiQ69YH5.

Polymorphism and mutation databases

BioMutaiCDCA2.
DMDMi308153420.

Proteomic databases

EPDiQ69YH5.
MaxQBiQ69YH5.
PaxDbiQ69YH5.
PeptideAtlasiQ69YH5.
PRIDEiQ69YH5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330560; ENSP00000328228; ENSG00000184661. [Q69YH5-1]
GeneIDi157313.
KEGGihsa:157313.
UCSCiuc003xep.2. human. [Q69YH5-1]

Organism-specific databases

CTDi157313.
GeneCardsiCDCA2.
H-InvDBHIX0021732.
HGNCiHGNC:14623. CDCA2.
HPAiHPA026293.
HPA030049.
neXtProtiNX_Q69YH5.
PharmGKBiPA26275.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IU6S. Eukaryota.
ENOG410YZZ3. LUCA.
GeneTreeiENSGT00390000013098.
HOGENOMiHOG000111496.
HOVERGENiHBG107632.
InParanoidiQ69YH5.
KOiK17590.
OMAiQSAFHSI.
OrthoDBiEOG76QFGJ.
PhylomeDBiQ69YH5.
TreeFamiTF336000.

Miscellaneous databases

GenomeRNAii157313.
PROiQ69YH5.

Gene expression databases

BgeeiQ69YH5.
CleanExiHS_CDCA2.
ExpressionAtlasiQ69YH5. baseline and differential.
GenevisibleiQ69YH5. HS.

Family and domain databases

InterProiIPR033064. CDCA2.
IPR029334. PP1-bd.
[Graphical view]
PANTHERiPTHR21603:SF16. PTHR21603:SF16. 1 hit.
PfamiPF15276. PP1_bind. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-717.
    Tissue: Endometrial tumor and Melanoma.
  2. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-1023 (ISOFORM 1), VARIANTS ILE-717 AND SER-884.
    Tissue: Chondrosarcoma, Skin and Testis.
  4. "Drug target discovery by gene expression analysis: cell cycle genes."
    Walker M.G.
    Curr. Cancer Drug Targets 1:73-83(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 559-1023 (ISOFORM 1), VARIANT ILE-717.
  5. "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] OF 561-1023 (ISOFORM 1).
    Tissue: Testis.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Repo-Man recruits PP1 gamma to chromatin and is essential for cell viability."
    Trinkle-Mulcahy L., Andersen J., Lam Y.W., Moorhead G., Mann M., Lamond A.I.
    J. Cell Biol. 172:679-692(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PPP1CC, MUTAGENESIS OF 393-VAL--PHE-395.
  8. "Condensin and Repo-Man-PP1 co-operate in the regulation of chromosome architecture during mitosis."
    Vagnarelli P., Hudson D.F., Ribeiro S.A., Trinkle-Mulcahy L., Spence J.M., Lai F., Farr C.J., Lamond A.I., Earnshaw W.C.
    Nat. Cell Biol. 8:1133-1142(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-126; SER-131; SER-291; SER-309; THR-312; SER-400; SER-407; THR-412; SER-591 AND SER-756, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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 SER-400 AND THR-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-98; SER-400; SER-437 AND SER-591, VARIANT [LARGE SCALE ANALYSIS] ILE-717, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-936 AND SER-977, VARIANT [LARGE SCALE ANALYSIS] ILE-717, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-120; SER-210; SER-400; SER-614; SER-936; SER-977 AND SER-1000, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710 (VARIANT ILE-717), VARIANT [LARGE SCALE ANALYSIS] ILE-717, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiCDCA2_HUMAN
AccessioniPrimary (citable) accession number: Q69YH5
Secondary accession number(s): Q3SX74
, Q4G0W0, Q5RKN0, Q69YI4, Q6P464, Q8N7C1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 5, 2010
Last modified: July 6, 2016
This is version 98 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 8
    Human chromosome 8: 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

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.