ID GCP2_HUMAN Reviewed; 902 AA.
AC Q9BSJ2; B4DM18; B7ZKL8; F5H4E0; F5H4L0; O43632; Q5VWX7;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 30-NOV-2016, entry version 148.
DE RecName: Full=Gamma-tubulin complex component 2;
DE Short=GCP-2;
DE Short=hGCP2;
DE AltName: Full=Gamma-ring complex protein 103 kDa;
DE Short=h103p;
DE Short=hGrip103;
DE AltName: Full=Spindle pole body protein Spc97 homolog;
DE Short=hSpc97;
GN Name=TUBGCP2; Synonyms=GCP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RX PubMed=9566967; DOI=10.1083/jcb.141.3.663;
RA Murphy S.M., Urbani L., Stearns T.;
RT "The mammalian gamma-tubulin complex contains homologues of the yeast
RT spindle pole body components spc97p and spc98p.";
RL J. Cell Biol. 141:663-674(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-83, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP INTERACTION WITH ATF5.
RX PubMed=26213385; DOI=10.1016/j.cell.2015.06.055;
RA Madarampalli B., Yuan Y., Liu D., Lengel K., Xu Y., Li G., Yang J.,
RA Liu X., Lu Z., Liu D.X.;
RT "ATF5 Connects the Pericentriolar Materials to the Proximal End of the
RT Mother Centriole.";
RL Cell 162:580-592(2015).
CC -!- FUNCTION: Gamma-tubulin complex is necessary for microtubule
CC nucleation at the centrosome.
CC -!- SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin,
CC TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. Interacts with
CC ATF5; the ATF5:PCNT:polyglutamylated tubulin (PGT) tripartite
CC unites the mother centriole and the pericentriolar material (PCM)
CC in the centrosome (PubMed:26213385). {ECO:0000269|PubMed:26213385,
CC ECO:0000269|PubMed:9566967}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms may exist. May be produced at very
CC low levels due to a premature stop codon in the mRNA, leading to
CC nonsense-mediated mRNA decay.;
CC Name=1;
CC IsoId=Q9BSJ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BSJ2-3; Sequence=VSP_044698;
CC Note=No experimental confirmation available.;
CC Name=3;
CC IsoId=Q9BSJ2-4; Sequence=VSP_045982;
CC Note=No experimental confirmation available. Ref.4 (AAI43248)
CC sequence is in conflict in position: 209:R->G. {ECO:0000305};
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC005011; Type=Frameshift; Positions=513; Evidence={ECO:0000305};
DR EMBL; AF042379; AAC39728.1; -; mRNA.
DR EMBL; AK297251; BAG59730.1; -; mRNA.
DR EMBL; AL360181; CAH70275.1; -; Genomic_DNA.
DR EMBL; AL592071; CAH70275.1; JOINED; Genomic_DNA.
DR EMBL; BC005011; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC093770; AAH93770.1; -; mRNA.
DR EMBL; BC111957; AAI11958.1; -; mRNA.
DR EMBL; BC143247; AAI43248.1; -; mRNA.
DR CCDS; CCDS58104.1; -. [Q9BSJ2-3]
DR CCDS; CCDS58105.1; -. [Q9BSJ2-4]
DR CCDS; CCDS7676.1; -. [Q9BSJ2-1]
DR RefSeq; NP_001243546.1; NM_001256617.1. [Q9BSJ2-4]
DR RefSeq; NP_001243547.1; NM_001256618.1. [Q9BSJ2-3]
DR RefSeq; NP_006650.1; NM_006659.3. [Q9BSJ2-1]
DR UniGene; Hs.523370; -.
DR ProteinModelPortal; Q9BSJ2; -.
DR BioGrid; 116055; 100.
DR IntAct; Q9BSJ2; 45.
DR MINT; MINT-1152554; -.
DR STRING; 9606.ENSP00000252936; -.
DR iPTMnet; Q9BSJ2; -.
DR PhosphoSitePlus; Q9BSJ2; -.
DR BioMuta; TUBGCP2; -.
DR DMDM; 21450889; -.
DR EPD; Q9BSJ2; -.
DR MaxQB; Q9BSJ2; -.
DR PaxDb; Q9BSJ2; -.
DR PeptideAtlas; Q9BSJ2; -.
DR PRIDE; Q9BSJ2; -.
DR Ensembl; ENST00000252936; ENSP00000252936; ENSG00000130640. [Q9BSJ2-1]
DR Ensembl; ENST00000368563; ENSP00000357551; ENSG00000130640. [Q9BSJ2-1]
DR Ensembl; ENST00000417178; ENSP00000395666; ENSG00000130640. [Q9BSJ2-3]
DR Ensembl; ENST00000543663; ENSP00000446093; ENSG00000130640. [Q9BSJ2-4]
DR GeneID; 10844; -.
DR KEGG; hsa:10844; -.
DR UCSC; uc001lmg.2; human. [Q9BSJ2-1]
DR CTD; 10844; -.
DR DisGeNET; 10844; -.
DR GeneCards; TUBGCP2; -.
DR HGNC; HGNC:18599; TUBGCP2.
DR HPA; HPA037885; -.
DR neXtProt; NX_Q9BSJ2; -.
DR OpenTargets; ENSG00000130640; -.
DR PharmGKB; PA38598; -.
DR eggNOG; KOG2001; Eukaryota.
DR eggNOG; ENOG410XNRE; LUCA.
DR GeneTree; ENSGT00850000132278; -.
DR HOGENOM; HOG000273895; -.
DR HOVERGEN; HBG026103; -.
DR InParanoid; Q9BSJ2; -.
DR KO; K16569; -.
DR OMA; FNAFYSD; -.
DR OrthoDB; EOG091G01V2; -.
DR PhylomeDB; Q9BSJ2; -.
DR TreeFam; TF324047; -.
DR BioCyc; ZFISH:ENSG00000130640-MONOMER; -.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR ChiTaRS; TUBGCP2; human.
DR GeneWiki; TUBGCP2; -.
DR GenomeRNAi; 10844; -.
DR PRO; PR:Q9BSJ2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR Bgee; ENSG00000130640; -.
DR CleanEx; HS_TUBGCP2; -.
DR ExpressionAtlas; Q9BSJ2; baseline and differential.
DR Genevisible; Q9BSJ2; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IBA:GO_Central.
DR GO; GO:0008275; C:gamma-tubulin small complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051415; P:interphase microtubule nucleation by interphase microtubule organizing center; IBA:GO_Central.
DR GO; GO:0007126; P:meiotic nuclear division; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; TAS:ProtInc.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR InterPro; IPR007259; GCP.
DR PANTHER; PTHR19302; PTHR19302; 2.
DR Pfam; PF04130; Spc97_Spc98; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
KW Microtubule; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 902 Gamma-tubulin complex component 2.
FT /FTId=PRO_0000078113.
FT COMPBIAS 109 112 Poly-Ala.
FT MOD_RES 83 83 Phosphotyrosine.
FT {ECO:0000244|PubMed:15592455}.
FT VAR_SEQ 1 130 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_044698.
FT VAR_SEQ 205 205 I -> IVLLRWNLALSPRLKCSGVISAHCNLHLP (in
FT isoform 3).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_045982.
FT VARIANT 111 111 A -> T (in dbSNP:rs2298121).
FT /FTId=VAR_022126.
FT VARIANT 193 193 I -> T (in dbSNP:rs11101682).
FT /FTId=VAR_049249.
FT VARIANT 809 809 A -> T (in dbSNP:rs11101677).
FT /FTId=VAR_049250.
FT CONFLICT 279 279 E -> G (in Ref. 2; BAG59730).
FT {ECO:0000305}.
FT CONFLICT 641 641 L -> F (in Ref. 4; BC005011).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 220 738 ipfam:Spc97_Spc98 [T]
SQ SEQUENCE 902 AA; 102534 MW; 4FAAF864A3758E6A CRC64;
MSEFRIHHDV NELLSLLRVH GGDGAEVYID LLQKNRTPYV TTTVSAHSAK VKIAEFSRTP
EDFLKKYDEL KSKNTRNLDP LVYLLSKLTE DKETLQYLQQ NAKERAELAA AAVGSSTTSI
NVPAAASKIS MQELEELRKQ LGSVATGSTL QQSLELKRKM LRDKQNKKNS GQHLPIFPAW
VYERPALIGD FLIGAGISTD TALPIGTLPL ASQESAVVED LLYVLVGVDG RYVSAQPLAG
RQSRTFLVDP NLDLSIRELV HRILPVAASY SAVTRFIEEK SSFEYGQVNH ALAAAMRTLV
KEHLILVSQL EQLHRQGLLS LQKLWFYIQP AMRTMDILAS LATSVDKGEC LGGSTLSLLH
DRSFSYTGDS QAQELCLYLT KAASAPYFEV LEKWIYRGII HDPYSEFMVE EHELRKERIQ
EDYNDKYWDQ RYTIVQQQIP SFLQKMADKI LSTGKYLNVV RECGHDVTCP VAKEIIYTLK
ERAYVEQIEK AFNYASKVLL DFLMEEKELV AHLRSIKRYF LMDQGDFFVH FMDLAEEELR
KPVEDITPPR LEALLELALR MSTANTDPFK DDLKIDLMPH DLITQLLRVL AIETKQEKAM
AHADPTELAL SGLEAFSFDY IVKWPLSLII NRKALTRYQM LFRHMFYCKH VERQLCSVWI
SNKTAKQHSL HSAQWFAGAF TLRQRMLNFV QNIQYYMMFE VMEPTWHILE KNLKSASNID
DVLGHHTGFL DTCLKDCMLT NPELLKVFSK LMSVCVMFTN CMQKFTQSMK LDGELGGQTL
EHSTVLGLPA GAEERARKEL ARKHLAEHAD TVQLVSGFEA TINKFDKNFS AHLLDLLARL
SIYSTSDCEH GMASVISRLD FNGFYTERLE RLSAERSQKA TPQVPVLRGP PAPAPRVAVT
AQ
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