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Q9BSJ2

- GCP2_HUMAN

UniProt

Q9BSJ2 - GCP2_HUMAN

Protein

Gamma-tubulin complex component 2

Gene

TUBGCP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (06 Jun 2002)
      Previous versions | rss
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    Functioni

    Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. G2/M transition of mitotic cell cycle Source: Reactome
    2. microtubule nucleation Source: ProtInc
    3. mitotic cell cycle Source: Reactome
    4. protein complex assembly Source: ProtInc

    Enzyme and pathway databases

    ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-tubulin complex component 2
    Short name:
    GCP-2
    Short name:
    hGCP2
    Alternative name(s):
    Gamma-ring complex protein 103 kDa
    Short name:
    h103p
    Short name:
    hGrip103
    Spindle pole body protein Spc97 homolog
    Short name:
    hSpc97
    Gene namesi
    Name:TUBGCP2
    Synonyms:GCP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:18599. TUBGCP2.

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasmic microtubule Source: ProtInc
    3. cytosol Source: Reactome
    4. membrane Source: UniProtKB
    5. microtubule organizing center Source: ProtInc
    6. spindle pole Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38598.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 902902Gamma-tubulin complex component 2PRO_0000078113Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei83 – 831Phosphotyrosine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BSJ2.
    PaxDbiQ9BSJ2.
    PRIDEiQ9BSJ2.

    PTM databases

    PhosphoSiteiQ9BSJ2.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.

    Gene expression databases

    ArrayExpressiQ9BSJ2.
    BgeeiQ9BSJ2.
    CleanExiHS_TUBGCP2.
    GenevestigatoriQ9BSJ2.

    Organism-specific databases

    HPAiHPA037885.

    Interactioni

    Subunit structurei

    Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6.

    Protein-protein interaction databases

    BioGridi116055. 21 interactions.
    IntActiQ9BSJ2. 20 interactions.
    MINTiMINT-1152554.
    STRINGi9606.ENSP00000252936.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BSJ2.
    SMRiQ9BSJ2. Positions 388-764.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi109 – 1124Poly-Ala

    Sequence similaritiesi

    Belongs to the TUBGCP family.Curated

    Phylogenomic databases

    eggNOGiNOG268971.
    HOGENOMiHOG000273895.
    HOVERGENiHBG026103.
    InParanoidiQ9BSJ2.
    KOiK16569.
    OMAiLTEDKEX.
    OrthoDBiEOG7FFMR6.
    PhylomeDBiQ9BSJ2.
    TreeFamiTF324047.

    Family and domain databases

    InterProiIPR007259. TUBGCP.
    [Graphical view]
    PANTHERiPTHR19302. PTHR19302. 1 hit.
    PfamiPF04130. Spc97_Spc98. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms may exist. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Isoform 1 (identifier: Q9BSJ2-1) [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

    MSEFRIHHDV NELLSLLRVH GGDGAEVYID LLQKNRTPYV TTTVSAHSAK    50
    VKIAEFSRTP EDFLKKYDEL KSKNTRNLDP LVYLLSKLTE DKETLQYLQQ 100
    NAKERAELAA AAVGSSTTSI NVPAAASKIS MQELEELRKQ LGSVATGSTL 150
    QQSLELKRKM LRDKQNKKNS GQHLPIFPAW VYERPALIGD FLIGAGISTD 200
    TALPIGTLPL ASQESAVVED LLYVLVGVDG RYVSAQPLAG RQSRTFLVDP 250
    NLDLSIRELV HRILPVAASY SAVTRFIEEK SSFEYGQVNH ALAAAMRTLV 300
    KEHLILVSQL EQLHRQGLLS LQKLWFYIQP AMRTMDILAS LATSVDKGEC 350
    LGGSTLSLLH DRSFSYTGDS QAQELCLYLT KAASAPYFEV LEKWIYRGII 400
    HDPYSEFMVE EHELRKERIQ EDYNDKYWDQ RYTIVQQQIP SFLQKMADKI 450
    LSTGKYLNVV RECGHDVTCP VAKEIIYTLK ERAYVEQIEK AFNYASKVLL 500
    DFLMEEKELV AHLRSIKRYF LMDQGDFFVH FMDLAEEELR KPVEDITPPR 550
    LEALLELALR MSTANTDPFK DDLKIDLMPH DLITQLLRVL AIETKQEKAM 600
    AHADPTELAL SGLEAFSFDY IVKWPLSLII NRKALTRYQM LFRHMFYCKH 650
    VERQLCSVWI SNKTAKQHSL HSAQWFAGAF TLRQRMLNFV QNIQYYMMFE 700
    VMEPTWHILE KNLKSASNID DVLGHHTGFL DTCLKDCMLT NPELLKVFSK 750
    LMSVCVMFTN CMQKFTQSMK LDGELGGQTL EHSTVLGLPA GAEERARKEL 800
    ARKHLAEHAD TVQLVSGFEA TINKFDKNFS AHLLDLLARL SIYSTSDCEH 850
    GMASVISRLD FNGFYTERLE RLSAERSQKA TPQVPVLRGP PAPAPRVAVT 900
    AQ 902
    Length:902
    Mass (Da):102,534
    Last modified:June 6, 2002 - v2
    Checksum:i4FAAF864A3758E6A
    GO
    Isoform 2 (identifier: Q9BSJ2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-130: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:772
    Mass (Da):88,091
    Checksum:i648F3F29C7510172
    GO
    Isoform 3 (identifier: Q9BSJ2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         205-205: I → IVLLRWNLALSPRLKCSGVISAHCNLHLP

    Note: No experimental confirmation available.Curated

    Show »
    Length:930
    Mass (Da):105,628
    Checksum:iE90F119D86C00010
    GO

    Sequence cautioni

    The sequence BC005011 differs from that shown. Reason: Frameshift at position 513.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti279 – 2791E → G in BAG59730. (PubMed:14702039)Curated
    Sequence conflicti641 – 6411L → F in BC005011. (PubMed:15489334)Curated
    Isoform 3 (identifier: Q9BSJ2-4)
    Sequence conflicti209 – 2091R → G in AAI43248. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti111 – 1111A → T.
    Corresponds to variant rs2298121 [ dbSNP | Ensembl ].
    VAR_022126
    Natural varianti193 – 1931I → T.
    Corresponds to variant rs11101682 [ dbSNP | Ensembl ].
    VAR_049249
    Natural varianti809 – 8091A → T.
    Corresponds to variant rs11101677 [ dbSNP | Ensembl ].
    VAR_049250

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 130130Missing in isoform 2. 1 PublicationVSP_044698Add
    BLAST
    Alternative sequencei205 – 2051I → IVLLRWNLALSPRLKCSGVI SAHCNLHLP in isoform 3. 1 PublicationVSP_045982

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF042379 mRNA. Translation: AAC39728.1.
    AK297251 mRNA. Translation: BAG59730.1.
    AL360181, AL592071 Genomic DNA. Translation: CAH70275.1.
    BC005011 mRNA. No translation available.
    BC093770 mRNA. Translation: AAH93770.1.
    BC111957 mRNA. Translation: AAI11958.1.
    BC143247 mRNA. Translation: AAI43248.1.
    CCDSiCCDS58104.1. [Q9BSJ2-3]
    CCDS58105.1. [Q9BSJ2-4]
    CCDS7676.1. [Q9BSJ2-1]
    RefSeqiNP_001243546.1. NM_001256617.1. [Q9BSJ2-4]
    NP_001243547.1. NM_001256618.1. [Q9BSJ2-3]
    NP_006650.1. NM_006659.3. [Q9BSJ2-1]
    XP_006717659.1. XM_006717596.1. [Q9BSJ2-1]
    UniGeneiHs.523370.

    Genome annotation databases

    EnsembliENST00000252936; ENSP00000252936; ENSG00000130640. [Q9BSJ2-1]
    ENST00000368563; ENSP00000357551; ENSG00000130640. [Q9BSJ2-1]
    ENST00000417178; ENSP00000395666; ENSG00000130640. [Q9BSJ2-3]
    ENST00000543663; ENSP00000446093; ENSG00000130640. [Q9BSJ2-4]
    GeneIDi10844.
    KEGGihsa:10844.
    UCSCiuc001lmf.2. human. [Q9BSJ2-1]

    Polymorphism databases

    DMDMi21450889.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF042379 mRNA. Translation: AAC39728.1 .
    AK297251 mRNA. Translation: BAG59730.1 .
    AL360181 , AL592071 Genomic DNA. Translation: CAH70275.1 .
    BC005011 mRNA. No translation available.
    BC093770 mRNA. Translation: AAH93770.1 .
    BC111957 mRNA. Translation: AAI11958.1 .
    BC143247 mRNA. Translation: AAI43248.1 .
    CCDSi CCDS58104.1. [Q9BSJ2-3 ]
    CCDS58105.1. [Q9BSJ2-4 ]
    CCDS7676.1. [Q9BSJ2-1 ]
    RefSeqi NP_001243546.1. NM_001256617.1. [Q9BSJ2-4 ]
    NP_001243547.1. NM_001256618.1. [Q9BSJ2-3 ]
    NP_006650.1. NM_006659.3. [Q9BSJ2-1 ]
    XP_006717659.1. XM_006717596.1. [Q9BSJ2-1 ]
    UniGenei Hs.523370.

    3D structure databases

    ProteinModelPortali Q9BSJ2.
    SMRi Q9BSJ2. Positions 388-764.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116055. 21 interactions.
    IntActi Q9BSJ2. 20 interactions.
    MINTi MINT-1152554.
    STRINGi 9606.ENSP00000252936.

    PTM databases

    PhosphoSitei Q9BSJ2.

    Polymorphism databases

    DMDMi 21450889.

    Proteomic databases

    MaxQBi Q9BSJ2.
    PaxDbi Q9BSJ2.
    PRIDEi Q9BSJ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252936 ; ENSP00000252936 ; ENSG00000130640 . [Q9BSJ2-1 ]
    ENST00000368563 ; ENSP00000357551 ; ENSG00000130640 . [Q9BSJ2-1 ]
    ENST00000417178 ; ENSP00000395666 ; ENSG00000130640 . [Q9BSJ2-3 ]
    ENST00000543663 ; ENSP00000446093 ; ENSG00000130640 . [Q9BSJ2-4 ]
    GeneIDi 10844.
    KEGGi hsa:10844.
    UCSCi uc001lmf.2. human. [Q9BSJ2-1 ]

    Organism-specific databases

    CTDi 10844.
    GeneCardsi GC10M135094.
    HGNCi HGNC:18599. TUBGCP2.
    HPAi HPA037885.
    neXtProti NX_Q9BSJ2.
    PharmGKBi PA38598.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG268971.
    HOGENOMi HOG000273895.
    HOVERGENi HBG026103.
    InParanoidi Q9BSJ2.
    KOi K16569.
    OMAi LTEDKEX.
    OrthoDBi EOG7FFMR6.
    PhylomeDBi Q9BSJ2.
    TreeFami TF324047.

    Enzyme and pathway databases

    Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.

    Miscellaneous databases

    ChiTaRSi TUBGCP2. human.
    GeneWikii TUBGCP2.
    GenomeRNAii 10844.
    NextBioi 41170.
    PROi Q9BSJ2.

    Gene expression databases

    ArrayExpressi Q9BSJ2.
    Bgeei Q9BSJ2.
    CleanExi HS_TUBGCP2.
    Genevestigatori Q9BSJ2.

    Family and domain databases

    InterProi IPR007259. TUBGCP.
    [Graphical view ]
    PANTHERi PTHR19302. PTHR19302. 1 hit.
    Pfami PF04130. Spc97_Spc98. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The mammalian gamma-tubulin complex contains homologues of the yeast spindle pole body components spc97p and spc98p."
      Murphy S.M., Urbani L., Stearns T.
      J. Cell Biol. 141:663-674(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Cervix carcinoma.
    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: Brain.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [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] (ISOFORMS 1 AND 3).
      Tissue: Brain and Pancreas.
    5. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGCP2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BSJ2
    Secondary accession number(s): B4DM18
    , B7ZKL8, F5H4E0, F5H4L0, O43632, Q5VWX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: June 6, 2002
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3