CAH2_HUMAN - dbPTM
CAH2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAH2_HUMAN
UniProt AC P00918
Protein Name Carbonic anhydrase 2
Gene Name CA2
Organism Homo sapiens (Human).
Sequence Length 260
Subcellular Localization Cytoplasm . Cell membrane . Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced c
Protein Description Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6..
Protein Sequence MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
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
2Phosphorylation------MSHHWGYGK
------CCCCCCCCC		24.8625849741
2Acetylation------MSHHWGYGK
------CCCCCCCCC		24.864207120
18AcetylationNGPEHWHKDFPIAKG
CCCCCCCCCCCCCCC		56.747306225
18UbiquitinationNGPEHWHKDFPIAKG
CCCCCCCCCCCCCCC		56.7421890473
29PhosphorylationIAKGERQSPVDIDTH
CCCCCCCCCCCCCCC		32.8625849741
35PhosphorylationQSPVDIDTHTAKYDP
CCCCCCCCCCCCCCC		22.81-
39UbiquitinationDIDTHTAKYDPSLKP
CCCCCCCCCCCCCCC		51.8721890473
39AcetylationDIDTHTAKYDPSLKP
CCCCCCCCCCCCCCC		51.8725038526
40PhosphorylationIDTHTAKYDPSLKPL
CCCCCCCCCCCCCCC		30.5326437602
43PhosphorylationHTAKYDPSLKPLSVS
CCCCCCCCCCCCCEE		46.2422673903
45UbiquitinationAKYDPSLKPLSVSYD
CCCCCCCCCCCEECC		48.5321890473
48PhosphorylationDPSLKPLSVSYDQAT
CCCCCCCCEECCCHH		19.9726657352
50PhosphorylationSLKPLSVSYDQATSL
CCCCCCEECCCHHEE		21.4426657352
51PhosphorylationLKPLSVSYDQATSLR
CCCCCEECCCHHEEE		15.2126657352
55PhosphorylationSVSYDQATSLRILNN
CEECCCHHEEEECCC		23.7422673903
56PhosphorylationVSYDQATSLRILNNG
EECCCHHEEEECCCC		20.7522673903
80UbiquitinationSQDKAVLKGGPLDGT
CCCCEEEECCCCCCE		56.0521890473
87PhosphorylationKGGPLDGTYRLIQFH
ECCCCCCEEEEEEEE		12.7228857561
99PhosphorylationQFHFHWGSLDGQGSE
EEEEECCCCCCCCCC		20.35-
113AcetylationEHTVDKKKYAAELHL
CEECCHHHHEEEEEE		45.9525038526
114PhosphorylationHTVDKKKYAAELHLV
EECCHHHHEEEEEEE		21.6626437602
151PhosphorylationGIFLKVGSAKPGLQK
EEEEEECCCCCCHHH		35.7926657352
158UbiquitinationSAKPGLQKVVDVLDS
CCCCCHHHHHHHHHH		49.6321890473
165PhosphorylationKVVDVLDSIKTKGKS
HHHHHHHHHHCCCCC		23.0924275569
172PhosphorylationSIKTKGKSADFTNFD
HHHCCCCCCCCCCCC		41.568218160
216PhosphorylationIVLKEPISVSSEQVL
EEECCCCCCCHHHEE		27.0226657352
218PhosphorylationLKEPISVSSEQVLKF
ECCCCCCCHHHEEEE		22.7425693802
219PhosphorylationKEPISVSSEQVLKFR
CCCCCCCHHHEEEEE		29.8725693802
224UbiquitinationVSSEQVLKFRKLNFN
CCHHHEEEEECCCCC		44.2421890473
258PhosphorylationKNRQIKASFK-----
CCCCCCCCCC-----		28.6824719451
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 CAH2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAH2_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 CAH2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
S4A8_HUMANSLC4A8physical
14736710
SL9A1_HUMANSLC9A1physical
12138085
CH60_HUMANHSPD1physical
9890926
B3AT_HUMANSLC4A1physical
11606574
NONO_HUMANNONOphysical
10821857
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
259730Osteopetrosis, autosomal recessive 3 (OPTB3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00819Acetazolamide
DB00436Bendroflumethiazide
DB00562Benzthiazide
DB01194Brinzolamide
DB00880Chlorothiazide
DB00606Cyclothiazide
DB01119Diazoxide
DB01144Diclofenamide
DB00869Dorzolamide
DB01031Ethinamate
DB00695Furosemide
DB00999Hydrochlorothiazide
DB00774Hydroflumethiazide
DB00703Methazolamide
DB00232Methyclothiazide
DB01325Quinethazone
DB00273Topiramate
DB01021Trichlormethiazide
DB00909Zonisamide
Regulatory Network of CAH2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Primary structure of human carbonic anhydrase C.";
Henderson L.E., Henriksson D., Nyman P.O.;
J. Biol. Chem. 251:5457-5463(1976).
Cited for: PROTEIN SEQUENCE OF 2-260.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory