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Q9BPX3

- CND3_HUMAN

UniProt

Q9BPX3 - CND3_HUMAN

Protein

Condensin complex subunit 3

Gene

NCAPG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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.1 Publication

    GO - Molecular functioni

    1. 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 3
    Alternative name(s):
    Chromosome-associated protein G
    Condensin subunit CAP-G
    Short name:
    hCAP-G
    Melanoma antigen NY-MEL-3
    Non-SMC condensin I complex subunit G
    XCAP-G homolog
    Gene namesi
    Name:NCAPG
    Synonyms:CAPG, NYMEL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:24304. NCAPG.

    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.

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. centrosome Source: HPA
    3. condensin complex Source: UniProtKB
    4. cytoplasm Source: HPA
    5. cytosol Source: Reactome
    6. membrane Source: UniProtKB
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162397165.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10151015Condensin complex subunit 3PRO_0000095041Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei390 – 3901Phosphoserine2 Publications
    Modified residuei674 – 6741Phosphoserine6 Publications
    Modified residuei931 – 9311Phosphothreonine1 Publication
    Modified residuei973 – 9731Phosphoserine1 Publication
    Modified residuei975 – 9751Phosphoserine1 Publication
    Modified residuei1002 – 10021Phosphoserine1 Publication
    Modified residuei1015 – 10151Phosphoserine5 Publications

    Post-translational modificationi

    Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPD2 and NCAPH subunits, activates the condensin complex and is required for chromosome condensation By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BPX3.
    PaxDbiQ9BPX3.
    PeptideAtlasiQ9BPX3.
    PRIDEiQ9BPX3.

    PTM databases

    PhosphoSiteiQ9BPX3.

    Expressioni

    Tissue specificityi

    Highly expressed in testis.1 Publication

    Gene expression databases

    ArrayExpressiQ9BPX3.
    BgeeiQ9BPX3.
    CleanExiHS_CAPG.
    HS_NCAPG.
    GenevestigatoriQ9BPX3.

    Organism-specific databases

    HPAiHPA039613.
    HPA040103.

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCAPD2Q150212EBI-970214,EBI-1044041
    NCAPHQ150032EBI-970214,EBI-1046410

    Protein-protein interaction databases

    BioGridi122089. 22 interactions.
    IntActiQ9BPX3. 8 interactions.
    MINTiMINT-3060256.
    STRINGi9606.ENSP00000251496.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BPX3.
    SMRiQ9BPX3. Positions 95-307, 408-451, 624-652, 692-718.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati94 – 13138HEAT 1Add
    BLAST
    Repeati138 – 17336HEAT 2Add
    BLAST
    Repeati174 – 21239HEAT 3Add
    BLAST
    Repeati238 – 27538HEAT 4Add
    BLAST
    Repeati276 – 31338HEAT 5Add
    BLAST
    Repeati399 – 43638HEAT 6Add
    BLAST
    Repeati439 – 47840HEAT 7Add
    BLAST
    Repeati617 – 65438HEAT 8Add
    BLAST
    Repeati687 – 72438HEAT 9Add
    BLAST
    Repeati865 – 90743HEAT 10Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi88 – 914Poly-Glu
    Compositional biasi912 – 9176Poly-Thr

    Sequence similaritiesi

    Belongs to the CND3 (condensin subunit 3) family.Curated
    Contains 10 HEAT repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5218.
    HOVERGENiHBG039407.
    InParanoidiQ9BPX3.
    KOiK06678.
    OMAiEACCYEP.
    OrthoDBiEOG7CVPWZ.
    PhylomeDBiQ9BPX3.
    TreeFamiTF101160.

    Family and domain databases

    Gene3Di1.25.10.10. 3 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR027165. CND3.
    IPR025977. Cnd3_C.
    [Graphical view]
    PANTHERiPTHR14418. PTHR14418. 1 hit.
    PfamiPF12719. Cnd3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9BPX3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAERRLLSI KEAFRLAQQP HQNQAKLVVA LSRTYRTMDD KTVFHEEFIH     50
    YLKYVMVVYK REPAVERVIE FAAKFVTSFH QSDMEDDEEE EDGGLLNYLF 100
    TFLLKSHEAN SNAVRFRVCL LINKLLGSMP ENAQIDDDVF DKINKAMLIR 150
    LKDKIPNVRI QAVLALSRLQ DPKDDECPVV NAYATLIEND SNPEVRRAVL 200
    SCIAPSAKTL PKIVGRTKDV KEAVRKLAYQ VLAEKVHMRA MSIAQRVMLL 250
    QQGLNDRSDA VKQAMQKHLL QGWLRFSEGN ILELLHRLDV ENSSEVAVSV 300
    LNALFSITPL SELVGLCKNN DGRKLIPVET LTPEIALYWC ALCEYLKSKG 350
    DEGEEFLEQI LPEPVVYADY LLSYIQSIPV VNEEHRGDFS YIGNLMTKEF 400
    IGQQLILIIK SLDTSEEGGR KKLLAVLQEI LILPTIPISL VSFLVERLLH 450
    IIIDDNKRTQ IVTEIISEIR APIVTVGVNN DPADVRKKEL KMAEIKVKLI 500
    EAKEALENCI TLQDFNRASE LKEEIKALED ARINLLKETE QLEIKEVHIE 550
    KNDAETLQKC LILCYELLKQ MSISTGLSAT MNGIIESLIL PGIISIHPVV 600
    RNLAVLCLGC CGLQNQDFAR KHFVLLLQVL QIDDVTIKIS ALKAIFDQLM 650
    TFGIEPFKTK KIKTLHCEGT EINSDDEQES KEVEETATAK NVLKLLSDFL 700
    DSEVSELRTG AAEGLAKLMF SGLLVSSRIL SRLILLWYNP VTEEDVQLRH 750
    CLGVFFPVFA YASRTNQECF EEAFLPTLQT LANAPASSPL AEIDITNVAE 800
    LLVDLTRPSG LNPQAKTSQD YQALTVHDNL AMKICNEILT SPCSPEIRVY 850
    TKALSSLELS SHLAKDLLVL LNEILEQVKD RTCLRALEKI KIQLEKGNKE 900
    FGDQAEAAQD ATLTTTTFQN EDEKNKEVYM TPLRGVKATQ ASKSTQLKTN 950
    RGQRKVTVSA RTNRRCQTAE ADSESDHEVP EPESEMKMRL PRRAKTAALE 1000
    KSKLNLAQFL NEDLS 1015
    Length:1,015
    Mass (Da):114,334
    Last modified:June 1, 2001 - v1
    Checksum:iD9ACC205C48F3AF5
    GO

    Sequence cautioni

    The sequence AAH00827.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB14429.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB55165.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1151R → G in BAB14069. (PubMed:14702039)Curated
    Sequence conflicti276 – 2761F → V in AAG30732. (PubMed:10910072)Curated
    Sequence conflicti519 – 5191S → P in BAB55165. (PubMed:14702039)Curated
    Sequence conflicti676 – 6761D → V in BAB14069. (PubMed:14702039)Curated
    Sequence conflicti681 – 6811K → R in BAB14069. (PubMed:14702039)Curated
    Sequence conflicti704 – 7041V → A in BAB14069. (PubMed:14702039)Curated
    Sequence conflicti836 – 8361N → D in BAB55165. (PubMed:14702039)Curated
    Sequence conflicti1010 – 10101L → F in AAG30732. (PubMed:10910072)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti64 – 641A → P.
    Corresponds to variant rs35722563 [ dbSNP | Ensembl ].
    VAR_053041
    Natural varianti265 – 2651M → T in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036125
    Natural varianti581 – 5811M → I.1 Publication
    Corresponds to variant rs3795243 [ dbSNP | Ensembl ].
    VAR_053042

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF235023 mRNA. Translation: AAG30732.1.
    AF331796 mRNA. Translation: AAG49627.1.
    AB013299 mRNA. Translation: BAB21557.1.
    AK022512 mRNA. Translation: BAB14069.1.
    AK023147 mRNA. Translation: BAB14429.1. Different initiation.
    AK027511 mRNA. Translation: BAB55165.1. Different initiation.
    BC000827 mRNA. Translation: AAH00827.1. Different initiation.
    BC101476 mRNA. Translation: AAI01477.1.
    CCDSiCCDS3424.1.
    RefSeqiNP_071741.2. NM_022346.4.
    UniGeneiHs.567567.

    Genome annotation databases

    EnsembliENST00000251496; ENSP00000251496; ENSG00000109805.
    GeneIDi64151.
    KEGGihsa:64151.
    UCSCiuc003gpp.4. human.

    Polymorphism databases

    DMDMi30172941.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF235023 mRNA. Translation: AAG30732.1 .
    AF331796 mRNA. Translation: AAG49627.1 .
    AB013299 mRNA. Translation: BAB21557.1 .
    AK022512 mRNA. Translation: BAB14069.1 .
    AK023147 mRNA. Translation: BAB14429.1 . Different initiation.
    AK027511 mRNA. Translation: BAB55165.1 . Different initiation.
    BC000827 mRNA. Translation: AAH00827.1 . Different initiation.
    BC101476 mRNA. Translation: AAI01477.1 .
    CCDSi CCDS3424.1.
    RefSeqi NP_071741.2. NM_022346.4.
    UniGenei Hs.567567.

    3D structure databases

    ProteinModelPortali Q9BPX3.
    SMRi Q9BPX3. Positions 95-307, 408-451, 624-652, 692-718.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122089. 22 interactions.
    IntActi Q9BPX3. 8 interactions.
    MINTi MINT-3060256.
    STRINGi 9606.ENSP00000251496.

    PTM databases

    PhosphoSitei Q9BPX3.

    Polymorphism databases

    DMDMi 30172941.

    Proteomic databases

    MaxQBi Q9BPX3.
    PaxDbi Q9BPX3.
    PeptideAtlasi Q9BPX3.
    PRIDEi Q9BPX3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251496 ; ENSP00000251496 ; ENSG00000109805 .
    GeneIDi 64151.
    KEGGi hsa:64151.
    UCSCi uc003gpp.4. human.

    Organism-specific databases

    CTDi 64151.
    GeneCardsi GC04P017812.
    HGNCi HGNC:24304. NCAPG.
    HPAi HPA039613.
    HPA040103.
    MIMi 606280. gene.
    neXtProti NX_Q9BPX3.
    PharmGKBi PA162397165.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5218.
    HOVERGENi HBG039407.
    InParanoidi Q9BPX3.
    KOi K06678.
    OMAi EACCYEP.
    OrthoDBi EOG7CVPWZ.
    PhylomeDBi Q9BPX3.
    TreeFami TF101160.

    Enzyme and pathway databases

    Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.

    Miscellaneous databases

    GeneWikii NCAPG.
    GenomeRNAii 64151.
    NextBioi 66065.
    PROi Q9BPX3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BPX3.
    Bgeei Q9BPX3.
    CleanExi HS_CAPG.
    HS_NCAPG.
    Genevestigatori Q9BPX3.

    Family and domain databases

    Gene3Di 1.25.10.10. 3 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR027165. CND3.
    IPR025977. Cnd3_C.
    [Graphical view ]
    PANTHERi PTHR14418. PTHR14418. 1 hit.
    Pfami PF12719. Cnd3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Serological cloning of a melanocyte rab guanosine 5'-triphosphate-binding protein and a chromosome condensation protein from a melanoma complementary DNA library."
      Jaeger D., Stockert E., Jaeger E., Guere A.O., Scanlan M.J., Knuth A., Old L.J., Chen Y.-T.
      Cancer Res. 60:3584-3591(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT ILE-581.
      Tissue: Melanocyte.
    2. "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: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; NCAPD2 AND NCAPH, FUNCTION OF THE COMPLEX.
    3. "Differentiation responsive gene."
      Minami T., Doi T., Tachibana K., Okada Y.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Erythroleukemia.
    4. "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].
      Tissue: Teratocarcinoma.
    5. "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].
      Tissue: Placenta.
    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-674 AND SER-1015, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    8. "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-674 AND SER-1015, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-973; SER-975 AND SER-1002, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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].
    11. "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-390; SER-674 AND SER-1015, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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-390; SER-674; THR-931 AND SER-1015, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-674 AND SER-1015, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-265.

    Entry informationi

    Entry nameiCND3_HUMAN
    AccessioniPrimary (citable) accession number: Q9BPX3
    Secondary accession number(s): Q3MJE0
    , Q96SV9, Q9BUR3, Q9BVY1, Q9H914, Q9H9Z6, Q9HBI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 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

    Miscellaneous

    Overexpressed in some cancer lines and some tumor cells.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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