AQP1_HUMAN - dbPTM
AQP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AQP1_HUMAN
UniProt AC P29972
Protein Name Aquaporin-1
Gene Name AQP1
Organism Homo sapiens (Human).
Sequence Length 269
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient..
Protein Sequence MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLTGNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK
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
42N-linked_GlycosylationFKYPVGNNQTAVQDN
CCCCCCCCCCCCCCC
34.35UniProtKB CARBOHYD
157PhosphorylationVLCVLATTDRRRRDL
HHHHHHCCCHHHHHC
23.1522817900
167PhosphorylationRRRDLGGSAPLAIGL
HHHHCCCCCCHHHHH
25.5525332170
175PhosphorylationAPLAIGLSVALGHLL
CCHHHHHHHHHHHHH
10.5125332170
205N-linked_GlycosylationGSAVITHNFSNHWIF
CCEEEEECCCCCEEE
33.13UniProtKB CARBOHYD
236O-linked_GlycosylationFILAPRSSDLTDRVK
HHHCCCCCCCCCCEE
37.6112623621
236PhosphorylationFILAPRSSDLTDRVK
HHHCCCCCCCCCCEE
37.61-
239PhosphorylationAPRSSDLTDRVKVWT
CCCCCCCCCCEEEEC
27.1028857561
246PhosphorylationTDRVKVWTSGQVEEY
CCCEEEECCCCEEEE
26.4323403867
247PhosphorylationDRVKVWTSGQVEEYD
CCEEEECCCCEEEEE
16.1226657352
253PhosphorylationTSGQVEEYDLDADDI
CCCCEEEEECCHHHH
14.3223403867
262PhosphorylationLDADDINSRVEMKPK
CCHHHHHCCCCCCCC
37.7319664994

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
157TPhosphorylationKinasePRKCAP17252
GPS
157TPhosphorylationKinasePKC-FAMILY-GPS
157TPhosphorylationKinasePKC_GROUP-PhosphoELM
239TPhosphorylationKinasePRKCAP17252
GPS
239TPhosphorylationKinasePKC-FAMILY-GPS
239TPhosphorylationKinasePKC_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AQP1_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 AQP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MDFI_HUMANMDFIphysical
16189514
FBLN4_HUMANEFEMP2physical
16189514
KCD17_HUMANKCTD17physical
16189514
KR412_HUMANKRTAP4-12physical
16189514
TRIP6_HUMANTRIP6physical
16189514
CC85B_HUMANCCDC85Bphysical
16189514
MDFI_HUMANMDFIphysical
19447967
MDFI_HUMANMDFIphysical
19060904
ATL4_HUMANADAMTSL4physical
19060904
AQP1_HUMANAQP1physical
25416956
TRI23_HUMANTRIM23physical
25416956
FOS_HUMANFOSphysical
25416956
K1H1_HUMANKRT31physical
25416956
KT33B_HUMANKRT33Bphysical
25416956
SIAH1_HUMANSIAH1physical
25416956
ITF2_HUMANTCF4physical
25416956
TRAF1_HUMANTRAF1physical
25416956
TRAF2_HUMANTRAF2physical
25416956
TRIP6_HUMANTRIP6physical
25416956
RGS20_HUMANRGS20physical
25416956
ACK1_HUMANTNK2physical
25416956
SPY2_HUMANSPRY2physical
25416956
TRIM1_HUMANMID2physical
25416956
IKZF3_HUMANIKZF3physical
25416956
IKZF2_HUMANIKZF2physical
25416956
MTUS2_HUMANMTUS2physical
25416956
RGS17_HUMANRGS17physical
25416956
KCTD9_HUMANKCTD9physical
25416956
CRAC1_HUMANCRTAC1physical
25416956
CSRN1_HUMANCSRNP1physical
25416956
CC136_HUMANCCDC136physical
25416956
CEP44_HUMANCEP44physical
25416956
KRA92_HUMANKRTAP9-2physical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
RIM3A_HUMANRIMBP3physical
25416956
FSD2_HUMANFSD2physical
25416956
K1C40_HUMANKRT40physical
25416956
K1958_HUMANKIAA1958physical
25416956
CCD57_HUMANCCDC57physical
25416956
IHO1_HUMANCCDC36physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
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
Regulatory Network of AQP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND MASSSPECTROMETRY.

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