CBPC1_HUMAN - dbPTM
CBPC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CBPC1_HUMAN
UniProt AC Q9UPW5
Protein Name Cytosolic carboxypeptidase 1
Gene Name AGTPBP1
Organism Homo sapiens (Human).
Sequence Length 1226
Subcellular Localization Cytoplasm . Cytoplasm, cytosol . Nucleus . Mitochondrion . Localizes in both the cytoplasm and nuclei of interphase and dividing cells.
Protein Description Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5..
Protein Sequence MSKLKVIPEKSLTNNSRIVGLLAQLEKINAEPSESDTARYVTSKILHLAQSQEKTRREMTAKGSTGMEILLSTLENTKDLQTTLNILSILVELVSAGGGRRVSFLVTKGGSQILLQLLMNASKESPPHEDLMVQIHSILAKIGPKDKKFGVKARINGALNITLNLVKQNLQNHRLVLPCLQLLRVYSANSVNSVSLGKNGVVELMFKIIGPFSKKNSSLIKVALDTLAALLKSKTNARRAVDRGYVQVLLTIYVDWHRHDNRHRNMLIRKGILQSLKSVTNIKLGRKAFIDANGMKILYNTSQECLAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSSFHFQLPVIPVTGPVAQLYSLPPEVDDVVDESDDNDDIDVEAENETENEDDLDQNFKNDDIETDINKLKPQQEPGRTIEDLKMYEHLFPELVDDFQDYDLISKEPKPFVFEGKVRGPIVVPTAGEETSGNSGNLRKVVMKENISSKGDEGEKKSTFMDLAKEDIKDNDRTLQQQPGDQNRTISSVHGLNNDIVKALDRITLQNIPSQTAPGFTAEMKKDCSLPLTVLTCAKACPHMATCGNVLFEGRTVQLGKLCCTGVETEDDEDTESNSSVEQASVEVPDGPTLHDPDLYIEIVKNTKSVPEYSEVAYPDYFGHIPPPFKEPILERPYGVQRTKIAQDIERLIHQSDIIDRVVYDLDNPNYTIPEEGDILKFNSKFESGNLRKVIQIRKNEYDLILNSDINSNHYHQWFYFEVSGMRPGVAYRFNIINCEKSNSQFNYGMQPLMYSVQEALNARPWWIRMGTDICYYKNHFSRSSVAAGGQKGKSYYTITFTVNFPHKDDVCYFAYHYPYTYSTLQMHLQKLESAHNPQQIYFRKDVLCETLSGNSCPLVTITAMPESNYYEHICHFRNRPYVFLSARVHPGETNASWVMKGTLEYLMSNNPTAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPSPDLHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRKKNVFMYGCSIKETVWHTNDNATSCDVVEDTGYRTLPKILSHIAPAFCMSSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGCDQGKYKGLQIGTRELEEMGAKFCVGLLRLKRLTSPLEYNLPSSLLDFENDLIESSCKVTSPTTYVLDEDEPRFLEEVDYSAESNDELDIELAENVGDYEPSAQEEVLSDSELSRTYLP
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
10AcetylationKLKVIPEKSLTNNSR
CCEECCHHHCCCCHH		45.4725953088
10UbiquitinationKLKVIPEKSLTNNSR
CCEECCHHHCCCCHH		45.47-
44UbiquitinationTARYVTSKILHLAQS
HHHHHHHHHHHHHHC		39.6621890473
44 (in isoform 2)Ubiquitination-39.6621890473
44 (in isoform 1)Ubiquitination-39.6621890473
44UbiquitinationTARYVTSKILHLAQS
HHHHHHHHHHHHHHC		39.662189047
60PhosphorylationEKTRREMTAKGSTGM
HHHHHHHHHCCHHHH		22.06-
64PhosphorylationREMTAKGSTGMEILL
HHHHHCCHHHHHHHH		22.53-
65PhosphorylationEMTAKGSTGMEILLS
HHHHCCHHHHHHHHH		49.57-
96UbiquitinationILVELVSAGGGRRVS
HHHHHHHCCCCCEEE		17.1121890473
96UbiquitinationILVELVSAGGGRRVS
HHHHHHHCCCCCEEE		17.11-
103PhosphorylationAGGGRRVSFLVTKGG
CCCCCEEEEEEECCH		15.8528450419
106UbiquitinationGRRVSFLVTKGGSQI
CCEEEEEEECCHHHH		4.97-
155PhosphorylationKFGVKARINGALNIT
CCCCEEEECCHHHHH		7.15-
213PhosphorylationFKIIGPFSKKNSSLI
EEECCCCCCCCCHHH		45.9416674116
218PhosphorylationPFSKKNSSLIKVALD
CCCCCCCHHHHHHHH		43.4324719451
232UbiquitinationDTLAALLKSKTNARR
HHHHHHHHHCCCHHH		51.24-
265PhosphorylationRHDNRHRNMLIRKGI
HCCCHHHHHHHHHHH		24.40-
278PhosphorylationGILQSLKSVTNIKLG
HHHHHHHHHHCCCCC		39.19-
280PhosphorylationLQSLKSVTNIKLGRK
HHHHHHHHCCCCCCC		38.01-
310PhosphorylationQECLAVRTLDPLVNT
CHHHHEEECCCCCCH		28.9928152594
317PhosphorylationTLDPLVNTSSLIMRK
ECCCCCCHHHHHHHH		16.5328152594
318PhosphorylationLDPLVNTSSLIMRKC
CCCCCCHHHHHHHHH		20.2428152594
319PhosphorylationDPLVNTSSLIMRKCF
CCCCCHHHHHHHHHC		21.6329666759
329UbiquitinationMRKCFPKNRLPLPTI
HHHHCCCCCCCCCCC		51.46-
335UbiquitinationKNRLPLPTIKSSFHF
CCCCCCCCCCCEEEE		49.04-
544PhosphorylationITLQNIPSQTAPGFT
HCCCCCCCCCCCCCC		36.0422210691
546PhosphorylationLQNIPSQTAPGFTAE
CCCCCCCCCCCCCHH		38.8722210691
551PhosphorylationSQTAPGFTAEMKKDC
CCCCCCCCHHHCCCC		27.8522210691
584UbiquitinationCGNVLFEGRTVQLGK
CCCEEECCCEEEECC		24.19-
607UbiquitinationEDDEDTESNSSVEQA
CCCCCCCCCCCCEEE		44.07-
674UbiquitinationPYGVQRTKIAQDIER
CCCCCHHHHHHHHHH		37.93-
712UbiquitinationEEGDILKFNSKFESG
CCCCEEEECCCCCCC		12.83-
726UbiquitinationGNLRKVIQIRKNEYD
CCCEEEEEEECCCEE		32.21-
763UbiquitinationMRPGVAYRFNIINCE
CCCCEEEEEEEEEEC		14.38-
1007UbiquitinationLQYLAAVKRLPLVYC
HHHHHHHHHCCEEEE		43.41-
1059UbiquitinationTGYRTLPKILSHIAP
CCCCCHHHHHHHHHH		60.43-
1062PhosphorylationRTLPKILSHIAPAFC
CCHHHHHHHHHHHHH		19.1329888752
1071PhosphorylationIAPAFCMSSCSFVVE
HHHHHHHHCCCEEEE		29.4029888752
1072PhosphorylationAPAFCMSSCSFVVEK
HHHHHHHCCCEEEEC		6.2129888752
1074PhosphorylationAFCMSSCSFVVEKSK
HHHHHCCCEEEECCC		24.0329888752
1099PhosphorylationEIGVQRSYTMESTLC
ECCCCCEEECCCCCC		16.5828985074
1100PhosphorylationIGVQRSYTMESTLCG
CCCCCEEECCCCCCC		18.7328985074
1103PhosphorylationQRSYTMESTLCGCDQ
CCEEECCCCCCCCCC		18.8328985074
1121DimethylationKGLQIGTRELEEMGA
CCCCCCHHHHHHHHH		41.09-
1121MethylationKGLQIGTRELEEMGA
CCCCCCHHHHHHHHH		41.0924377081
1128PhosphorylationRELEEMGAKFCVGLL
HHHHHHHHHHHHHHH		10.6327251275
1131PhosphorylationEEMGAKFCVGLLRLK
HHHHHHHHHHHHHHH		2.0324719451
1141PhosphorylationLLRLKRLTSPLEYNL
HHHHHCCCCCCCCCC		32.1228450419
1142PhosphorylationLRLKRLTSPLEYNLP
HHHHCCCCCCCCCCC		31.8928464451
1146PhosphorylationRLTSPLEYNLPSSLL
CCCCCCCCCCCHHHH		29.6727732954
1150PhosphorylationPLEYNLPSSLLDFEN
CCCCCCCHHHHHCCH		36.4627732954
1151PhosphorylationLEYNLPSSLLDFEND
CCCCCCHHHHHCCHH		30.8927732954
1162PhosphorylationFENDLIESSCKVTSP
CCHHHHHHCCCCCCC		33.7626074081
1163PhosphorylationENDLIESSCKVTSPT
CHHHHHHCCCCCCCC		12.7426074081
1167PhosphorylationIESSCKVTSPTTYVL
HHHCCCCCCCCEEEC		17.9328176443
1168PhosphorylationESSCKVTSPTTYVLD
HHCCCCCCCCEEECC		24.2025159151
1170PhosphorylationSCKVTSPTTYVLDED
CCCCCCCCEEECCCC		30.4428176443
1171PhosphorylationCKVTSPTTYVLDEDE
CCCCCCCEEECCCCC		18.2828176443
1172PhosphorylationKVTSPTTYVLDEDEP
CCCCCCEEECCCCCC		11.0728796482
1206PhosphorylationLAENVGDYEPSAQEE
HHHHHCCCCCCHHHH		24.66-
1216PhosphorylationSAQEEVLSDSELSRT
CHHHHHCCCHHHHCC		44.2422468782
1219PhosphorylationEEVLSDSELSRTYLP
HHHCCCHHHHCCCCC		56.6119413330
1220PhosphorylationEVLSDSELSRTYLP-
HHCCCHHHHCCCCC-		4.9315302935
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 CBPC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CBPC1_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 CBPC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CYC_HUMANCYCSphysical
16713569
NYNRI_HUMANNYNRINphysical
16713569
CBY1_HUMANCBY1physical
16713569
LIPA1_HUMANPPFIA1physical
16713569
LIPA4_HUMANPPFIA4physical
16713569
ENOA_HUMANENO1physical
16713569
TTLL4_HUMANTTLL4physical
28514442
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 CBPC1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1168, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1167, AND MASSSPECTROMETRY.

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