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Protein

Gamma-tubulin complex component 2

Gene

TUBGCP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

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
Complete GO annotation...

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. nucleoplasm Source: HPA
  7. spindle pole Source: InterPro
Complete GO annotation...

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

BgeeiQ9BSJ2.
CleanExiHS_TUBGCP2.
ExpressionAtlasiQ9BSJ2. baseline and differential.
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. 68 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.
GeneTreeiENSGT00780000121933.
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. AlignAdd to basket

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

        10         20         30         40         50
MSEFRIHHDV NELLSLLRVH GGDGAEVYID LLQKNRTPYV TTTVSAHSAK
60 70 80 90 100
VKIAEFSRTP EDFLKKYDEL KSKNTRNLDP LVYLLSKLTE DKETLQYLQQ
110 120 130 140 150
NAKERAELAA AAVGSSTTSI NVPAAASKIS MQELEELRKQ LGSVATGSTL
160 170 180 190 200
QQSLELKRKM LRDKQNKKNS GQHLPIFPAW VYERPALIGD FLIGAGISTD
210 220 230 240 250
TALPIGTLPL ASQESAVVED LLYVLVGVDG RYVSAQPLAG RQSRTFLVDP
260 270 280 290 300
NLDLSIRELV HRILPVAASY SAVTRFIEEK SSFEYGQVNH ALAAAMRTLV
310 320 330 340 350
KEHLILVSQL EQLHRQGLLS LQKLWFYIQP AMRTMDILAS LATSVDKGEC
360 370 380 390 400
LGGSTLSLLH DRSFSYTGDS QAQELCLYLT KAASAPYFEV LEKWIYRGII
410 420 430 440 450
HDPYSEFMVE EHELRKERIQ EDYNDKYWDQ RYTIVQQQIP SFLQKMADKI
460 470 480 490 500
LSTGKYLNVV RECGHDVTCP VAKEIIYTLK ERAYVEQIEK AFNYASKVLL
510 520 530 540 550
DFLMEEKELV AHLRSIKRYF LMDQGDFFVH FMDLAEEELR KPVEDITPPR
560 570 580 590 600
LEALLELALR MSTANTDPFK DDLKIDLMPH DLITQLLRVL AIETKQEKAM
610 620 630 640 650
AHADPTELAL SGLEAFSFDY IVKWPLSLII NRKALTRYQM LFRHMFYCKH
660 670 680 690 700
VERQLCSVWI SNKTAKQHSL HSAQWFAGAF TLRQRMLNFV QNIQYYMMFE
710 720 730 740 750
VMEPTWHILE KNLKSASNID DVLGHHTGFL DTCLKDCMLT NPELLKVFSK
760 770 780 790 800
LMSVCVMFTN CMQKFTQSMK LDGELGGQTL EHSTVLGLPA GAEERARKEL
810 820 830 840 850
ARKHLAEHAD TVQLVSGFEA TINKFDKNFS AHLLDLLARL SIYSTSDCEH
860 870 880 890 900
GMASVISRLD FNGFYTERLE RLSAERSQKA TPQVPVLRGP PAPAPRVAVT

AQ
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi116055. 68 interactions.
IntActiQ9BSJ2. 20 interactions.
MINTiMINT-1152554.
STRINGi9606.ENSP00000252936.

PTM databases

PhosphoSiteiQ9BSJ2.

Polymorphism databases

DMDMi21450889.

Proteomic databases

MaxQBiQ9BSJ2.
PaxDbiQ9BSJ2.
PRIDEiQ9BSJ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi10844.
GeneCardsiGC10M135094.
HGNCiHGNC:18599. TUBGCP2.
HPAiHPA037885.
neXtProtiNX_Q9BSJ2.
PharmGKBiPA38598.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG268971.
GeneTreeiENSGT00780000121933.
HOGENOMiHOG000273895.
HOVERGENiHBG026103.
InParanoidiQ9BSJ2.
KOiK16569.
OMAiLTEDKEX.
OrthoDBiEOG7FFMR6.
PhylomeDBiQ9BSJ2.
TreeFamiTF324047.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiTUBGCP2. human.
GeneWikiiTUBGCP2.
GenomeRNAii10844.
NextBioi41170.
PROiQ9BSJ2.

Gene expression databases

BgeeiQ9BSJ2.
CleanExiHS_TUBGCP2.
ExpressionAtlasiQ9BSJ2. baseline and differential.
GenevestigatoriQ9BSJ2.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 129 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.