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Q15021

- CND1_HUMAN

UniProt

Q15021 - CND1_HUMAN

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Protein
Condensin complex subunit 1
Gene
NCAPD2, CAPD2, CNAP1, KIAA0159
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. May target the condensin complex to DNA via its C-terminal domain.1 Publication

GO - Molecular functioni

  1. histone binding Source: UniProtKB
  2. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. mitotic cell cycle Source: Reactome
  2. mitotic chromosome condensation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150260. Condensation of Prometaphase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Condensin complex subunit 1
Alternative name(s):
Chromosome condensation-related SMC-associated protein 1
Chromosome-associated protein D2
Short name:
hCAP-D2
Non-SMC condensin I complex subunit D2
XCAP-D2 homolog
Gene namesi
Name:NCAPD2
Synonyms:CAPD2, CNAP1, KIAA0159
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:24305. NCAPD2.

Subcellular locationi

Nucleus. Cytoplasm. Chromosome
Note: In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.1 Publication

GO - Cellular componenti

  1. condensed chromosome Source: MGI
  2. condensin complex Source: UniProtKB
  3. condensin core heterodimer Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. cytosol Source: Reactome
  6. nucleus Source: UniProtKB
  7. pronucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1343 – 13486RRTTRR → AATTAA: Abolishes localization to the nucleus, while it only reduces chromosome binding. 1 Publication
Mutagenesisi1358 – 13603KKK → AAA: Abolishes localization to the nucleus, while it only reduces chromosome binding. 1 Publication

Organism-specific databases

PharmGKBiPA162397021.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14011401Condensin complex subunit 1
PRO_0000095035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine1 Publication
Modified residuei585 – 5851Phosphoserine1 Publication
Modified residuei1310 – 13101Phosphoserine1 Publication
Modified residuei1330 – 13301Phosphoserine1 Publication
Modified residuei1331 – 13311Phosphothreonine1 Publication
Modified residuei1333 – 13331Phosphoserine4 Publications
Modified residuei1339 – 13391Phosphothreonine6 Publications
Modified residuei1366 – 13661Phosphoserine1 Publication
Modified residuei1367 – 13671Phosphoserine1 Publication
Modified residuei1370 – 13701Phosphoserine1 Publication
Modified residuei1371 – 13711Phosphoserine1 Publication
Modified residuei1376 – 13761Phosphoserine1 Publication
Modified residuei1384 – 13841Phosphothreonine; by CDK1 By similarity
Modified residuei1389 – 13891Phosphothreonine; by CDK1 By similarity

Post-translational modificationi

Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPH and NCAPG subunits, activates the condensin complex and is required for chromosome condensation By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15021.
PaxDbiQ15021.
PRIDEiQ15021.

PTM databases

PhosphoSiteiQ15021.

Expressioni

Gene expression databases

ArrayExpressiQ15021.
BgeeiQ15021.
CleanExiHS_NCAPD2.
GenevestigatoriQ15021.

Organism-specific databases

HPAiCAB012423.
HPA036947.
HPA037363.

Interactioni

Subunit structurei

Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and NCAPG. Interacts with histones H1 and H3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCAPGQ9BPX32EBI-1044041,EBI-970214
NCAPHQ150034EBI-1044041,EBI-1046410

Protein-protein interaction databases

BioGridi115246. 25 interactions.
IntActiQ15021. 7 interactions.
MINTiMINT-3030640.
STRINGi9606.ENSP00000325017.

Structurei

3D structure databases

ProteinModelPortaliQ15021.
SMRiQ15021. Positions 407-434, 1030-1121.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 603603Interactions with SMC2 and SMC4
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1342 – 136221Bipartite nuclear localization signal
Add
BLAST

Domaini

The C-terminal domain interacts with histones H1 and H3, and may be responsible for condensin complex targeting to mitotic chromosomes. This domain is independent from the bipartite nuclear localization signal, although they are contained within the same region.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5098.
HOGENOMiHOG000068001.
HOVERGENiHBG038048.
InParanoidiQ15021.
KOiK06677.
OMAiATEKVAC.
OrthoDBiEOG7FJGZN.
PhylomeDBiQ15021.
TreeFamiTF105712.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026971. CND1/NCAPD3.
IPR007673. Condensin_cplx_su1.
IPR024324. Condensin_cplx_su1_N.
[Graphical view]
PANTHERiPTHR14222. PTHR14222. 1 hit.
PfamiPF12922. Cnd1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF017127. Condensin_D2. 1 hit.
SUPFAMiSSF48371. SSF48371. 4 hits.

Sequencei

Sequence statusi: Complete.

Q15021-1 [UniParc]FASTAAdd to Basket

« Hide

MAPQMYEFHL PLSPEELLKS GGVNQYVVQE VLSIKHLPPQ LRAFQAAFRA     50
QGPLAMLQHF DTIYSILHHF RSIDPGLKED TLQFLIKVVS RHSQELPAIL 100
DDTTLSGSDR NAHLNALKMN CYALIRLLES FETMASQTNL VDLDLGGKGK 150
KARTKAAHGF DWEEERQPIL QLLTQLLQLD IRHLWNHSII EEEFVSLVTG 200
CCYRLLENPT INHQKNRPTR EAITHLLGVA LTRYNHMLSA TVKIIQMLQH 250
FEHLAPVLVA AVSLWATDYG MKSIVGEIVR EIGQKCPQEL SRDPSGTKGF 300
AAFLTELAER VPAILMSSMC ILLDHLDGEN YMMRNAVLAA MAEMVLQVLS 350
GDQLEAAARD TRDQFLDTLQ AHGHDVNSFV RSRVLQLFTR IVQQKALPLT 400
RFQAVVALAV GRLADKSVLV CKNAIQLLAS FLANNPFSCK LSDADLAGPL 450
QKETQKLQEM RAQRRTAAAS AVLDPEEEWE AMLPELKSTL QQLLQLPQGE 500
EEIPEQIANT ETTEDVKGRI YQLLAKASYK KAIILTREAT GHFQESEPFS 550
HIDPEESEET RLLNILGLIF KGPAASTQEK NPRESTGNMV TGQTVCKNKP 600
NMSDPEESRG NDELVKQEML VQYLQDAYSF SRKITEAIGI ISKMMYENTT 650
TVVQEVIEFF VMVFQFGVPQ ALFGVRRMLP LIWSKEPGVR EAVLNAYRQL 700
YLNPKGDSAR AKAQALIQNL SLLLVDASVG TIQCLEEILC EFVQKDELKP 750
AVTQLLWERA TEKVACCPLE RCSSVMLLGM MARGKPEIVG SNLDTLVSIG 800
LDEKFPQDYR LAQQVCHAIA NISDRRKPSL GKRHPPFRLP QEHRLFERLR 850
ETVTKGFVHP DPLWIPFKEV AVTLIYQLAE GPEVICAQIL QGCAKQALEK 900
LEEKRTSQED PKESPAMLPT FLLMNLLSLA GDVALQQLVH LEQAVSGELC 950
RRRVLREEQE HKTKDPKEKN TSSETTMEEE LGLVGATADD TEAELIRGIC 1000
EMELLDGKQT LAAFVPLLLK VCNNPGLYSN PDLSAAASLA LGKFCMISAT 1050
FCDSQLRLLF TMLEKSPLPI VRSNLMVATG DLAIRFPNLV DPWTPHLYAR 1100
LRDPAQQVRK TAGLVMTHLI LKDMVKVKGQ VSEMAVLLID PEPQIAALAK 1150
NFFNELSHKG NAIYNLLPDI ISRLSDPELG VEEEPFHTIM KQLLSYITKD 1200
KQTESLVEKL CQRFRTSRTE RQQRDLAYCV SQLPLTERGL RKMLDNFDCF 1250
GDKLSDESIF SAFLSVVGKL RRGAKPEGKA IIDEFEQKLR ACHTRGLDGI 1300
KELEIGQAGS QRAPSAKKPS TGSRYQPLAS TASDNDFVTP EPRRTTRRHP 1350
NTQQRASKKK PKVVFSSDES SEEDLSAEMT EDETPKKTTP ILRASARRHR 1400
S 1401
Length:1,401
Mass (Da):157,182
Last modified:September 22, 2009 - v3
Checksum:i35E31642B94B513D
GO

Sequence cautioni

The sequence BAA09930.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti83 – 831Q → E.4 Publications
Corresponds to variant rs714774 [ dbSNP | Ensembl ].
VAR_024421
Natural varianti580 – 5801K → R.
Corresponds to variant rs17725914 [ dbSNP | Ensembl ].
VAR_057511
Natural varianti797 – 7971V → M.
Corresponds to variant rs10849482 [ dbSNP | Ensembl ].
VAR_024422
Natural varianti1321 – 13211T → S.1 Publication
Corresponds to variant rs2240871 [ dbSNP | Ensembl ].
VAR_058713

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1062 – 10621M → I in BAA09930. 1 Publication
Sequence conflicti1218 – 12181R → L in BAA09930. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63880 mRNA. Translation: BAA09930.2. Different initiation.
AC006064 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88788.1.
CH471116 Genomic DNA. Translation: EAW88789.1.
BC028182 mRNA. Translation: AAH28182.1.
CCDSiCCDS8548.1.
RefSeqiNP_055680.3. NM_014865.3.
UniGeneiHs.5719.

Genome annotation databases

EnsembliENST00000315579; ENSP00000325017; ENSG00000010292.
GeneIDi9918.
KEGGihsa:9918.
UCSCiuc001qoo.2. human.

Polymorphism databases

DMDMi259016362.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63880 mRNA. Translation: BAA09930.2 . Different initiation.
AC006064 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88788.1 .
CH471116 Genomic DNA. Translation: EAW88789.1 .
BC028182 mRNA. Translation: AAH28182.1 .
CCDSi CCDS8548.1.
RefSeqi NP_055680.3. NM_014865.3.
UniGenei Hs.5719.

3D structure databases

ProteinModelPortali Q15021.
SMRi Q15021. Positions 407-434, 1030-1121.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115246. 25 interactions.
IntActi Q15021. 7 interactions.
MINTi MINT-3030640.
STRINGi 9606.ENSP00000325017.

PTM databases

PhosphoSitei Q15021.

Polymorphism databases

DMDMi 259016362.

Proteomic databases

MaxQBi Q15021.
PaxDbi Q15021.
PRIDEi Q15021.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315579 ; ENSP00000325017 ; ENSG00000010292 .
GeneIDi 9918.
KEGGi hsa:9918.
UCSCi uc001qoo.2. human.

Organism-specific databases

CTDi 9918.
GeneCardsi GC12P006602.
H-InvDBi HIX0201829.
HGNCi HGNC:24305. NCAPD2.
HPAi CAB012423.
HPA036947.
HPA037363.
MIMi 615638. gene.
neXtProti NX_Q15021.
PharmGKBi PA162397021.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5098.
HOGENOMi HOG000068001.
HOVERGENi HBG038048.
InParanoidi Q15021.
KOi K06677.
OMAi ATEKVAC.
OrthoDBi EOG7FJGZN.
PhylomeDBi Q15021.
TreeFami TF105712.

Enzyme and pathway databases

Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

ChiTaRSi NCAPD2. human.
GeneWikii NCAPD2.
GenomeRNAii 9918.
NextBioi 37412.
PROi Q15021.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15021.
Bgeei Q15021.
CleanExi HS_NCAPD2.
Genevestigatori Q15021.

Family and domain databases

Gene3Di 1.25.10.10. 3 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR026971. CND1/NCAPD3.
IPR007673. Condensin_cplx_su1.
IPR024324. Condensin_cplx_su1_N.
[Graphical view ]
PANTHERi PTHR14222. PTHR14222. 1 hit.
Pfami PF12922. Cnd1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF017127. Condensin_D2. 1 hit.
SUPFAMi SSF48371. SSF48371. 4 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-83.
    Tissue: Bone marrow.
  2. "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].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-83.
  4. "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], VARIANTS GLU-83 AND SER-1321.
    Tissue: Mammary gland.
  5. "A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3 during the early stage of mitotic chromosome condensation."
    Schmiesing J.A., Gregson H.C., Zhou S., Yokomori K.
    Mol. Cell. Biol. 20:6996-7006(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 359-365; 537-560; 698-709 AND 1324-1331, IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2 AND SMC4, SUBCELLULAR LOCATION.
  6. "Chromosome condensation by a human condensin complex in Xenopus egg extracts."
    Kimura K., Cuvier O., Hirano T.
    J. Biol. Chem. 276:5417-5420(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; NCAPH AND NCAPG, FUNCTION OF THE CONDENSIN COMPLEX.
  7. "Identification of a chromosome-targeting domain in the human condensin subunit CNAP1/hCAP-D2/Eg7."
    Ball A.R. Jr., Schmiesing J.A., Zhou C., Gregson H.C., Okada Y., Doi T., Yokomori K.
    Mol. Cell. Biol. 22:5769-5781(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HISTONE H1 AND HISTONE H3, MUTAGENESIS OF 1343-ARG--ARG-1348 AND 1358-LYS--LYS-1360.
  8. "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-1376, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-1339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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 THR-1339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585; SER-1330; THR-1331; SER-1333; THR-1339; SER-1366; SER-1367; SER-1370 AND SER-1371, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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].
  15. "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-1333 AND THR-1339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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-20; SER-1333 AND THR-1339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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-1333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCND1_HUMAN
AccessioniPrimary (citable) accession number: Q15021
Secondary accession number(s): D3DUR4, Q8N6U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: September 22, 2009
Last modified: September 3, 2014
This is version 139 of the entry and version 3 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, Direct protein sequencing, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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