CAH9_HUMAN - dbPTM
CAH9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAH9_HUMAN
UniProt AC Q16790
Protein Name Carbonic anhydrase 9
Gene Name CA9
Organism Homo sapiens (Human).
Sequence Length 459
Subcellular Localization Nucleus . Nucleus, nucleolus . Cell membrane
Single-pass type I membrane protein . Cell projection, microvillus membrane
Single-pass type I membrane protein . Found on the surface microvilli and in the nucleus, particularly in nucleolus.
Protein Description Reversible hydration of carbon dioxide. Participates in pH regulation. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia..
Protein Sequence MAPLCPSPWLPLLIPAPAPGLTVQLLLSLLLLVPVHPQRLPRMQEDSPLGGGSSGEDDPLGEEDLPSEEDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGSLKLEDLPTVEAPGDPQEPQNNAHRDKEGDDQSHWRYGGDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPGREYRALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQLNFRATQPLNGRVIEASFPAGVDSSPRAAEPVQLNSCLAAGDILALVFGLLFAVTSVAFLVQMRRQHRRGTKGGVSYRPAEVAETGA
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
47PhosphorylationLPRMQEDSPLGGGSS
CCCCCCCCCCCCCCC		22.6726657352
53PhosphorylationDSPLGGGSSGEDDPL
CCCCCCCCCCCCCCC		38.1426657352
54PhosphorylationSPLGGGSSGEDDPLG
CCCCCCCCCCCCCCC		49.8526657352
67PhosphorylationLGEEDLPSEEDSPRE
CCCCCCCCCCCCCCC		62.0026657352
71PhosphorylationDLPSEEDSPREEDPP
CCCCCCCCCCCCCCC		29.1826657352
102PhosphorylationLPEVKPKSEEEGSLK
CCCCCCCCCCCCCCC		59.7826657352
107PhosphorylationPKSEEEGSLKLEDLP
CCCCCCCCCCHHCCC		26.1328857561
115O-linked_GlycosylationLKLEDLPTVEAPGDP
CCHHCCCCCCCCCCC		37.9718703501
304PhosphorylationEEIAEEGSETQVPGL
HHHHHHCCCCCCCCC		40.5322210691
306PhosphorylationIAEEGSETQVPGLDI
HHHHCCCCCCCCCCH		36.2422210691
346N-linked_GlycosylationGVIWTVFNQTVMLSA
CCHHHHCCCEEEECH		32.0718703501
443PhosphorylationRRQHRRGTKGGVSYR
HHHHHCCCCCCCCCC		25.3822037869
448PhosphorylationRGTKGGVSYRPAEVA
CCCCCCCCCCHHHHH		20.7825463755
449PhosphorylationGTKGGVSYRPAEVAE
CCCCCCCCCHHHHHC		20.438084592
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
443TPhosphorylationKinasePRKACAP17612
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAH9_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 CAH9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
14567991
CADH1_HUMANCDH1physical
14567991
CTNA1_HUMANCTNNA1physical
14567991
FLOT1_HUMANFLOT1physical
22939629
CAND1_HUMANCAND1physical
23181366
G3BP2_HUMANG3BP2physical
23181366
ATPA_HUMANATP5A1physical
23181366
ATPB_HUMANATP5Bphysical
23181366
RTCB_HUMANRTCBphysical
23181366
RS5_HUMANRPS5physical
23181366
CAND2_HUMANCAND2physical
23181366
ACACA_HUMANACACAphysical
23181366
IPO9_HUMANIPO9physical
23181366
IPO4_HUMANIPO4physical
23181366
IPO5_HUMANIPO5physical
23181366
IPO7_HUMANIPO7physical
23181366
IMA1_HUMANKPNA2physical
23181366
XPO5_HUMANXPO5physical
23181366
XPOT_HUMANXPOTphysical
23181366
XPO2_HUMANCSE1Lphysical
23181366
XPO1_HUMANXPO1physical
23181366
TNPO3_HUMANTNPO3physical
23181366
TNPO1_HUMANTNPO1physical
23181366
ATX10_HUMANATXN10physical
23181366
CAH2_HUMANCA2physical
23181366
HEAT3_HUMANHEATR3physical
23181366
SAAL1_HUMANSAAL1physical
23181366
SRPRB_HUMANSRPRBphysical
23181366
ECHA_HUMANHADHAphysical
23181366
Drug and Disease Associations
Kegg Disease
H00021 Renal cell carcinoma
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D00218 Acetazolamide (JP16/USP/INN); Diamox (TN)
D00219 Acetohexamide (JP16/USP/INN); Dymelor (TN)
D00518 Diclofenamide (JP16/INN); Dichlorphenamide (USP); Daranide (TN)
D00652 Brinzolamide (JAN/USP/INN); Azopt (TN)
D00653 Dorzolamide hydrochloride (JP16/USP); Trusopt (TN)
D00655 Methazolamide (JAN/USP/INN); Neptazane (TN)
D01196 Acetazolamide sodium (JAN); Diamox (TN)
D01822 Clofenamide (JAN/INN)
D02441 Ethoxzolamide; Cardrase (TN)
D03845 Sezolamide hydrochloride (USAN)
D07871 Dorzolamide (INN); Trusopt (TN)
D09593 Girentuximab (USAN/INN)
D09632 Iodine (124I) girentuximab (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAH9_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structure of the catalytic domain of the tumor-associatedhuman carbonic anhydrase IX.";
Alterio V., Hilvo M., Di Fiore A., Supuran C.T., Pan P., Parkkila S.,Scaloni A., Pastorek J., Pastorekova S., Pedone C., Scozzafava A.,Monti S.M., De Simone G.;
Proc. Natl. Acad. Sci. U.S.A. 106:16233-16238(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 137-391 IN COMPLEX WITH ZINCION AND THE INHIBITOR ACETAZOLAMIDE, GLYCOSYLATION AT ASN-346,DISULFIDE BOND, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
"Biochemical characterization of CA IX, one of the most activecarbonic anhydrase isozymes.";
Hilvo M., Baranauskiene L., Salzano A.M., Scaloni A., Matulis D.,Innocenti A., Scozzafava A., Monti S.M., Di Fiore A., De Simone G.,Lindfors M., Janis J., Valjakka J., Pastorekova S., Pastorek J.,Kulomaa M.S., Nordlund H.R., Supuran C.T., Parkkila S.;
J. Biol. Chem. 283:27799-27809(2008).
Cited for: FUNCTION, SUBUNIT, INDUCTION, GLYCOSYLATION AT THR-115 AND ASN-346,AND DISULFIDE BONDS.
O-linked Glycosylation
ReferencePubMed
"Biochemical characterization of CA IX, one of the most activecarbonic anhydrase isozymes.";
Hilvo M., Baranauskiene L., Salzano A.M., Scaloni A., Matulis D.,Innocenti A., Scozzafava A., Monti S.M., Di Fiore A., De Simone G.,Lindfors M., Janis J., Valjakka J., Pastorekova S., Pastorek J.,Kulomaa M.S., Nordlund H.R., Supuran C.T., Parkkila S.;
J. Biol. Chem. 283:27799-27809(2008).
Cited for: FUNCTION, SUBUNIT, INDUCTION, GLYCOSYLATION AT THR-115 AND ASN-346,AND DISULFIDE BONDS.
Phosphorylation
ReferencePubMed
"The role of carbonic anhydrase IX overexpression in kidney cancer.";
Dorai T., Sawczuk I.S., Pastorek J., Wiernik P.H., Dutcher J.P.;
Eur. J. Cancer 41:2935-2947(2005).
Cited for: PHOSPHORYLATION AT TYR-449.

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