CANT1_HUMAN - dbPTM
CANT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CANT1_HUMAN
UniProt AC Q8WVQ1
Protein Name Soluble calcium-activated nucleotidase 1
Gene Name CANT1
Organism Homo sapiens (Human).
Sequence Length 401
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein . Golgi apparatus, Golgi stack membrane
Single-pass type II membrane protein . Cell membrane . Processed form: Secreted.
Protein Description Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. [PubMed: 12234496]
Protein Sequence MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLCSHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQEENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDVVNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPRRASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVALKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
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
14PhosphorylationEHPEWNESMHSLRIS
CCCCCCHHHHEEEEE		20.6925627689
17PhosphorylationEWNESMHSLRISVGG
CCCHHHHEEEEEECC		15.65-
21PhosphorylationSMHSLRISVGGLPVL
HHHEEEEEECCHHHH		14.3126657352
88N-linked_GlycosylationQAPANWYNDTYPLSP
CCCCCCCCCCCCCCC		27.11UniProtKB CARBOHYD
127PhosphorylationQEENTWFSYLKKGYL
HHHHCHHHHHHCCEE		22.5524719451
133PhosphorylationFSYLKKGYLTLSDSG
HHHHHCCEEEECCCC		12.8528102081
135PhosphorylationYLKKGYLTLSDSGDK
HHHCCEEEECCCCCE		18.7428102081
137PhosphorylationKKGYLTLSDSGDKVA
HCCEEEECCCCCEEE		25.21-
139PhosphorylationGYLTLSDSGDKVAVE
CEEEECCCCCEEEEE		45.58-
156PhosphorylationKDHGVLESHLAEKGR
CCCCHHHHHHHHCCC		21.46-
161UbiquitinationLESHLAEKGRGMELS
HHHHHHHCCCCCCHH		48.58-
202PhosphorylationAVPWVILSDGDGTVE
CCCEEEEECCCCCCC		28.55-
236O-linked_GlycosylationLGKEWTTTTGDVVNE
CCCCEECCCCCCCCC		22.77OGP
237O-linked_GlycosylationGKEWTTTTGDVVNEN
CCCEECCCCCCCCCC		29.32OGP
264PhosphorylationVDHENWVSNYNALRA
CCCCHHHHCHHHHHH		25.8030576142
303PhosphorylationFFLPRRASQERYSEK
HCCCCHHHCCHHCCC		30.6624719451
308PhosphorylationRASQERYSEKDDERK
HHHCCHHCCCCCCCH		44.3724719451
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 CANT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CANT1_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 CANT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLXA1_HUMANPLXNA1physical
26186194
ENTP6_HUMANENTPD6physical
26186194
LRIG1_HUMANLRIG1physical
26186194
ATF6B_HUMANATF6Bphysical
26186194
CELR1_HUMANCELSR1physical
26186194
ITA6_HUMANITGA6physical
26186194
TOIP2_HUMANTOR1AIP2physical
28514442
IFG15_HUMANTOR1AIP2physical
28514442
LRIG1_HUMANLRIG1physical
28514442
TGBR3_HUMANTGFBR3physical
28514442
ITA6_HUMANITGA6physical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CANT1_HUMAN

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Related Literatures of Post-Translational Modification

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