S12A5_HUMAN - dbPTM
S12A5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S12A5_HUMAN
UniProt AC Q9H2X9
Protein Name Solute carrier family 12 member 5
Gene Name SLC12A5
Organism Homo sapiens (Human).
Sequence Length 1139
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Mediates electroneutral potassium-chloride cotransport in mature neurons and is required for neuronal Cl(-) homeostasis. As major extruder of intracellular chloride, it establishes the low neuronal Cl(-) levels required for chloride influx after binding of GABA-A and glycine to their receptors, with subsequent hyperpolarization and neuronal inhibition (By similarity). Involved in the regulation of dendritic spine formation and maturation. [PubMed: 24668262]
Protein Sequence MSRRFTVTSLPPAGPARSPDPESRRHSVADPRHLPGEDVKGDGNPKESSPFINSTDTEKGKEYDGKNMALFEEEMDTSPMVSSLLSGLANYTNLPQGSREHEEAENNEGGKKKPVQAPRMGTFMGVYLPCLQNIFGVILFLRLTWVVGIAGIMESFCMVFICCSCTMLTAISMSAIATNGVVPAGGSYYMISRSLGPEFGGAVGLCFYLGTTFAGAMYILGTIEILLAYLFPAMAIFKAEDASGEAAAMLNNMRVYGTCVLTCMATVVFVGVKYVNKFALVFLGCVILSILAIYAGVIKSAFDPPNFPICLLGNRTLSRHGFDVCAKLAWEGNETVTTRLWGLFCSSRFLNATCDEYFTRNNVTEIQGIPGAASGLIKENLWSSYLTKGVIVERSGMTSVGLADGTPIDMDHPYVFSDMTSYFTLLVGIYFPSVTGIMAGSNRSGDLRDAQKSIPTGTILAIATTSAVYISSVVLFGACIEGVVLRDKFGEAVNGNLVVGTLAWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAISRDGIVPFLQVFGHGKANGEPTWALLLTACICEIGILIASLDEVAPILSMFFLMCYMFVNLACAVQTLLRTPNWRPRFRYYHWTLSFLGMSLCLALMFICSWYYALVAMLIAGLIYKYIEYRGAEKEWGDGIRGLSLSAARYALLRLEEGPPHTKNWRPQLLVLVRVDQDQNVVHPQLLSLTSQLKAGKGLTIVGSVLEGTFLENHPQAQRAEESIRRLMEAEKVKGFCQVVISSNLRDGVSHLIQSGGLGGLQHNTVLVGWPRNWRQKEDHQTWRNFIELVRETTAGHLALLVTKNVSMFPGNPERFSEGSIDVWWIVHDGGMLMLLPFLLRHHKVWRKCKMRIFTVAQMDDNSIQMKKDLTTFLYHLRITAEVEVVEMHESDISAYTYEKTLVMEQRSQILKQMHLTKNEREREIQSITDESRGSIRRKNPANTRLRLNVPEETAGDSEEKPEEEVQLIHDQSAPSCPSSSPSPGEEPEGEGETDPEKVHLTWTKDKSVAEKNKGPSPVSSEGIKDFFSMKPEWENLNQSNVRRMHTAVRLNEVIVKKSRDAKLVLLNMPGPPRNRNGDENYMEFLEVLTEHLDRVMLVRGGGREVITIYS
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------MSRRFTVTS
------CCCCEEECC
43.3924043423
6Phosphorylation--MSRRFTVTSLPPA
--CCCCEEECCCCCC
22.5130266825
8PhosphorylationMSRRFTVTSLPPAGP
CCCCEEECCCCCCCC
22.8430266825
9PhosphorylationSRRFTVTSLPPAGPA
CCCEEECCCCCCCCC
34.2430266825
18PhosphorylationPPAGPARSPDPESRR
CCCCCCCCCCHHHHC
35.4430266825
23PhosphorylationARSPDPESRRHSVAD
CCCCCHHHHCCCCCC
39.7530266825
27PhosphorylationDPESRRHSVADPRHL
CHHHHCCCCCCCCCC
19.7229691806
49PhosphorylationDGNPKESSPFINSTD
CCCCCCCCCCCCCCC
25.5624076635
54PhosphorylationESSPFINSTDTEKGK
CCCCCCCCCCCCCCC
23.89-
57PhosphorylationPFINSTDTEKGKEYD
CCCCCCCCCCCCCCC
39.42-
77PhosphorylationLFEEEMDTSPMVSSL
HHHHHHCCCHHHHHH
33.16-
78PhosphorylationFEEEMDTSPMVSSLL
HHHHHCCCHHHHHHH
13.51-
82PhosphorylationMDTSPMVSSLLSGLA
HCCCHHHHHHHHHHH
14.71-
92PhosphorylationLSGLANYTNLPQGSR
HHHHHHCCCCCCCCH
30.04-
335PhosphorylationLAWEGNETVTTRLWG
ECCCCCCCHHHHHHH
27.4427251275
337PhosphorylationWEGNETVTTRLWGLF
CCCCCCHHHHHHHHH
17.3927251275
338PhosphorylationEGNETVTTRLWGLFC
CCCCCHHHHHHHHHH
21.3027251275
442N-linked_GlycosylationTGIMAGSNRSGDLRD
CEECCCCCCCCCHHH
41.02UniProtKB CARBOHYD
444PhosphorylationIMAGSNRSGDLRDAQ
ECCCCCCCCCHHHHH
40.69-
501PhosphorylationNGNLVVGTLAWPSPW
CCCEEEEECCCCCCE
11.16-
537PhosphorylationPRLLQAISRDGIVPF
HHHHHHHHCCCCEEE
27.6029083192
617PhosphorylationWRPRFRYYHWTLSFL
CCCCCHHHHHHHHHH
6.14-
622PhosphorylationRYYHWTLSFLGMSLC
HHHHHHHHHHHHHHH
15.85-
668UbiquitinationEKEWGDGIRGLSLSA
CCHHCCCHHHHHHHH
3.6222817900
672PhosphorylationGDGIRGLSLSAARYA
CCCHHHHHHHHHHHH
24.0930108239
674PhosphorylationGIRGLSLSAARYALL
CHHHHHHHHHHHHHH
19.2630108239
691UbiquitinationEEGPPHTKNWRPQLL
CCCCCCCCCCCCEEE
52.0222817900
702UbiquitinationPQLLVLVRVDQDQNV
CEEEEEEEECCCCCC
23.3330230243
725UbiquitinationTSQLKAGKGLTIVGS
HHHHHCCCCEEEEEE
56.4530230243
751PhosphorylationQAQRAEESIRRLMEA
HHHHHHHHHHHHHHH
16.9526437602
770PhosphorylationGFCQVVISSNLRDGV
CEEEEEECCCCCCHH
11.1030576142
821PhosphorylationFIELVRETTAGHLAL
HHHHHHHCCHHHHHE
16.04-
831PhosphorylationGHLALLVTKNVSMFP
HHHHEEEECCCCCCC
19.50-
833N-linked_GlycosylationLALLVTKNVSMFPGN
HHEEEECCCCCCCCC
23.02UniProtKB CARBOHYD
872UbiquitinationPFLLRHHKVWRKCKM
HHHHHCHHHHHHCCC
37.0530230243
895UbiquitinationDDNSIQMKKDLTTFL
CCCCEECHHHHHHHH
27.1030230243
929PhosphorylationSAYTYEKTLVMEQRS
CEEEECCHHHHHHHH
16.7919665974
936PhosphorylationTLVMEQRSQILKQMH
HHHHHHHHHHHHHHC
22.6723401153
945PhosphorylationILKQMHLTKNERERE
HHHHHCCCCCHHHHH
19.6927762562
960PhosphorylationIQSITDESRGSIRRK
HHHCCCCCCCCCCCC
44.7630108239
963PhosphorylationITDESRGSIRRKNPA
CCCCCCCCCCCCCCC
16.2930108239
1007PhosphorylationQSAPSCPSSSPSPGE
CCCCCCCCCCCCCCC
48.0132142685
1030PhosphorylationDPEKVHLTWTKDKSV
CHHHEEEEEECCHHH
19.0619665974
1032PhosphorylationEKVHLTWTKDKSVAE
HHEEEEEECCHHHHH
24.91-
1045PhosphorylationAEKNKGPSPVSSEGI
HHHCCCCCCCCCCHH
46.7524076635
1048PhosphorylationNKGPSPVSSEGIKDF
CCCCCCCCCCHHHHH
26.5125307156
1049PhosphorylationKGPSPVSSEGIKDFF
CCCCCCCCCHHHHHH
39.82-
1057PhosphorylationEGIKDFFSMKPEWEN
CHHHHHHHCCHHHHC
26.3724719451
1110PhosphorylationNRNGDENYMEFLEVL
CCCCCCCHHHHHHHH
8.9310942735

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
6TPhosphorylationKinaseSTK39Q9UEW8
GPS
1032TPhosphorylationKinaseSTK39Q9UEW8
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S12A5_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 S12A5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of S12A5_HUMAN !!

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
DB00887Bumetanide
DB00761Potassium Chloride
Regulatory Network of S12A5_HUMAN

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Related Literatures of Post-Translational Modification

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