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Q6IBW4

- CNDH2_HUMAN

UniProt

Q6IBW4 - CNDH2_HUMAN

Protein

Condensin-2 complex subunit H2

Gene

NCAPH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Regulatory subunit of the condensin-2 complex, a complex that seems to provide chromosomes with an additional level of organization and rigidity and in establishing mitotic chromosome architecture. May play a role in lineage-specific role in T-cell development By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Biological processi

    DNA condensation

    Enzyme and pathway databases

    ReactomeiREACT_172744. Condensation of Prophase Chromosomes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Condensin-2 complex subunit H2
    Alternative name(s):
    Chromosome-associated protein H2
    Short name:
    hCAP-H2
    Kleisin-beta
    Non-SMC condensin II complex subunit H2
    Gene namesi
    Name:NCAPH2
    Synonyms:CAPH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:25071. NCAPH2.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication
    Note: Distributed along the arms of chromosomes assembled in vivo and in vitro.

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB
    3. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162397314.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 605605Condensin-2 complex subunit H2PRO_0000326241Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Phosphothreonine1 Publication
    Modified residuei95 – 951Phosphoserine1 Publication
    Modified residuei96 – 961Phosphoserine1 Publication
    Modified residuei200 – 2001Phosphoserine1 Publication
    Modified residuei208 – 2081Phosphoserine2 Publications
    Modified residuei282 – 2821Phosphoserine1 Publication
    Modified residuei284 – 2841Phosphoserine2 Publications
    Modified residuei466 – 4661Phosphoserine1 Publication
    Modified residuei492 – 4921Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ6IBW4.
    PaxDbiQ6IBW4.
    PRIDEiQ6IBW4.

    PTM databases

    PhosphoSiteiQ6IBW4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6IBW4.
    BgeeiQ6IBW4.
    CleanExiHS_NCAPH2.
    GenevestigatoriQ6IBW4.

    Interactioni

    Subunit structurei

    Component of the condensin-2 complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits, NCAPG2, NCAPH2 and NCAPD3 that probably regulate the complex.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCAPD3P426952EBI-2548296,EBI-722805
    NCAPG2Q86XI22EBI-2548296,EBI-1047404
    SMC2O953472EBI-2548296,EBI-355822

    Protein-protein interaction databases

    BioGridi118913. 8 interactions.
    DIPiDIP-43901N.
    IntActiQ6IBW4. 10 interactions.
    MINTiMINT-4329914.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6IBW4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG238357.
    HOVERGENiHBG098083.
    KOiK11490.
    OMAiAPEPASC.
    OrthoDBiEOG7W41C5.
    PhylomeDBiQ6IBW4.
    TreeFamiTF101164.

    Family and domain databases

    InterProiIPR009378. Condensin_II_H2-like.
    [Graphical view]
    PfamiPF06278. DUF1032. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6IBW4-1) [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

    MEDVEARFAH LLQPIRDLTK NWEVDVAAQL GEYLEELDQI CISFDEGKTT    50
    MNFIEAALLI QGSACVYSKK VEYLYSLVYQ ALDFISGKRR AKQLSSVQED 100
    RANGVASSGV PQEAENEFLS LDDFPDSRTN VDLKNDQTPS EVLIIPLLPM 150
    ALVAPDEMEK NNNPLYSRQG EVLASRKDFR MNTCVPHPRG AFMLEPEGMS 200
    PMEPAGVSPM PGTQKDTGRT EEQPMEVSVC RSPVPALGFS QEPGPSPEGP 250
    MPLGGGEDED AEEAVELPEA SAPKAALEPK ESRSPQQSAA LPRRYMLRER 300
    EGAPEPASCV KETPDPWQSL DPFDSLESKP FKKGRPYSVP PCVEEALGQK 350
    RKRKGAAKLQ DFHQWYLAAY ADHADSRRLR RKGPSFADME VLYWTHVKEQ 400
    LETLRKLQRR EVAEQWLRPA EEDHLEDSLE DLGAADDFLE PEEYMEPEGA 450
    DPREAADLDA VPMSLSYEEL VRRNVELFIA TSQKFVQETE LSQRIRDWED 500
    TVQPLLQEQE QHVPFDIHTY GDQLVSRFPQ LNEWCPFAEL VAGQPAFEVC 550
    RSMLASLQLA NDYTVEITQQ PGLEMAVDTM SLRLLTHQRA HKRFQTYAAP 600
    SMAQP 605
    Length:605
    Mass (Da):68,227
    Last modified:July 5, 2004 - v1
    Checksum:i2C8A1070C27B4547
    GO
    Isoform 2 (identifier: Q6IBW4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         167-188: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:583
    Mass (Da):65,716
    Checksum:i21B93C7E157E1E5C
    GO
    Isoform 3 (identifier: Q6IBW4-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         288-299: SAALPRRYMLRE → VGPTWRPAEPEL
         300-605: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:299
    Mass (Da):32,819
    Checksum:iC47577DA567D7AAA
    GO
    Isoform 4 (identifier: Q6IBW4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         435-435: A → AA

    Note: No experimental confirmation available.

    Show »
    Length:606
    Mass (Da):68,298
    Checksum:i9D6FAEBA6500B608
    GO

    Sequence cautioni

    The sequence CAA16670.1 differs from that shown. Reason: Frameshift at positions 56 and 429.
    The sequence AAH00473.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH01509.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH01833.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH01937.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH09441.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAB03345.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAW73552.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361E → D in CAA16670. (PubMed:12529303)Curated
    Sequence conflicti61 – 611Q → H in CAA16670. (PubMed:12529303)Curated
    Sequence conflicti76 – 761S → W in CAA16670. (PubMed:12529303)Curated
    Sequence conflicti161 – 1611N → I in CAA16670. (PubMed:12529303)Curated
    Sequence conflicti190 – 1901G → R in CAA16670. (PubMed:12529303)Curated
    Sequence conflicti215 – 2151K → N in CAA16670. (PubMed:12529303)Curated
    Sequence conflicti249 – 2491G → R in CAA16670. (PubMed:12529303)Curated
    Sequence conflicti282 – 2821S → F in AAH09441. (PubMed:15489334)Curated
    Sequence conflicti316 – 3161P → L in CAA16670. (PubMed:12529303)Curated
    Sequence conflicti323 – 3242FD → LN in CAA16670. (PubMed:12529303)Curated
    Sequence conflicti368 – 3681A → V in CAA16670. (PubMed:12529303)Curated
    Sequence conflicti474 – 4741N → K in CAA16670. (PubMed:12529303)Curated
    Sequence conflicti486 – 4861V → I in CAA16670. (PubMed:12529303)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei167 – 18822Missing in isoform 2. CuratedVSP_032636Add
    BLAST
    Alternative sequencei288 – 29912SAALP…YMLRE → VGPTWRPAEPEL in isoform 3. 1 PublicationVSP_032637Add
    BLAST
    Alternative sequencei300 – 605306Missing in isoform 3. 1 PublicationVSP_032638Add
    BLAST
    Alternative sequencei435 – 4351A → AA in isoform 4. 1 PublicationVSP_032639

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL021682 mRNA. Translation: CAA16670.1. Frameshift.
    CR456604 mRNA. Translation: CAG30490.1.
    U62317 Genomic DNA. Translation: AAB03345.1. Sequence problems.
    CH471138 Genomic DNA. Translation: EAW73554.1.
    CH471138 Genomic DNA. Translation: EAW73556.1.
    CH471138 Genomic DNA. Translation: EAW73552.1. Sequence problems.
    BC000473 mRNA. Translation: AAH00473.1. Different initiation.
    BC001509 mRNA. Translation: AAH01509.1. Different initiation.
    BC001833 mRNA. Translation: AAH01833.1. Different initiation.
    BC001937 mRNA. Translation: AAH01937.1. Different initiation.
    BC009441 mRNA. Translation: AAH09441.1. Different initiation.
    BC014939 mRNA. Translation: AAH14939.2.
    CCDSiCCDS14094.2. [Q6IBW4-1]
    CCDS43038.1. [Q6IBW4-5]
    CCDS54546.1. [Q6IBW4-4]
    RefSeqiNP_001171940.1. NM_001185011.1. [Q6IBW4-4]
    NP_055366.3. NM_014551.4. [Q6IBW4-5]
    NP_689512.2. NM_152299.3. [Q6IBW4-1]
    UniGeneiHs.730607.

    Genome annotation databases

    EnsembliENST00000299821; ENSP00000299821; ENSG00000025770. [Q6IBW4-4]
    ENST00000395698; ENSP00000379050; ENSG00000025770. [Q6IBW4-5]
    ENST00000420993; ENSP00000410088; ENSG00000025770. [Q6IBW4-1]
    GeneIDi29781.
    KEGGihsa:29781.
    UCSCiuc003blq.4. human. [Q6IBW4-5]
    uc003blr.4. human. [Q6IBW4-1]
    uc003blx.4. human. [Q6IBW4-4]

    Polymorphism databases

    DMDMi74709496.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL021682 mRNA. Translation: CAA16670.1 . Frameshift.
    CR456604 mRNA. Translation: CAG30490.1 .
    U62317 Genomic DNA. Translation: AAB03345.1 . Sequence problems.
    CH471138 Genomic DNA. Translation: EAW73554.1 .
    CH471138 Genomic DNA. Translation: EAW73556.1 .
    CH471138 Genomic DNA. Translation: EAW73552.1 . Sequence problems.
    BC000473 mRNA. Translation: AAH00473.1 . Different initiation.
    BC001509 mRNA. Translation: AAH01509.1 . Different initiation.
    BC001833 mRNA. Translation: AAH01833.1 . Different initiation.
    BC001937 mRNA. Translation: AAH01937.1 . Different initiation.
    BC009441 mRNA. Translation: AAH09441.1 . Different initiation.
    BC014939 mRNA. Translation: AAH14939.2 .
    CCDSi CCDS14094.2. [Q6IBW4-1 ]
    CCDS43038.1. [Q6IBW4-5 ]
    CCDS54546.1. [Q6IBW4-4 ]
    RefSeqi NP_001171940.1. NM_001185011.1. [Q6IBW4-4 ]
    NP_055366.3. NM_014551.4. [Q6IBW4-5 ]
    NP_689512.2. NM_152299.3. [Q6IBW4-1 ]
    UniGenei Hs.730607.

    3D structure databases

    ProteinModelPortali Q6IBW4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118913. 8 interactions.
    DIPi DIP-43901N.
    IntActi Q6IBW4. 10 interactions.
    MINTi MINT-4329914.

    PTM databases

    PhosphoSitei Q6IBW4.

    Polymorphism databases

    DMDMi 74709496.

    Proteomic databases

    MaxQBi Q6IBW4.
    PaxDbi Q6IBW4.
    PRIDEi Q6IBW4.

    Protocols and materials databases

    DNASUi 29781.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000299821 ; ENSP00000299821 ; ENSG00000025770 . [Q6IBW4-4 ]
    ENST00000395698 ; ENSP00000379050 ; ENSG00000025770 . [Q6IBW4-5 ]
    ENST00000420993 ; ENSP00000410088 ; ENSG00000025770 . [Q6IBW4-1 ]
    GeneIDi 29781.
    KEGGi hsa:29781.
    UCSCi uc003blq.4. human. [Q6IBW4-5 ]
    uc003blr.4. human. [Q6IBW4-1 ]
    uc003blx.4. human. [Q6IBW4-4 ]

    Organism-specific databases

    CTDi 29781.
    GeneCardsi GC22P050946.
    H-InvDB HIX0016615.
    HGNCi HGNC:25071. NCAPH2.
    MIMi 611230. gene.
    neXtProti NX_Q6IBW4.
    PharmGKBi PA162397314.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238357.
    HOVERGENi HBG098083.
    KOi K11490.
    OMAi APEPASC.
    OrthoDBi EOG7W41C5.
    PhylomeDBi Q6IBW4.
    TreeFami TF101164.

    Enzyme and pathway databases

    Reactomei REACT_172744. Condensation of Prophase Chromosomes.

    Miscellaneous databases

    GeneWikii NCAPH2.
    GenomeRNAii 29781.
    NextBioi 52312.
    PROi Q6IBW4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6IBW4.
    Bgeei Q6IBW4.
    CleanExi HS_NCAPH2.
    Genevestigatori Q6IBW4.

    Family and domain databases

    InterProi IPR009378. Condensin_II_H2-like.
    [Graphical view ]
    Pfami PF06278. DUF1032. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
      Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
      Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1; 3 AND 4).
      Tissue: Brain, Lung, Muscle and Skin.
    6. "Differential contributions of condensin I and condensin II to mitotic chromosome architecture in vertebrate cells."
      Ono T., Losada A., Hirano M., Myers M.P., Neuwald A.F., Hirano T.
      Cell 115:109-121(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN CONDENSIN-2 COMPLEX WITH SMC2; SMC4; NCAPG2; NCAPH2 AND NCAPD3, FUNCTION OF THE COMPLEX, SUBCELLULAR LOCATION.
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "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-284 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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].
    12. "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-208, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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 THR-19; SER-95; SER-96; SER-200; SER-208; SER-284; SER-466 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCNDH2_HUMAN
    AccessioniPrimary (citable) accession number: Q6IBW4
    Secondary accession number(s): B7WPH1
    , O43788, Q13391, Q96C14, Q96GJ0, Q9BQ71, Q9BUT3, Q9BVD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 87 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3