Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15003

- CND2_HUMAN

UniProt

Q15003 - CND2_HUMAN

Protein

Condensin complex subunit 2

Gene

NCAPH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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: IntAct

    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 2
    Alternative name(s):
    Barren homolog protein 1
    Chromosome-associated protein H
    Short name:
    hCAP-H
    Non-SMC condensin I complex subunit H
    XCAP-H homolog
    Gene namesi
    Name:NCAPH
    Synonyms:BRRN, BRRN1, CAPH, KIAA0074
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:1112. NCAPH.

    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. condensin complex Source: UniProtKB
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. membrane Source: UniProtKB
    5. microtubule cytoskeleton Source: HPA
    6. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162397273.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 741741Condensin complex subunit 2PRO_0000095038Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151Phosphoserine1 Publication
    Modified residuei25 – 251Phosphoserine1 Publication
    Modified residuei49 – 491Phosphothreonine1 Publication
    Modified residuei70 – 701Phosphoserine1 Publication
    Modified residuei78 – 781Phosphoserine2 Publications
    Modified residuei81 – 811Phosphoserine3 Publications
    Modified residuei87 – 871Phosphoserine2 Publications
    Modified residuei92 – 921Phosphoserine2 Publications
    Modified residuei96 – 961Phosphoserine1 Publication
    Modified residuei201 – 2011Phosphoserine2 Publications
    Modified residuei432 – 4321Phosphoserine2 Publications
    Modified residuei598 – 5981Phosphothreonine1 Publication
    Modified residuei605 – 6051Phosphothreonine1 Publication
    Modified residuei637 – 6371N6-acetyllysine1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15003.
    PaxDbiQ15003.
    PeptideAtlasiQ15003.
    PRIDEiQ15003.

    PTM databases

    PhosphoSiteiQ15003.

    Miscellaneous databases

    PMAP-CutDBQ15003.

    Expressioni

    Tissue specificityi

    Widely expressed at low level. Expressed in proliferating cells.1 Publication

    Gene expression databases

    ArrayExpressiQ15003.
    BgeeiQ15003.
    CleanExiHS_NCAPH.
    GenevestigatoriQ15003.

    Organism-specific databases

    HPAiHPA002647.
    HPA003008.

    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
    DDX3XO005712EBI-1046410,EBI-353779
    NCAPD2Q150214EBI-1046410,EBI-1044041
    NCAPGQ9BPX32EBI-1046410,EBI-970214
    SMC2O953472EBI-1046410,EBI-355822

    Protein-protein interaction databases

    BioGridi116970. 18 interactions.
    DIPiDIP-43899N.
    IntActiQ15003. 7 interactions.
    MINTiMINT-5004625.
    STRINGi9606.ENSP00000240423.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15003.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CND2 (condensin subunit 2) family.Curated

    Phylogenomic databases

    eggNOGiCOG5229.
    HOGENOMiHOG000231887.
    HOVERGENiHBG036823.
    InParanoidiQ15003.
    KOiK06676.
    OMAiPYPCHPP.
    OrthoDBiEOG7JMGDB.
    PhylomeDBiQ15003.
    TreeFamiTF105678.

    Family and domain databases

    InterProiIPR022816. Condensin_barren_su2.
    [Graphical view]
    PfamiPF05786. Cnd2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017126. Condensin_H. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15003-1) [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

    MGPPGPALPA TMNNSSSETR GHPHSASSPS ERVFPMPLPR KAPLNIPGTP    50
    VLEDFPQNDD EKERLQRRRS RVFDLQFSTD SPRLLASPSS RSIDISATIP 100
    KFTNTQITEH YSTCIKLSTE NKITTKNAFG LHLIDFMSEI LKQKDTEPTN 150
    FKVAAGTLDA STKIYAVRVD AVHADVYRVL GGLGKDAPSL EEVEGHVADG 200
    SATEMGTTKK AVKPKKKHLH RTIEQNINNL NVSEADRKCE IDPMFQKTAA 250
    SFDECSTAGV FLSTLHCQDY RSELLFPSDV QTLSTGEPLE LPELGCVEMT 300
    DLKAPLQQCA EDRQICPSLA GFQFTQWDSE THNESVSALV DKFKKNDQVF 350
    DINAEVDESD CGDFPDGSLG DDFDANDEPD HTAVGDHEEF RSWKEPCQVQ 400
    SCQEEMISLG DGDIRTMCPL LSMKPGEYSY FSPRTMSMWA GPDHWRFRPR 450
    RKQDAPSQSE NKKKSTKKDF EIDFEDDIDF DVYFRKTKAA TILTKSTLEN 500
    QNWRATTLPT DFNYNVDTLV QLHLKPGTRL LKMAQGHRVE TEHYEEIEDY 550
    DYNNPNDTSN FCPGLQAADS DDEDLDDLFV GPVGNSDLSP YPCHPPKTAQ 600
    QNGDTPEAQG LDITTYGESN LVAEPQKVNK IEIHYAKTAK KMDMKKLKQS 650
    MWSLLTALSG KEADAEANHR EAGKEAALAE VADEKMLSGL TKDLQRSLPP 700
    VMAQNLSIPL AFACLLHLAN EKNLKLEGTE DLSDVLVRQG D 741
    Length:741
    Mass (Da):82,563
    Last modified:October 17, 2006 - v3
    Checksum:iB5B34A36CAE0C28E
    GO
    Isoform 2 (identifier: Q15003-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-136: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:605
    Mass (Da):67,495
    Checksum:i4ABE503B4CB20935
    GO

    Sequence cautioni

    The sequence BAA07556.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti539 – 5391V → A.1 Publication
    Corresponds to variant rs2305935 [ dbSNP | Ensembl ].
    VAR_027882

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 136136Missing in isoform 2. 1 PublicationVSP_055179Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38553 mRNA. Translation: BAA07556.1. Different initiation.
    AK303725 mRNA. Translation: BAG64701.1.
    AC021188 Genomic DNA. No translation available.
    BC024211 mRNA. Translation: AAH24211.1.
    CCDSiCCDS2021.1. [Q15003-1]
    CCDS62960.1. [Q15003-2]
    RefSeqiNP_001268639.1. NM_001281710.1.
    NP_001268640.1. NM_001281711.1.
    NP_001268641.1. NM_001281712.1.
    NP_056156.2. NM_015341.4.
    UniGeneiHs.308045.

    Genome annotation databases

    EnsembliENST00000240423; ENSP00000240423; ENSG00000121152. [Q15003-1]
    ENST00000427946; ENSP00000400774; ENSG00000121152. [Q15003-2]
    GeneIDi23397.
    KEGGihsa:23397.
    UCSCiuc002svz.1. human. [Q15003-1]

    Polymorphism databases

    DMDMi116241306.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38553 mRNA. Translation: BAA07556.1 . Different initiation.
    AK303725 mRNA. Translation: BAG64701.1 .
    AC021188 Genomic DNA. No translation available.
    BC024211 mRNA. Translation: AAH24211.1 .
    CCDSi CCDS2021.1. [Q15003-1 ]
    CCDS62960.1. [Q15003-2 ]
    RefSeqi NP_001268639.1. NM_001281710.1.
    NP_001268640.1. NM_001281711.1.
    NP_001268641.1. NM_001281712.1.
    NP_056156.2. NM_015341.4.
    UniGenei Hs.308045.

    3D structure databases

    ProteinModelPortali Q15003.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116970. 18 interactions.
    DIPi DIP-43899N.
    IntActi Q15003. 7 interactions.
    MINTi MINT-5004625.
    STRINGi 9606.ENSP00000240423.

    PTM databases

    PhosphoSitei Q15003.

    Polymorphism databases

    DMDMi 116241306.

    Proteomic databases

    MaxQBi Q15003.
    PaxDbi Q15003.
    PeptideAtlasi Q15003.
    PRIDEi Q15003.

    Protocols and materials databases

    DNASUi 23397.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000240423 ; ENSP00000240423 ; ENSG00000121152 . [Q15003-1 ]
    ENST00000427946 ; ENSP00000400774 ; ENSG00000121152 . [Q15003-2 ]
    GeneIDi 23397.
    KEGGi hsa:23397.
    UCSCi uc002svz.1. human. [Q15003-1 ]

    Organism-specific databases

    CTDi 23397.
    GeneCardsi GC02P097001.
    HGNCi HGNC:1112. NCAPH.
    HPAi HPA002647.
    HPA003008.
    MIMi 602332. gene.
    neXtProti NX_Q15003.
    PharmGKBi PA162397273.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5229.
    HOGENOMi HOG000231887.
    HOVERGENi HBG036823.
    InParanoidi Q15003.
    KOi K06676.
    OMAi PYPCHPP.
    OrthoDBi EOG7JMGDB.
    PhylomeDBi Q15003.
    TreeFami TF105678.

    Enzyme and pathway databases

    Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.

    Miscellaneous databases

    GeneWikii NCAPH.
    GenomeRNAii 23397.
    NextBioi 35476965.
    PMAP-CutDB Q15003.
    PROi Q15003.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15003.
    Bgeei Q15003.
    CleanExi HS_NCAPH.
    Genevestigatori Q15003.

    Family and domain databases

    InterProi IPR022816. Condensin_barren_su2.
    [Graphical view ]
    Pfami PF05786. Cnd2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017126. Condensin_H. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    2. "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] (ISOFORM 2).
      Tissue: Kidney.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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], VARIANT ALA-539.
      Tissue: Placenta.
    5. "Cell cycle-dependent expression and nucleolar localization of hCAP-H."
      Cabello O.A., Eliseeva E., He W.G., Youssoufian H., Plon S.E., Brinkley B.R., Belmont J.W.
      Mol. Biol. Cell 12:3527-3537(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION DURING THE CELL CYCLE, TISSUE SPECIFICITY.
    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; NCAPD2 AND NCAPG, FUNCTION OF THE COMPLEX.
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-78; SER-81; SER-87; SER-92; SER-201; SER-432 AND THR-605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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].
    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-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-15; SER-25; THR-49; SER-78; SER-81; SER-87; SER-92; SER-96; SER-201; SER-432 AND THR-598, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCND2_HUMAN
    AccessioniPrimary (citable) accession number: Q15003
    Secondary accession number(s): B4E189, Q8TB87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 126 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, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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