GCP2_HUMAN - dbPTM
GCP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GCP2_HUMAN
UniProt AC Q9BSJ2
Protein Name Gamma-tubulin complex component 2
Gene Name TUBGCP2
Organism Homo sapiens (Human).
Sequence Length 902
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Description Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome..
Protein Sequence MSEFRIHHDVNELLSLLRVHGGDGAEVYIDLLQKNRTPYVTTTVSAHSAKVKIAEFSRTPEDFLKKYDELKSKNTRNLDPLVYLLSKLTEDKETLQYLQQNAKERAELAAAAVGSSTTSINVPAAASKISMQELEELRKQLGSVATGSTLQQSLELKRKMLRDKQNKKNSGQHLPIFPAWVYERPALIGDFLIGAGISTDTALPIGTLPLASQESAVVEDLLYVLVGVDGRYVSAQPLAGRQSRTFLVDPNLDLSIRELVHRILPVAASYSAVTRFIEEKSSFEYGQVNHALAAAMRTLVKEHLILVSQLEQLHRQGLLSLQKLWFYIQPAMRTMDILASLATSVDKGECLGGSTLSLLHDRSFSYTGDSQAQELCLYLTKAASAPYFEVLEKWIYRGIIHDPYSEFMVEEHELRKERIQEDYNDKYWDQRYTIVQQQIPSFLQKMADKILSTGKYLNVVRECGHDVTCPVAKEIIYTLKERAYVEQIEKAFNYASKVLLDFLMEEKELVAHLRSIKRYFLMDQGDFFVHFMDLAEEELRKPVEDITPPRLEALLELALRMSTANTDPFKDDLKIDLMPHDLITQLLRVLAIETKQEKAMAHADPTELALSGLEAFSFDYIVKWPLSLIINRKALTRYQMLFRHMFYCKHVERQLCSVWISNKTAKQHSLHSAQWFAGAFTLRQRMLNFVQNIQYYMMFEVMEPTWHILEKNLKSASNIDDVLGHHTGFLDTCLKDCMLTNPELLKVFSKLMSVCVMFTNCMQKFTQSMKLDGELGGQTLEHSTVLGLPAGAEERARKELARKHLAEHADTVQLVSGFEATINKFDKNFSAHLLDLLARLSIYSTSDCEHGMASVISRLDFNGFYTERLERLSAERSQKATPQVPVLRGPPAPAPRVAVTAQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSEFRIHHD
------CCCCCCCCC		45.5024043423
15PhosphorylationHDVNELLSLLRVHGG
CCHHHHHHHHHHCCC		37.6724043423
37PhosphorylationDLLQKNRTPYVTTTV
HHHHCCCCCCEEEEE		28.5028555341
39PhosphorylationLQKNRTPYVTTTVSA
HHCCCCCCEEEEEEH		15.1527642862
50AcetylationTVSAHSAKVKIAEFS
EEEHHHCEEEEHHHC		47.2625953088
65UbiquitinationRTPEDFLKKYDELKS
CCHHHHHHHHHHHHC		49.64-
83PhosphorylationRNLDPLVYLLSKLTE
CCCHHHHHHHHHHCC		15.0322115753
86PhosphorylationDPLVYLLSKLTEDKE
HHHHHHHHHHCCCHH		24.0320068231
92UbiquitinationLSKLTEDKETLQYLQ
HHHHCCCHHHHHHHH		46.49-
103UbiquitinationQYLQQNAKERAELAA
HHHHHHHHHHHHHHH		56.11-
130PhosphorylationPAAASKISMQELEEL
CHHHHCCCHHHHHHH		20.3928555341
131SulfoxidationAAASKISMQELEELR
HHHHCCCHHHHHHHH		4.0121406390
148PhosphorylationLGSVATGSTLQQSLE
HCCCCCCCHHHHHHH		22.9128348404
149PhosphorylationGSVATGSTLQQSLEL
CCCCCCCHHHHHHHH		29.9028348404
153PhosphorylationTGSTLQQSLELKRKM
CCCHHHHHHHHHHHH		15.7328348404
157UbiquitinationLQQSLELKRKMLRDK
HHHHHHHHHHHHHHH		40.37-
182PhosphorylationPIFPAWVYERPALIG
CCCCHHHHCCCHHHC		8.7727642862
243PhosphorylationQPLAGRQSRTFLVDP
CCCCCCCCCEEEECC		31.7428348404
255PhosphorylationVDPNLDLSIRELVHR
ECCCCCCCHHHHHHH		21.1924719451
320PhosphorylationLHRQGLLSLQKLWFY
HHHCCCCHHHHHHHH		33.5224719451
426UbiquitinationIQEDYNDKYWDQRYT
HHHHCCHHHHHHHHH		44.6021890473
445UbiquitinationQIPSFLQKMADKILS
HHHHHHHHHHHHHHH		37.90-
449UbiquitinationFLQKMADKILSTGKY
HHHHHHHHHHHCCCH		35.69-
455UbiquitinationDKILSTGKYLNVVRE
HHHHHCCCHHHHHHH		46.8021890473
455UbiquitinationDKILSTGKYLNVVRE
HHHHHCCCHHHHHHH		46.8021890473
455UbiquitinationDKILSTGKYLNVVRE
HHHHHCCCHHHHHHH		46.8021890473
468PhosphorylationRECGHDVTCPVAKEI
HHHCCCCCCHHHHHH		19.70-
473AcetylationDVTCPVAKEIIYTLK
CCCCHHHHHHHHHHH		50.0826051181
477PhosphorylationPVAKEIIYTLKERAY
HHHHHHHHHHHHHHH		16.2229514088
478PhosphorylationVAKEIIYTLKERAYV
HHHHHHHHHHHHHHH		22.4229514088
480UbiquitinationKEIIYTLKERAYVEQ
HHHHHHHHHHHHHHH		37.04-
483UbiquitinationIYTLKERAYVEQIEK
HHHHHHHHHHHHHHH		17.5121890473
490UbiquitinationAYVEQIEKAFNYASK
HHHHHHHHHHHHHHH		60.96-
504SulfoxidationKVLLDFLMEEKELVA
HHHHHHHHHHHHHHH		6.7121406390
547PhosphorylationRKPVEDITPPRLEAL
CCCHHHCCHHHHHHH		39.2924719451
584PhosphorylationLMPHDLITQLLRVLA
CCCHHHHHHHHHHHH		22.06-
594PhosphorylationLRVLAIETKQEKAMA
HHHHHHHHHHHHHHH		31.73-
595UbiquitinationRVLAIETKQEKAMAH
HHHHHHHHHHHHHHC		43.60-
606PhosphorylationAMAHADPTELALSGL
HHHCCCHHHHHHHHH		44.1520860994
636PhosphorylationIINRKALTRYQMLFR
HCCHHHHHHHHHHHH		31.9926074081
638PhosphorylationNRKALTRYQMLFRHM
CHHHHHHHHHHHHHH		7.9526074081
681PhosphorylationQWFAGAFTLRQRMLN
HHHHHHHHHHHHHHH		22.0924719451
697AcetylationVQNIQYYMMFEVMEP
HHHHHHHHHHHCCCC		1.7919608861
714UbiquitinationHILEKNLKSASNIDD
HHHHHHHHCCCCHHH		54.06-
735UbiquitinationGFLDTCLKDCMLTNP
CHHHHHHHHHHCCCH		51.53-
803UbiquitinationARKELARKHLAEHAD
HHHHHHHHHHHHCCC		37.05-
827AcetylationATINKFDKNFSAHLL
HHHHHCCCCHHHHHH		64.1319608861
841PhosphorylationLDLLARLSIYSTSDC
HHHHHHHCCCCCCCC		17.5829978859
843PhosphorylationLLARLSIYSTSDCEH
HHHHHCCCCCCCCCC		11.5229978859
844PhosphorylationLARLSIYSTSDCEHG
HHHHCCCCCCCCCCC		21.5529978859
845PhosphorylationARLSIYSTSDCEHGM
HHHCCCCCCCCCCCC		16.1829978859
846PhosphorylationRLSIYSTSDCEHGMA
HHCCCCCCCCCCCCC		34.0329978859
855AcetylationCEHGMASVISRLDFN
CCCCCCHHHHHHCCC		3.1519608861
873PhosphorylationTERLERLSAERSQKA
HHHHHHHCHHHHHCC		34.0120860994
877PhosphorylationERLSAERSQKATPQV
HHHCHHHHHCCCCCC		27.7728555341
879UbiquitinationLSAERSQKATPQVPV
HCHHHHHCCCCCCCC		56.31-
881PhosphorylationAERSQKATPQVPVLR
HHHHHCCCCCCCCCC		22.6820860994
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of GCP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GCP2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GCP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCP3_HUMANTUBGCP3physical
23886939
ACTB_HUMANACTBphysical
23443559
ATD3A_HUMANATAD3Aphysical
23443559
BAG2_HUMANBAG2physical
23443559
MZT1_HUMANMZT1physical
23443559
UQCC2_HUMANUQCC2physical
23443559
CPNS1_HUMANCAPNS1physical
23443559
TBB5_HUMANTUBBphysical
23443559
DDB1_HUMANDDB1physical
23443559
EF1A1_HUMANEEF1A1physical
23443559
EMD_HUMANEMDphysical
23443559
TBB4A_HUMANTUBB4Aphysical
23443559
MZT2A_HUMANMZT2Aphysical
23443559
MZT2B_HUMANMZT2Bphysical
23443559
HAX1_HUMANHAX1physical
23443559
HS90B_HUMANHSP90AB1physical
23443559
GRP78_HUMANHSPA5physical
23443559
HSP7C_HUMANHSPA8physical
23443559
GRP75_HUMANHSPA9physical
23443559
IF2B1_HUMANIGF2BP1physical
23443559
NDK7_HUMANNME7physical
23443559
KPB1_HUMANPHKA1physical
23443559
KPB2_HUMANPHKA2physical
23443559
PRP4_HUMANPRPF4physical
23443559
SYRC_HUMANRARSphysical
23443559
RL11_HUMANRPL11physical
23443559
RLA2_HUMANRPLP2physical
23443559
RS19_HUMANRPS19physical
23443559
RS20_HUMANRPS20physical
23443559
RS3_HUMANRPS3physical
23443559
SCO2_HUMANSCO2physical
23443559
TBA1A_HUMANTUBA1Aphysical
23443559
TBA1B_HUMANTUBA1Bphysical
23443559
TBA4A_HUMANTUBA4Aphysical
23443559
TBB2A_HUMANTUBB2Aphysical
23443559
TBB4B_HUMANTUBB4Bphysical
23443559
TBG1_HUMANTUBG1physical
23443559
GCP3_HUMANTUBGCP3physical
23443559
GCP4_HUMANTUBGCP4physical
23443559
GCP5_HUMANTUBGCP5physical
23443559
GCP6_HUMANTUBGCP6physical
23443559
UBB_HUMANUBBphysical
23443559
MZT2B_HUMANMZT2Bphysical
26344197
GCP6_HUMANTUBGCP6physical
26344197
LG3BP_HUMANLGALS3BPphysical
26496610
RAD51_HUMANRAD51physical
26496610
TBG1_HUMANTUBG1physical
26496610
XPO1_HUMANXPO1physical
26496610
GCP3_HUMANTUBGCP3physical
26496610
SRS10_HUMANSRSF10physical
26496610
WWP2_HUMANWWP2physical
26496610
GCP4_HUMANTUBGCP4physical
26496610
NDK7_HUMANNME7physical
26496610
MZT2B_HUMANMZT2Bphysical
26496610
GCP6_HUMANTUBGCP6physical
26496610
GCP5_HUMANTUBGCP5physical
26496610
NEDD1_HUMANNEDD1physical
26496610
MZT1_HUMANMZT1physical
26496610
MZT2A_HUMANMZT2Aphysical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GCP2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-827, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-83, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-83, AND MASSSPECTROMETRY.

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