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GCP5_HUMAN
ID   GCP5_HUMAN              Reviewed;        1024 AA.
AC   Q96RT8; E9PB12; Q6IQ52; Q96PY8;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 172.
DE   RecName: Full=Gamma-tubulin complex component 5;
DE            Short=GCP-5;
GN   Name=TUBGCP5; Synonyms=GCP5, KIAA1899;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RX   PubMed=11694571; DOI=10.1091/mbc.12.11.3340;
RA   Murphy S.M., Preble A.M., Patel U.K., O'Connell K.L., Dias D.P., Moritz M.,
RA   Agard D., Stults J.T., Stearns T.;
RT   "GCP5 and GCP6: two new members of the human gamma-tubulin complex.";
RL   Mol. Biol. Cell 12:3340-3352(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA   Nagase T., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XXI. The
RT   complete sequences of 60 new cDNA clones from brain which code for large
RT   proteins.";
RL   DNA Res. 8:179-187(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Teratocarcinoma;
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [5]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Testis;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=14508708; DOI=10.1086/378816;
RA   Chai J.-H., Locke D.P., Greally J.M., Knoll J.H.M., Ohta T., Dunai J.,
RA   Yavor A., Eichler E.E., Nicholls R.D.;
RT   "Identification of four highly conserved genes between breakpoint hotspots
RT   BP1 and BP2 of the Prader-Willi/Angelman syndromes deletion region that
RT   have undergone evolutionary transposition mediated by flanking duplicons.";
RL   Am. J. Hum. Genet. 73:898-925(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [9]
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., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation
CC       at the centrosome.
CC   -!- SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2,
CC       TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6.
CC   -!- INTERACTION:
CC       Q96RT8; Q9Y5R4: HEMK1; NbExp=3; IntAct=EBI-2555061, EBI-10329202;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000269|PubMed:14654843}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96RT8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96RT8-2; Sequence=VSP_047496;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in heart and
CC       skeletal muscle and moderate levels in brain.
CC       {ECO:0000269|PubMed:14508708}.
CC   -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH46182.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AK056416; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AK056416; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB67792.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF272884; AAK77662.1; -; mRNA.
DR   EMBL; AB067486; BAB67792.2; ALT_INIT; mRNA.
DR   EMBL; AK056416; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC116166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC046182; AAH46182.1; ALT_INIT; mRNA.
DR   EMBL; BC071560; AAH71560.1; -; mRNA.
DR   CCDS; CCDS73697.1; -. [Q96RT8-2]
DR   CCDS; CCDS73698.1; -. [Q96RT8-1]
DR   RefSeq; NP_001096080.1; NM_001102610.1. [Q96RT8-2]
DR   RefSeq; NP_443135.3; NM_052903.4. [Q96RT8-1]
DR   PDB; 6L81; X-ray; 2.20 A; A/C=1-119.
DR   PDB; 6V69; EM; 4.20 A; J=1-1024.
DR   PDB; 6V6S; EM; 4.30 A; J=1-1024.
DR   PDB; 7AS4; EM; 4.13 A; J=1-1024.
DR   PDB; 7QJ0; EM; 5.32 A; J/l=1-1024.
DR   PDB; 7QJ1; EM; 7.00 A; J/l=1-1024.
DR   PDB; 7QJ2; EM; 8.60 A; J/l=1-1024.
DR   PDB; 7QJ3; EM; 7.60 A; J/l=1-1024.
DR   PDB; 7QJ4; EM; 9.00 A; J/l=1-1024.
DR   PDB; 7QJ5; EM; 8.70 A; J/l=1-1024.
DR   PDB; 7QJ6; EM; 7.80 A; J/l=1-1024.
DR   PDB; 7QJ7; EM; 8.70 A; J/l=1-1024.
DR   PDB; 7QJ8; EM; 8.70 A; J/l=1-1024.
DR   PDB; 7QJ9; EM; 8.10 A; J/l=1-1024.
DR   PDB; 7QJA; EM; 9.20 A; J/l=1-1024.
DR   PDB; 7QJB; EM; 9.20 A; J/l=1-1024.
DR   PDB; 7QJC; EM; 16.10 A; J/l=1-1024.
DR   PDB; 7QJD; EM; 7.10 A; J/l=1-1024.
DR   PDB; 7QJE; EM; 7.80 A; J=1-1024.
DR   PDBsum; 6L81; -.
DR   PDBsum; 6V69; -.
DR   PDBsum; 6V6S; -.
DR   PDBsum; 7AS4; -.
DR   PDBsum; 7QJ0; -.
DR   PDBsum; 7QJ1; -.
DR   PDBsum; 7QJ2; -.
DR   PDBsum; 7QJ3; -.
DR   PDBsum; 7QJ4; -.
DR   PDBsum; 7QJ5; -.
DR   PDBsum; 7QJ6; -.
DR   PDBsum; 7QJ7; -.
DR   PDBsum; 7QJ8; -.
DR   PDBsum; 7QJ9; -.
DR   PDBsum; 7QJA; -.
DR   PDBsum; 7QJB; -.
DR   PDBsum; 7QJC; -.
DR   PDBsum; 7QJD; -.
DR   PDBsum; 7QJE; -.
DR   AlphaFoldDB; Q96RT8; -.
DR   SMR; Q96RT8; -.
DR   BioGRID; 125353; 57.
DR   CORUM; Q96RT8; -.
DR   IntAct; Q96RT8; 39.
DR   MINT; Q96RT8; -.
DR   STRING; 9606.ENSP00000480316; -.
DR   iPTMnet; Q96RT8; -.
DR   PhosphoSitePlus; Q96RT8; -.
DR   BioMuta; TUBGCP5; -.
DR   DMDM; 20454926; -.
DR   EPD; Q96RT8; -.
DR   jPOST; Q96RT8; -.
DR   MassIVE; Q96RT8; -.
DR   MaxQB; Q96RT8; -.
DR   PaxDb; Q96RT8; -.
DR   PeptideAtlas; Q96RT8; -.
DR   PRIDE; Q96RT8; -.
DR   ProteomicsDB; 19119; -.
DR   ProteomicsDB; 78032; -. [Q96RT8-1]
DR   Antibodypedia; 72633; 148 antibodies from 27 providers.
DR   DNASU; 114791; -.
DR   Ensembl; ENST00000615383.5; ENSP00000480316.1; ENSG00000275835.5. [Q96RT8-1]
DR   Ensembl; ENST00000620435.4; ENSP00000481853.1; ENSG00000275835.5. [Q96RT8-2]
DR   GeneID; 114791; -.
DR   KEGG; hsa:114791; -.
DR   MANE-Select; ENST00000615383.5; ENSP00000480316.1; NM_052903.6; NP_443135.3.
DR   UCSC; uc001yuq.3; human. [Q96RT8-1]
DR   CTD; 114791; -.
DR   DisGeNET; 114791; -.
DR   GeneCards; TUBGCP5; -.
DR   HGNC; HGNC:18600; TUBGCP5.
DR   HPA; ENSG00000275835; Low tissue specificity.
DR   MIM; 608147; gene.
DR   neXtProt; NX_Q96RT8; -.
DR   OpenTargets; ENSG00000275835; -.
DR   PharmGKB; PA38599; -.
DR   VEuPathDB; HostDB:ENSG00000275835; -.
DR   eggNOG; KOG4344; Eukaryota.
DR   GeneTree; ENSGT00940000155962; -.
DR   HOGENOM; CLU_011574_0_0_1; -.
DR   InParanoid; Q96RT8; -.
DR   OMA; RTNQFEV; -.
DR   OrthoDB; 110079at2759; -.
DR   PhylomeDB; Q96RT8; -.
DR   TreeFam; TF329759; -.
DR   PathwayCommons; Q96RT8; -.
DR   Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR   SignaLink; Q96RT8; -.
DR   SIGNOR; Q96RT8; -.
DR   BioGRID-ORCS; 114791; 694 hits in 1080 CRISPR screens.
DR   ChiTaRS; TUBGCP5; human.
DR   GeneWiki; TUBGCP5; -.
DR   GenomeRNAi; 114791; -.
DR   Pharos; Q96RT8; Tbio.
DR   PRO; PR:Q96RT8; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q96RT8; protein.
DR   Bgee; ENSG00000275835; Expressed in sural nerve and 99 other tissues.
DR   ExpressionAtlas; Q96RT8; baseline and differential.
DR   Genevisible; Q96RT8; HS.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0000923; C:equatorial microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR   GO; GO:0000931; C:gamma-tubulin large complex; IDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR   GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR   GO; GO:0007020; P:microtubule nucleation; IDA:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR   Gene3D; 1.20.120.1900; -; 1.
DR   InterPro; IPR007259; GCP.
DR   InterPro; IPR040457; GCP_C.
DR   InterPro; IPR042241; GCP_C_sf.
DR   InterPro; IPR041470; GCP_N.
DR   PANTHER; PTHR19302; PTHR19302; 1.
DR   Pfam; PF04130; GCP_C_terminal; 1.
DR   Pfam; PF17681; GCP_N_terminal; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule;
KW   Reference proteome.
FT   CHAIN           1..1024
FT                   /note="Gamma-tubulin complex component 5"
FT                   /id="PRO_0000078129"
FT   REGION          155..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1010..1024
FT                   /note="LESLALSLMAGMEQS -> CEYIMLKYFYLCISL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_047496"
FT   VARIANT         662
FT                   /note="E -> D (in dbSNP:rs35612840)"
FT                   /id="VAR_049252"
FT   CONFLICT        198
FT                   /note="R -> G (in Ref. 6; AAH71560)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        994
FT                   /note="L -> F (in Ref. 3; AK056416)"
FT                   /evidence="ECO:0000305"
FT   HELIX           14..27
FT                   /evidence="ECO:0007829|PDB:6L81"
FT   HELIX           35..49
FT                   /evidence="ECO:0007829|PDB:6L81"
FT   HELIX           58..74
FT                   /evidence="ECO:0007829|PDB:6L81"
FT   HELIX           78..91
FT                   /evidence="ECO:0007829|PDB:6L81"
FT   HELIX           106..117
FT                   /evidence="ECO:0007829|PDB:6L81"
SQ   SEQUENCE   1024 AA;  118321 MW;  21350677DF126CD1 CRC64;
     MARHGPPWSR LDAQQERDVR ELVRGVAGLQ DEADPNFQLA LNFAWSNFRF HRFLDVNSHK
     IEKTIEGIYE KFVIHSDLSK AASWKRLTEE FLNAPLPSIK EIKTDAHYSI LSLLLCLSDS
     PSNSSYVETP RNKEVEKKDD FDWGKYLMED EEMDIGPYMD TPNWSEESEE ENDQQPLSRE
     DSGIQVDRTP LEEQDQNRKL DPCISWKDEP DDRSWLEHHV VHQYWTARPS QFPHSLHLHS
     NLAAVWDQHL YSSDPLYVPD DRVLVTETQV IRETLWLLSG VKKLFIFQLI DGKVTVRNNI
     IVTHLTHSCL RSVLEQIAAY GQVVFRLQEF IDEVMGHSSE SMLPGSGSVP KKSTEAPFRT
     YQAFMWALYK YFISFKEELA EIEKCIINND TTITLAIVVD KLAPRLSQLK VLHKVFSTGV
     AEVPPDTRNV VRASHLLNTL YKAILEYDNV GEASEQTVSL LFSLWVETVR PYLQTVDEWI
     VHGHLWDGAR EFIIQRNKNV PVNHRDFWYA TYTLYSVSEK TENEEKMSDN ASASSGSDQG
     PSSRQHTMVS FLKPVLKQII MAGKSMQLLK NLQCAESTTC QAGARDAERK SLYTLFLESV
     QSRLRHGEDS TPQVLTEQQA TKENLMKMQS IAESHLELDD VHDPLLAINF ARMYLEQSDF
     HEKFAGGDVC VDRSSESVTC QTFELTLRSC LYPHIDKQYL DCCGNLMQTL KKDYRLVEYL
     QAMRNFFLME GGDTMYDFYT SIFDKIREKE TWQNVSFLNV QLQEAVGQRY PEDSSRLSIS
     FENVDTAKKK LPVHILDGLT LSYKVPWPVD IVISLECQKI YNQVFLLLLQ IKWAKYSLDV
     LLFGELVSTA EKPRLKEGLI HEQDTVAQFG PQKEPVRQQI HRMFLLRVKL MHFVNSLHNY
     IMTRILHSTG LEFQHQVEEA KDLDQLIKIH YRYLSTIHDR CLLREKVSFV KEAIMKVLNL
     ALMFADGWQA GLGTWRMESI EKMESDFKNC HMFLVTILNK AVCRGSFPHL ESLALSLMAG
     MEQS
 
 
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