SO3A1_HUMAN - dbPTM
SO3A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SO3A1_HUMAN
UniProt AC Q9UIG8
Protein Name Solute carrier organic anion transporter family member 3A1
Gene Name SLCO3A1
Organism Homo sapiens (Human).
Sequence Length 710
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description Mediates the Na(+)-independent transport of organic anions such as estrone-3-sulfate. [PubMed: 10873595 Mediates transport of prostaglandins (PG) E1 and E2, thyroxine (T4), deltorphin II, BQ-123 and vasopressin, but not DPDPE (a derivative of enkephalin lacking an N-terminal tyrosine residue), estrone-3-sulfate, taurocholate, digoxin nor DHEAS]
Protein Sequence MQGKKPGGSSGGGRSGELQGDEAQRNKKKKKKVSCFSNIKIFLVSECALMLAQGTVGAYLVSVLTTLERRFNLQSADVGVIASSFEIGNLALILFVSYFGARGHRPRLIGCGGIVMALGALLSALPEFLTHQYKYEAGEIRWGAEGRDVCAANGSGGDEGPDPDLICRNRTATNMMYLLLIGAQVLLGIGATPVQPLGVSYIDDHVRRKDSSLYIGILFTMLVFGPACGFILGSFCTKIYVDAVFIDTSNLDITPDDPRWIGAWWGGFLLCGALLFFSSLLMFGFPQSLPPHSEPAMESEQAMLSEREYERPKPSNGVLRHPLEPDSSASCFQQLRVIPKVTKHLLSNPVFTCIILAACMEIAVVAGFAAFLGKYLEQQFNLTTSSANQLLGMTAIPCACLGIFLGGLLVKKLSLSALGAIRMAMLVNLVSTACYVSFLFLGCDTGPVAGVTVPYGNSTAPGSALDPYSPCNNNCECQTDSFTPVCGADGITYLSACFAGCNSTNLTGCACLTTVPAENATVVPGKCPSPGCQEAFLTFLCVMCICSLIGAMAQTPSVIILIRTVSPELKSYALGVLFLLLRLLGFIPPPLIFGAGIDSTCLFWSTFCGEQGACVLYDNVVYRYLYVSIAIALKSFAFILYTTTWQCLRKNYKRYIKNHEGGLSTSEFFASTLTLDNLGRDPVPANQTHRTKFIYNLEDHEWCENMESVL
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
1Acetylation-------MQGKKPGG
-------CCCCCCCC		12.2125732826
4 (in isoform 3)Phosphorylation-38.6124043423
7 (in isoform 3)Phosphorylation-58.4524043423
8 (in isoform 3)Phosphorylation-27.4524043423
15PhosphorylationGSSGGGRSGELQGDE
CCCCCCCCCCCCCCH		39.6428674419
34PhosphorylationKKKKKKVSCFSNIKI
CCCCCCCCCCCCCHH		20.51-
153N-linked_GlycosylationGRDVCAANGSGGDEG
CCCCEECCCCCCCCC		27.00UniProtKB CARBOHYD
169N-linked_GlycosylationDPDLICRNRTATNMM
CCCCCCCCCCHHHHH		41.04UniProtKB CARBOHYD
171PhosphorylationDLICRNRTATNMMYL
CCCCCCCCHHHHHHH		41.1926074081
173PhosphorylationICRNRTATNMMYLLL
CCCCCCHHHHHHHHH		24.0426074081
177PhosphorylationRTATNMMYLLLIGAQ
CCHHHHHHHHHHHHH		5.3926074081
288PhosphorylationLMFGFPQSLPPHSEP
HHHCCCCCCCCCCCC		42.9824043423
293PhosphorylationPQSLPPHSEPAMESE
CCCCCCCCCCCHHHH		51.5624043423
299PhosphorylationHSEPAMESEQAMLSE
CCCCCHHHHHHHHHH		23.1724043423
305PhosphorylationESEQAMLSEREYERP
HHHHHHHHHCHHCCC		22.8624043423
309PhosphorylationAMLSEREYERPKPSN
HHHHHCHHCCCCCCC		24.3725106551
331S-palmitoylationEPDSSASCFQQLRVI
CCCCCCHHHHHHCCH		3.4029575903
381N-linked_GlycosylationKYLEQQFNLTTSSAN
HHHHHHHCCCCCCHH		31.94UniProtKB CARBOHYD
457N-linked_GlycosylationGVTVPYGNSTAPGSA
CEEECCCCCCCCCCC		30.28UniProtKB CARBOHYD
502N-linked_GlycosylationSACFAGCNSTNLTGC
HHHHCCCCCCCCCCC		51.45UniProtKB CARBOHYD
505N-linked_GlycosylationFAGCNSTNLTGCACL
HCCCCCCCCCCCEEE		35.11UniProtKB CARBOHYD
519N-linked_GlycosylationLTTVPAENATVVPGK
EEEEECCCCEECCCC		42.91UniProtKB CARBOHYD
566PhosphorylationIILIRTVSPELKSYA
EEEEECCCHHHHHHH		16.4324719451
571PhosphorylationTVSPELKSYALGVLF
CCCHHHHHHHHHHHH		28.4122461510
572PhosphorylationVSPELKSYALGVLFL
CCHHHHHHHHHHHHH		12.3122461510
624PhosphorylationYDNVVYRYLYVSIAI
ECCCHHHHHHHHHHH		5.6829083192
626PhosphorylationNVVYRYLYVSIAIAL
CCHHHHHHHHHHHHH		5.3429083192
628PhosphorylationVYRYLYVSIAIALKS
HHHHHHHHHHHHHHH		7.8629083192
655PhosphorylationLRKNYKRYIKNHEGG
HHHHHHHHHHHCCCC		16.4624719451
664PhosphorylationKNHEGGLSTSEFFAS
HHCCCCCCHHHHHHH		32.9123663014
665PhosphorylationNHEGGLSTSEFFAST
HCCCCCCHHHHHHHH		37.0023663014
666PhosphorylationHEGGLSTSEFFASTL
CCCCCCHHHHHHHHC		29.0923663014
671PhosphorylationSTSEFFASTLTLDNL
CHHHHHHHHCCCCCC		20.8421955146
672PhosphorylationTSEFFASTLTLDNLG
HHHHHHHHCCCCCCC		21.9723663014
674PhosphorylationEFFASTLTLDNLGRD
HHHHHHCCCCCCCCC		31.9623663014
676UbiquitinationFASTLTLDNLGRDPV
HHHHCCCCCCCCCCC		42.9729967540
677 (in isoform 2)Phosphorylation-47.73-
685 (in isoform 2)Phosphorylation-22.46-
688PhosphorylationDPVPANQTHRTKFIY
CCCCCCCCCCEEEEE		17.0921955146
688 (in isoform 2)Phosphorylation-17.09-
692 (in isoform 2)Phosphorylation-29.71-
695PhosphorylationTHRTKFIYNLEDHEW
CCCEEEEEECCCCHH		19.4827642862
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 SO3A1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SO3A1_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 SO3A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SO3A1_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SO3A1_HUMAN

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Related Literatures of Post-Translational Modification

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