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Q15021

- CND1_HUMAN

UniProt

Q15021 - CND1_HUMAN

Protein

Condensin complex subunit 1

Gene

NCAPD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 3 (22 Sep 2009)
      Previous versions | rss
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    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

    GO - Biological processi

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

    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 1 Publication. Cytoplasm 1 Publication. Chromosome 1 Publication
    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.

    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. membrane Source: UniProtKB
    7. nucleus Source: UniProtKB
    8. pronucleus Source: Ensembl

    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 1PRO_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 CDK1By similarity
    Modified residuei1389 – 13891Phosphothreonine; by CDK1By 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.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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 603603Interactions with SMC2 and SMC4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1342 – 136221Bipartite nuclear localization signalAdd
    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

    Belongs to the CND1 (condensin subunit 1) family.Curated

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1062 – 10621M → I in BAA09930. (PubMed:8590280)Curated
    Sequence conflicti1218 – 12181R → L in BAA09930. (PubMed:8590280)Curated

    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 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...
    MobiDBi 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-InvDB 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

    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: October 1, 2014
    This is version 140 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