CNDP2_HUMAN - dbPTM
CNDP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNDP2_HUMAN
UniProt AC Q96KP4
Protein Name Cytosolic non-specific dipeptidase
Gene Name CNDP2
Organism Homo sapiens (Human).
Sequence Length 475
Subcellular Localization Cytoplasm .
Protein Description Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. [PubMed: 19346245 Acts as a functional tumor suppressor in gastric cancer via activation of the mitogen-activated protein kinase (MAPK) pathway. An elevated level of CNDP2 activates the p38 and JNK MAPK pathways to induce cell apoptosis, and a lower level of CNDP2 activates the ERK MAPK pathway to promote cell proliferation]
Protein Sequence MAALTTLFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDGSEIPLPPILLGRLGSDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVDKRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGSGAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFGVEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEVSQLKD
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
2Acetylation------MAALTTLFK
------CCHHHHHHH		15.9222223895
5Phosphorylation---MAALTTLFKYID
---CCHHHHHHHHHC		19.4121406692
6Phosphorylation--MAALTTLFKYIDE
--CCHHHHHHHHHCC		30.9229255136
9AcetylationAALTTLFKYIDENQD
CHHHHHHHHHCCCCH		44.3919608861
9UbiquitinationAALTTLFKYIDENQD
CHHHHHHHHHCCCCH		44.3933845483
17MethylationYIDENQDRYIKKLAK
HHCCCCHHHHHHHHH		25.88-
20AcetylationENQDRYIKKLAKWVA
CCCHHHHHHHHHHHH		32.5725953088
20UbiquitinationENQDRYIKKLAKWVA
CCCHHHHHHHHHHHH		32.5722817900
21UbiquitinationNQDRYIKKLAKWVAI
CCHHHHHHHHHHHHH		44.0822817900
24UbiquitinationRYIKKLAKWVAIQSV
HHHHHHHHHHHHHHC		53.2721890473
24 (in isoform 2)Ubiquitination-53.2721890473
24 (in isoform 1)Ubiquitination-53.2721890473
24AcetylationRYIKKLAKWVAIQSV
HHHHHHHHHHHHHHC		53.2725953088
24UbiquitinationRYIKKLAKWVAIQSV
HHHHHHHHHHHHHHC		53.2721890473
30PhosphorylationAKWVAIQSVSAWPEK
HHHHHHHHCCCCHHH		16.3628857561
32PhosphorylationWVAIQSVSAWPEKRG
HHHHHHCCCCHHHHH		29.8428857561
372-HydroxyisobutyrylationSVSAWPEKRGEIRRM
HCCCCHHHHHHHHHH		62.72-
37UbiquitinationSVSAWPEKRGEIRRM
HCCCCHHHHHHHHHH		62.7230230243
53UbiquitinationEVAAADVKQLGGSVE
HHHHHHHHHHCCEEE		40.1132015554
58PhosphorylationDVKQLGGSVELVDIG
HHHHHCCEEEEEECC		15.6028102081
66UbiquitinationVELVDIGKQKLPDGS
EEEEECCCCCCCCCC		44.5929967540
68UbiquitinationLVDIGKQKLPDGSEI
EEECCCCCCCCCCCC		66.5330230243
87PhosphorylationILLGRLGSDPQKKTV
HHHHCCCCCCCCCEE		51.1928857561
100UbiquitinationTVCIYGHLDVQPAAL
EEEEEEECCCCCHHH		6.3127667366
117UbiquitinationGWDSEPFTLVERDGK
CCCCCCEEEEEECCE		40.3823000965
118UbiquitinationWDSEPFTLVERDGKL
CCCCCEEEEEECCEE		3.7423000965
119UbiquitinationDSEPFTLVERDGKLY
CCCCEEEEEECCEEE		5.2823000965
124UbiquitinationTLVERDGKLYGRGST
EEEEECCEEECCCCC		42.7127667366
136UbiquitinationGSTDDKGPVAGWINA
CCCCCCCCHHHHHHH		20.6527667366
144UbiquitinationVAGWINALEAYQKTG
HHHHHHHHHHHHHHC		3.1521890473
149UbiquitinationNALEAYQKTGQEIPV
HHHHHHHHHCCCCCC		41.7821906983
163UbiquitinationVNVRFCLEGMEESGS
CCEEHHHHCCHHHCC		58.6421890473
190PhosphorylationTFFKDVDYVCISDNY
CCCCCCCEEEECCCE		9.3228064214
201UbiquitinationSDNYWLGKKKPCITY
CCCEECCCCCCCEEE		56.2923000965
202UbiquitinationDNYWLGKKKPCITYG
CCEECCCCCCCEEEC		61.2123000965
203UbiquitinationNYWLGKKKPCITYGL
CEECCCCCCCEEECC		48.9123000965
205UbiquitinationWLGKKKPCITYGLRG
ECCCCCCCEEECCCC		5.0829967540
207PhosphorylationGKKKPCITYGLRGIC
CCCCCCEEECCCCEE		20.4628857561
217UbiquitinationLRGICYFFIEVECSN
CCCEEEEEEEEEECC		1.5633845483
218UbiquitinationRGICYFFIEVECSNK
CCEEEEEEEEEECCC		4.0933845483
232PhosphorylationKDLHSGVYGGSVHEA
CCCCCCCCCCCHHHH		21.21-
255UbiquitinationGSLVDKRGNILIPGI
HHHHCCCCCEECCCH		31.1327667366
277PhosphorylationTEEEHKLYDDIDFDI
CHHHHHHHCCCCCCH		19.1727642862
289UbiquitinationFDIEEFAKDVGAQIL
CCHHHHHHHHCHHHH		59.2629967540
291UbiquitinationIEEFAKDVGAQILLH
HHHHHHHHCHHHHEE		7.2527667366
299UbiquitinationGAQILLHSHKKDILM
CHHHHEECCHHHEEE		36.6521890473
299PhosphorylationGAQILLHSHKKDILM
CHHHHEECCHHHEEE		36.6525159151
299 (in isoform 2)Ubiquitination-36.6521890473
3012-HydroxyisobutyrylationQILLHSHKKDILMHR
HHHEECCHHHEEEEC		55.97-
301UbiquitinationQILLHSHKKDILMHR
HHHEECCHHHEEEEC		55.9733845483
3022-HydroxyisobutyrylationILLHSHKKDILMHRW
HHEECCHHHEEEECC		44.57-
302UbiquitinationILLHSHKKDILMHRW
HHEECCHHHEEEECC		44.5733845483
311PhosphorylationILMHRWRYPSLSLHG
EEEECCCCCCCEEEC		7.1020090780
313PhosphorylationMHRWRYPSLSLHGIE
EECCCCCCCEEECCC		22.9628152594
315PhosphorylationRWRYPSLSLHGIEGA
CCCCCCCEEECCCCC		23.7428152594
318 (in isoform 2)Ubiquitination-25.5721890473
318UbiquitinationYPSLSLHGIEGAFSG
CCCCEEECCCCCCCC		25.5723000965
324PhosphorylationHGIEGAFSGSGAKTV
ECCCCCCCCCCCCCE		31.3620068231
326PhosphorylationIEGAFSGSGAKTVIP
CCCCCCCCCCCCEEE		34.0928857561
329AcetylationAFSGSGAKTVIPRKV
CCCCCCCCCEEECEE		47.0225953088
330PhosphorylationFSGSGAKTVIPRKVV
CCCCCCCCEEECEEE		24.1228857561
339UbiquitinationIPRKVVGKFSIRLVP
EECEEEEEEEEEECC		25.0727667366
341PhosphorylationRKVVGKFSIRLVPNM
CEEEEEEEEEECCCC		15.4128857561
346UbiquitinationKFSIRLVPNMTPEVV
EEEEEECCCCCHHHH		29.4829967540
348SulfoxidationSIRLVPNMTPEVVGE
EEEECCCCCHHHHHH		5.6030846556
358PhosphorylationEVVGEQVTSYLTKKF
HHHHHHHHHHHHHHH		16.0228348404
359PhosphorylationVVGEQVTSYLTKKFA
HHHHHHHHHHHHHHH		21.2028857561
362PhosphorylationEQVTSYLTKKFAELR
HHHHHHHHHHHHHCC		24.7728857561
363AcetylationQVTSYLTKKFAELRS
HHHHHHHHHHHHCCC		43.2125953088
363UbiquitinationQVTSYLTKKFAELRS
HHHHHHHHHHHHCCC		43.21-
366UbiquitinationSYLTKKFAELRSPNE
HHHHHHHHHCCCCCC		24.6429967540
370PhosphorylationKKFAELRSPNEFKVY
HHHHHCCCCCCCEEE		44.7128857561
375UbiquitinationLRSPNEFKVYMGHGG
CCCCCCCEEEECCCC		26.6927667366
377PhosphorylationSPNEFKVYMGHGGKP
CCCCCEEEECCCCCC		9.6622817900
383UbiquitinationVYMGHGGKPWVSDFS
EEECCCCCCCCCCCC		40.0623000965
383UbiquitinationVYMGHGGKPWVSDFS
EEECCCCCCCCCCCC		40.0621890473
383 (in isoform 1)Ubiquitination-40.0621890473
402UbiquitinationLAGRRAMKTVFGVEP
HCHHHHHHHHHCCCC		40.3221890473
402 (in isoform 1)Ubiquitination-40.3221890473
402UbiquitinationLAGRRAMKTVFGVEP
HCHHHHHHHHHCCCC		40.3223000965
402AcetylationLAGRRAMKTVFGVEP
HCHHHHHHHHHCCCC		40.3225953088
403PhosphorylationAGRRAMKTVFGVEPD
CHHHHHHHHHCCCCC		14.1628857561
412PhosphorylationFGVEPDLTREGGSIP
HCCCCCCCCCCCCCC		33.7728857561
417PhosphorylationDLTREGGSIPVTLTF
CCCCCCCCCCEEEEE		34.2828857561
421PhosphorylationEGGSIPVTLTFQEAT
CCCCCCEEEEEEECC		18.0928857561
430UbiquitinationTFQEATGKNVMLLPV
EEEECCCCCEEEEEE		41.8529967540
433SulfoxidationEATGKNVMLLPVGSA
ECCCCCEEEEEECCC		4.4330846556
439PhosphorylationVMLLPVGSADDGAHS
EEEEEECCCCCCCCC		28.8523911959
446PhosphorylationSADDGAHSQNEKLNR
CCCCCCCCCCHHHHC		33.88-
450UbiquitinationGAHSQNEKLNRYNYI
CCCCCCHHHHCCCCC		59.6229967540
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 CNDP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNDP2_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 CNDP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASSY_HUMANASS1physical
22863883
CAN1_HUMANCAPN1physical
22863883
CASP7_HUMANCASP7physical
22863883
KCRB_HUMANCKBphysical
22863883
DLDH_HUMANDLDphysical
22863883
G6PD_HUMANG6PDphysical
22863883
GBP2_HUMANGBP2physical
22863883
PSF2_HUMANGINS2physical
22863883
AGAL_HUMANGLAphysical
22863883
MVD1_HUMANMVDphysical
22863883
SIAS_HUMANNANSphysical
22863883
PEPD_HUMANPEPDphysical
22863883
RL23_HUMANRPL23physical
22863883
KS6A1_HUMANRPS6KA1physical
22863883
SCLY_HUMANSCLYphysical
22863883
NHRF1_HUMANSLC9A3R1physical
22863883
TGM2_HUMANTGM2physical
22863883
UBFD1_HUMANUBFD1physical
22863883
UBP14_HUMANUSP14physical
22863883
GDPP1_HUMANGDPGP1physical
26344197
NMRL1_HUMANNMRAL1physical
26344197
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 CNDP2_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-9, AND MASS SPECTROMETRY.

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