NHRF3_HUMAN - dbPTM
NHRF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NHRF3_HUMAN
UniProt AC Q5T2W1
Protein Name Na(+)/H(+) exchange regulatory cofactor NHE-RF3
Gene Name PDZK1
Organism Homo sapiens (Human).
Sequence Length 519
Subcellular Localization Membrane
Peripheral membrane protein . Cell membrane . Associated with peripheral membranes. Localizes to the apical compartment of proximal tubular cells and to sinusoidal liver membranes.
Protein Description A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity. Required for normal cell-surface expression of SCARB1. Plays a role in maintaining normal plasma cholesterol levels via its effects on SCARB1. Plays a role in the normal localization and function of the chloride-anion exchanger SLC26A6 to the plasma membrane in the brush border of the proximal tubule of the kidney. May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function (By similarity)..
Protein Sequence MTSTFNPRECKLSKQEGQNYGFFLRIEKDTEGHLVRVVEKCSPAEKAGLQDGDRVLRINGVFVDKEEHMQVVDLVRKSGNSVTLLVLDGDSYEKAVKTRVDLKELGQSQKEQGLSDNILSPVMNGGVQTWTQPRLCYLVKEGGSYGFSLKTVQGKKGVYMTDITPQGVAMRAGVLADDHLIEVNGENVEDASHEEVVEKVKKSGSRVMFLLVDKETDKRHVEQKIQFKRETASLKLLPHQPRIVEMKKGSNGYGFYLRAGSEQKGQIIKDIDSGSPAEEAGLKNNDLVVAVNGESVETLDHDSVVEMIRKGGDQTSLLVVDKETDNMYRLAHFSPFLYYQSQELPNGSVKEAPAPTPTSLEVSSPPDTTEEVDHKPKLCRLAKGENGYGFHLNAIRGLPGSFIKEVQKGGPADLAGLEDEDVIIEVNGVNVLDEPYEKVVDRIQSSGKNVTLLVCGKKAYDYFQAKKIPIVSSLADPLDTPPDSKEGIVVESNHDSHMAKERAHSTASHSSSNSEDTEM
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------MTSTFNPRE
------CCCCCCHHH
36.15-
78PhosphorylationVVDLVRKSGNSVTLL
HHEEEECCCCEEEEE
32.4228857561
81PhosphorylationLVRKSGNSVTLLVLD
EEECCCCEEEEEEEC
21.7228857561
83PhosphorylationRKSGNSVTLLVLDGD
ECCCCEEEEEEECCC
17.7528857561
108PhosphorylationDLKELGQSQKEQGLS
CHHHHCHHHHHCCCC
41.23-
120PhosphorylationGLSDNILSPVMNGGV
CCCCCCCHHHHCCCC
16.2028857561
144PhosphorylationYLVKEGGSYGFSLKT
EEEECCCCCCEEEEE
32.7028857561
148PhosphorylationEGGSYGFSLKTVQGK
CCCCCCEEEEEECCC
25.2928857561
151PhosphorylationSYGFSLKTVQGKKGV
CCCEEEEEECCCCEE
24.2928857561
192PhosphorylationGENVEDASHEEVVEK
CCCCCCCCHHHHHHH
43.69-
250PhosphorylationIVEMKKGSNGYGFYL
EEEEECCCCCCCEEE
35.6428857561
261PhosphorylationGFYLRAGSEQKGQII
CEEEECCCCCCCEEE
35.5528857561
316PhosphorylationRKGGDQTSLLVVDKE
HCCCCCCEEEEEECC
17.6722210691
328PhosphorylationDKETDNMYRLAHFSP
ECCCCCCCHHHHCCH
14.5522210691
334PhosphorylationMYRLAHFSPFLYYQS
CCHHHHCCHHHEEEC
12.60-
348PhosphorylationSQELPNGSVKEAPAP
CCCCCCCCCCCCCCC
36.3328857561
356PhosphorylationVKEAPAPTPTSLEVS
CCCCCCCCCCCEEEC
41.1126657352
358PhosphorylationEAPAPTPTSLEVSSP
CCCCCCCCCEEECCC
48.7130278072
359PhosphorylationAPAPTPTSLEVSSPP
CCCCCCCCEEECCCC
24.6030278072
363PhosphorylationTPTSLEVSSPPDTTE
CCCCEEECCCCCCCC
27.9630278072
364PhosphorylationPTSLEVSSPPDTTEE
CCCEEECCCCCCCCC
45.7028188228
368PhosphorylationEVSSPPDTTEEVDHK
EECCCCCCCCCCCCC
41.7123312004
369PhosphorylationVSSPPDTTEEVDHKP
ECCCCCCCCCCCCCC
37.2128857561
401PhosphorylationAIRGLPGSFIKEVQK
HHCCCCHHHHHHHHH
23.1224719451
451PhosphorylationQSSGKNVTLLVCGKK
HHCCCEEEEEEECCC
24.6228857561
472PhosphorylationAKKIPIVSSLADPLD
HCCCCEEECCCCCCC
21.9829978859
473PhosphorylationKKIPIVSSLADPLDT
CCCCEEECCCCCCCC
19.3829978859
480PhosphorylationSLADPLDTPPDSKEG
CCCCCCCCCCCCCCC
44.3928192239
484PhosphorylationPLDTPPDSKEGIVVE
CCCCCCCCCCCEEEE
38.0829978859
492PhosphorylationKEGIVVESNHDSHMA
CCCEEEECCCCHHHH
28.0521082442
505PhosphorylationMAKERAHSTASHSSS
HHHHHHHHHCCCCCC
25.3628857561
506PhosphorylationAKERAHSTASHSSSN
HHHHHHHHCCCCCCC
23.4728857561
508PhosphorylationERAHSTASHSSSNSE
HHHHHHCCCCCCCCC
24.8028857561
510PhosphorylationAHSTASHSSSNSEDT
HHHHCCCCCCCCCCC
32.7328857561
511PhosphorylationHSTASHSSSNSEDTE
HHHCCCCCCCCCCCC
28.2828857561
512PhosphorylationSTASHSSSNSEDTEM
HHCCCCCCCCCCCCC
47.6028857561
514PhosphorylationASHSSSNSEDTEM--
CCCCCCCCCCCCC--
38.5028857561
517PhosphorylationSSSNSEDTEM-----
CCCCCCCCCC-----
29.8725072903

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
505SPhosphorylationKinasePKACAP17612
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NHRF3_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 NHRF3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SL9A3_HUMANSLC9A3physical
14531806
NPT1_HUMANSLC17A1physical
14531806
MRP2_HUMANABCC2physical
10496535
S22A4_HUMANSLC22A4physical
14531806
AKA10_HUMANAKAP10physical
14531806
S22AC_HUMANSLC22A12physical
14531806
PEX5_HUMANPEX5physical
16189514
UBC9_HUMANUBE2Iphysical
14531806
PDZ1I_HUMANPDZK1IP1physical
14531806
NHRF2_HUMANSLC9A3R2physical
14531806
FARP2_HUMANFARP2physical
14531806
SLK_HUMANSLKphysical
14531806
NHRF1_HUMANSLC9A3R1physical
14531806
PDZ1I_HUMANPDZK1IP1physical
12837682
PDZ1I_HUMANPDZK1IP1physical
12754212
SCRB1_HUMANSCARB1physical
12119305
CLCN3_HUMANCLCN3physical
12471024
CFTR_HUMANCFTRphysical
12471024
CFTR_HUMANCFTRphysical
11051556
KLH17_RATKlhl17physical
12063253
DLG4_RATDlg4physical
12063253
A4_HUMANAPPphysical
21832049
MRP4_HUMANABCC4physical
18045536
PI2R_MOUSEPtgirphysical
23457445
CDC37_HUMANCDC37physical
24869908
AKT1_HUMANAKT1physical
24869908
NPT2A_HUMANSLC34A1physical
14531806
MRP2_HUMANABCC2physical
21059598
RHG17_HUMANARHGAP17physical
28514442
ASND1_HUMANASNSD1physical
28514442
MRP4_HUMANABCC4physical
28514442
BCR_HUMANBCRphysical
28514442
FRYL_HUMANFRYLphysical
28514442
SHKB1_HUMANSHKBP1physical
28514442
KCTD3_HUMANKCTD3physical
28514442
SH2D5_HUMANSH2D5physical
28514442
KCD17_HUMANKCTD17physical
28514442
SC6A6_HUMANSLC6A6physical
28514442
S22A5_HUMANSLC22A5physical
28514442
ZBED1_HUMANZBED1physical
28514442
KCTD2_HUMANKCTD2physical
28514442
COL12_HUMANCOLEC12physical
28514442
S4A7_HUMANSLC4A7physical
28514442
KCTD5_HUMANKCTD5physical
28514442
KLH17_HUMANKLHL17physical
28514442
SC5A6_HUMANSLC5A6physical
28514442
OTUL_HUMANOTULINphysical
28514442
SCRB1_HUMANSCARB1physical
28514442
ZBTB5_HUMANZBTB5physical
28514442
S19A3_HUMANSLC19A3physical
28514442
DECR2_HUMANDECR2physical
28514442
KLH24_HUMANKLHL24physical
28514442
ECI2_HUMANECI2physical
28514442
CK5P1_HUMANCDK5RAP1physical
28514442
EAA1_HUMANSLC1A3physical
28514442
CSK22_HUMANCSNK2A2physical
28514442

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
There are no disease associations of PTM sites.
Regulatory Network of NHRF3_HUMAN

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Related Literatures of Post-Translational Modification

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