CAH1_HUMAN - dbPTM
CAH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAH1_HUMAN
UniProt AC P00915
Protein Name Carbonic anhydrase 1
Gene Name CA1
Organism Homo sapiens (Human).
Sequence Length 261
Subcellular Localization Cytoplasm.
Protein Description Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea..
Protein Sequence MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF
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------MASPDWGYD
------CCCCCCCCC
29.764217196
30PhosphorylationIANGNNQSPVDIKTS
CCCCCCCCCCCCCCC
29.0727251275
36PhosphorylationQSPVDIKTSETKHDT
CCCCCCCCCCCCCCC
31.9330576142
43PhosphorylationTSETKHDTSLKPISV
CCCCCCCCCCCEEEE
35.3630576142
49PhosphorylationDTSLKPISVSYNPAT
CCCCCEEEEECCHHC
17.3423312004
51PhosphorylationSLKPISVSYNPATAK
CCCEEEEECCHHCHH
16.6428857561
56PhosphorylationSVSYNPATAKEIINV
EEECCHHCHHHHEEE
39.2530576142
78PhosphorylationFEDNDNRSVLKGGPF
CCCCCCCEEEECCCC
37.7527251275
86PhosphorylationVLKGGPFSDSYRLFQ
EEECCCCCCCEEEEE
28.8723025827
88PhosphorylationKGGPFSDSYRLFQFH
ECCCCCCCEEEEEEE
15.7922673903
89PhosphorylationGGPFSDSYRLFQFHF
CCCCCCCEEEEEEEE
19.14-
130PhosphorylationHWNSAKYSSLAEAAS
ECCCHHHHHHHHHHH
20.40-
130O-linked_GlycosylationHWNSAKYSSLAEAAS
ECCCHHHHHHHHHHH
20.4024126823
131PhosphorylationWNSAKYSSLAEAASK
CCCHHHHHHHHHHHH
28.6328857561
137PhosphorylationSSLAEAASKADGLAV
HHHHHHHHHCCCEEH
35.1127251275
218O-linked_GlycosylationIICKESISVSSEQLA
EEECCCCCCCHHHHH
25.8112556433
220PhosphorylationCKESISVSSEQLAQF
ECCCCCCCHHHHHHH
22.7427251275
221PhosphorylationKESISVSSEQLAQFR
CCCCCCCHHHHHHHH
27.4928857561
229PhosphorylationEQLAQFRSLLSNVEG
HHHHHHHHHHHCCCC
34.6427251275
232PhosphorylationAQFRSLLSNVEGDNA
HHHHHHHHCCCCCCC
44.0927251275
260PhosphorylationKGRTVRASF------
CCCEEEECC------
22.4123025827

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 CAH1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAH1_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 CAH1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHB7_HUMANHSD17B7physical
21988832
TFCP2_HUMANTFCP2physical
25416956

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
DB00819Acetazolamide
DB00381Amlodipine
DB00436Bendroflumethiazide
DB00562Benzthiazide
DB01194Brinzolamide
DB00880Chlorothiazide
DB00606Cyclothiazide
DB01119Diazoxide
DB01144Diclofenamide
DB00869Dorzolamide
DB01031Ethinamate
DB00999Hydrochlorothiazide
DB00774Hydroflumethiazide
DB00703Methazolamide
DB00423Methocarbamol
DB00232Methyclothiazide
DB01325Quinethazone
DB01021Trichlormethiazide
DB00909Zonisamide
Regulatory Network of CAH1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Human carbonic anhydrases. XII. The complete primary structure of theC isozyme.";
Lin K.-T.D., Deutsch H.F.;
J. Biol. Chem. 249:2329-2337(1974).
Cited for: SEQUENCE REVISION.

TOP