CLIP3_HUMAN - dbPTM
CLIP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLIP3_HUMAN
UniProt AC Q96DZ5
Protein Name CAP-Gly domain-containing linker protein 3
Gene Name CLIP3
Organism Homo sapiens (Human).
Sequence Length 547
Subcellular Localization Cell membrane
Lipid-anchor . Cytoplasm . Golgi apparatus, Golgi stack . Localized to Golgi stacks as well as on tubulovesicular elements juxtaposed to Golgi cisternae.
Protein Description Functions as a cytoplasmic linker protein. Involved in TGN-endosome dynamics. May modulate the cellular compartmentalization of AKT kinase family and promote its cell membrane localization, thereby playing a role in glucose transport in adipocytes..
Protein Sequence MTKTDPAPMAPPPRGEEEEEEEEDEPVPEAPSPTQERRQKPVVHPSAPAPLPKDYAFTFFDPNDPACQEILFDPQTTIPELFAIVRQWVPQVQHKIDVIGNEILRRGCHVNDRDGLTDMTLLHYACKAGAHGVGDPAAAVRLSQQLLALGADVTLRSRWTNMNALHYAAYFDVPDLVRVLLKGARPRVVNSTCSDFNHGSALHIAASSLCLGAAKCLLEHGANPALRNRKGQVPAEVVPDPMDMSLDKAEAALVAKELRTLLEEAVPLSCALPKVTLPNYDNVPGNLMLSALGLRLGDRVLLDGQKTGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLFASVSKISKAVDAPPSSVTSTPRTPRMDFSRVTGKGRREHKGKKKTPSSPSLGSLQQRDGAKAEVGDQVLVAGQKQGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCPPRHGVFAPASRIQRIGGSTDSPGDSVGAKKVHQVTMTQPKRTFTTVRTPKDIASENSISRLLFCCWFPWMLRAEMQS
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
32PhosphorylationEPVPEAPSPTQERRQ
CCCCCCCCCCCHHCC		47.8528176443
34PhosphorylationVPEAPSPTQERRQKP
CCCCCCCCCHHCCCC		47.6128176443
95UbiquitinationWVPQVQHKIDVIGNE
HHHHHCHHHEEECHH		24.4230230243
127UbiquitinationTLLHYACKAGAHGVG
HHHHHHHHCCCCCCC		41.50-
154PhosphorylationLALGADVTLRSRWTN
HHCCCCEEEHHHCCC		19.5924719451
245PhosphorylationVPDPMDMSLDKAEAA
CCCCCCCCCCHHHHH		29.20-
256UbiquitinationAEAALVAKELRTLLE
HHHHHHHHHHHHHHH		50.2129967540
260PhosphorylationLVAKELRTLLEEAVP
HHHHHHHHHHHHHHC		48.6022210691
269PhosphorylationLEEAVPLSCALPKVT
HHHHHCCCCCCCCEE		7.4122210691
276PhosphorylationSCALPKVTLPNYDNV
CCCCCCEECCCCCCC		42.4926356563
280PhosphorylationPKVTLPNYDNVPGNL
CCEECCCCCCCCCCH		13.6226356563
290PhosphorylationVPGNLMLSALGLRLG
CCCCHHHHHHCCEEC		13.9022210691
306UbiquitinationRVLLDGQKTGTLRFC
EEEECCCCCEEEEEC		55.2230230243
362UbiquitinationASVSKISKAVDAPPS
EEHHHHHCCCCCCCC		56.7730230243
369PhosphorylationKAVDAPPSSVTSTPR
CCCCCCCCCCCCCCC		36.0626434776
370PhosphorylationAVDAPPSSVTSTPRT
CCCCCCCCCCCCCCC		34.8826434776
372PhosphorylationDAPPSSVTSTPRTPR
CCCCCCCCCCCCCCC		28.9127732954
373PhosphorylationAPPSSVTSTPRTPRM
CCCCCCCCCCCCCCC		33.9724732914
374PhosphorylationPPSSVTSTPRTPRMD
CCCCCCCCCCCCCCC		13.8727732954
377PhosphorylationSVTSTPRTPRMDFSR
CCCCCCCCCCCCHHH		19.2227732954
386PhosphorylationRMDFSRVTGKGRREH
CCCHHHCCCCCCCCC		31.87-
399PhosphorylationEHKGKKKTPSSPSLG
CCCCCCCCCCCCCHH		36.9623403867
401PhosphorylationKGKKKTPSSPSLGSL
CCCCCCCCCCCHHHH		61.1823403867
402PhosphorylationGKKKTPSSPSLGSLQ
CCCCCCCCCCHHHHH		21.5123403867
404PhosphorylationKKTPSSPSLGSLQQR
CCCCCCCCHHHHHHC		47.5123403867
407PhosphorylationPSSPSLGSLQQRDGA
CCCCCHHHHHHCCCC		28.4420230923
428UbiquitinationQVLVAGQKQGIVRFY
EEEECCCCCEEEEEE		49.9629967540
456UbiquitinationELDQPTGKHDGSVFG
EECCCCCCCCCCEEE		40.79-
466PhosphorylationGSVFGVRYFTCPPRH
CCEEEEEEEECCCCC		10.7929759185
480PhosphorylationHGVFAPASRIQRIGG
CCCEECHHHEEEECC		28.9329759185
488PhosphorylationRIQRIGGSTDSPGDS
HEEEECCCCCCCCCC		24.6727732954
489PhosphorylationIQRIGGSTDSPGDSV
EEEECCCCCCCCCCC		43.7127732954
491PhosphorylationRIGGSTDSPGDSVGA
EECCCCCCCCCCCCC		30.7630576142
495PhosphorylationSTDSPGDSVGAKKVH
CCCCCCCCCCCEEEE		28.5027732954
499UbiquitinationPGDSVGAKKVHQVTM
CCCCCCCEEEEEEEE		49.7722505724
500UbiquitinationGDSVGAKKVHQVTMT
CCCCCCEEEEEEEEC		44.4029967540
505PhosphorylationAKKVHQVTMTQPKRT
CEEEEEEEECCCCCE		14.1329449344
507PhosphorylationKVHQVTMTQPKRTFT
EEEEEEECCCCCEEE		32.1429449344
510UbiquitinationQVTMTQPKRTFTTVR
EEEECCCCCEEEECC		55.0129967540
512PhosphorylationTMTQPKRTFTTVRTP
EECCCCCEEEECCCH		31.3129449344
514PhosphorylationTQPKRTFTTVRTPKD
CCCCCEEEECCCHHH		24.6229449344
515PhosphorylationQPKRTFTTVRTPKDI
CCCCEEEECCCHHHH		12.0929449344
520UbiquitinationFTTVRTPKDIASENS
EEECCCHHHHCCCCH		62.2432142685
534S-palmitoylationSISRLLFCCWFPWML
HHHHHHHHHHHHHHH		1.7024001771
535S-palmitoylationISRLLFCCWFPWMLR
HHHHHHHHHHHHHHH		3.0824001771
547PhosphorylationMLRAEMQS-------
HHHHHHCC-------		40.66-
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 CLIP3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLIP3_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 CLIP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TNR1A_HUMANTNFRSF1Aphysical
22297296
TNR21_HUMANTNFRSF21physical
22297296
CYLD_HUMANCYLDphysical
22297296
AKT1_HUMANAKT1physical
19139280
AKT2_HUMANAKT2physical
19139280
SPDYA_HUMANSPDYAphysical
26017671
CYLD_HUMANCYLDphysical
26017671
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 CLIP3_HUMAN

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Related Literatures of Post-Translational Modification

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