CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005153
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tubulin gamma-1 chain 
Protein Synonyms/Alias
 Gamma-1-tubulin; Gamma-tubulin complex component 1; GCP-1 
Gene Name
 TUBG1 
Gene Synonyms/Alias
 TUBG 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
48ATEGTDRKDVFFYQAubiquitination[1, 2]
84ILNSPYAKLYNPENIubiquitination[1]
164LNDRYPKKLVQTYSVubiquitination[1, 2]
193YNSLLTLKRLTQNADubiquitination[1, 2]
287QSVASVRKTTVLDVMubiquitination[2, 3, 4, 5, 6]
301MRRLLQPKNVMVSTGubiquitination[1, 2, 5, 6, 7, 8, 9]
344LQRIRERKLANFIPWubiquitination[2, 6]
363IQVALSRKSPYLPSAubiquitination[2, 6]
400RQYDKLRKREAFLEQubiquitination[2]
410AFLEQFRKEDMFKDNubiquitination[1, 2, 8]
415FRKEDMFKDNFDEMDubiquitination[1, 2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation. 
Sequence Annotation
 NP_BIND 142 148 GTP (Potential).
 MOD_RES 131 131 Phosphoserine; by BRSK1 (By similarity).  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 451 AA 
Protein Sequence
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY 60
IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD 120
IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD 180
VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST 240
TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP 300
KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL 360
SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQYDKLRK REAFLEQFRK EDMFKDNFDE 420
MDTSREIVQQ LIDEYHAATR PDYISWGTQE Q 451 
Gene Ontology
 GO:0045177; C:apical part of cell; IEA:Compara.
 GO:0031252; C:cell leading edge; IEA:Compara.
 GO:0005814; C:centriole; IEA:Compara.
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0000794; C:condensed nuclear chromosome; ISS:UniProtKB.
 GO:0005881; C:cytoplasmic microtubule; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000930; C:gamma-tubulin complex; TAS:UniProtKB.
 GO:0000242; C:pericentriolar material; IEA:Compara.
 GO:0005827; C:polar microtubule; IDA:UniProtKB.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0000212; P:meiotic spindle organization; ISS:UniProtKB.
 GO:0051258; P:protein polymerization; IEA:InterPro. 
Interpro
 IPR002454; Gamma_tubulin.
 IPR008280; Tub_FtsZ_C.
 IPR000217; Tubulin.
 IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
 IPR023123; Tubulin_C.
 IPR017975; Tubulin_CS.
 IPR003008; Tubulin_FtsZ_GTPase. 
Pfam
 PF00091; Tubulin
 PF03953; Tubulin_C 
SMART
 SM00864; Tubulin
 SM00865; Tubulin_C 
PROSITE
 PS00227; TUBULIN 
PRINTS
 PR01164; GAMMATUBULIN.
 PR01161; TUBULIN.