SATT_HUMAN - dbPTM
SATT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SATT_HUMAN
UniProt AC P43007
Protein Name Neutral amino acid transporter A
Gene Name SLC1A4
Organism Homo sapiens (Human).
Sequence Length 532
Subcellular Localization Membrane
Multi-pass membrane protein . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description Transporter for alanine, serine, cysteine, and threonine. Exhibits sodium dependence..
Protein Sequence MEKSNETNGYLDSAQAGPAAGPGAPGTAAGRARRCAGFLRRQALVLLTVSGVLAGAGLGAALRGLSLSRTQVTYLAFPGEMLLRMLRMIILPLVVCSLVSGAASLDASCLGRLGGIAVAYFGLTTLSASALAVALAFIIKPGSGAQTLQSSDLGLEDSGPPPVPKETVDSFLDLARNLFPSNLVVAAFRTYATDYKVVTQNSSSGNVTHEKIPIGTEIEGMNILGLVLFALVLGVALKKLGSEGEDLIRFFNSLNEATMVLVSWIMWYVPVGIMFLVGSKIVEMKDIIVLVTSLGKYIFASILGHVIHGGIVLPLIYFVFTRKNPFRFLLGLLAPFATAFATCSSSATLPSMMKCIEENNGVDKRISRFILPIGATVNMDGAAIFQCVAAVFIAQLNNVELNAGQIFTILVTATASSVGAAGVPAGGVLTIAIILEAIGLPTHDLPLILAVDWIVDRTTTVVNVEGDALGAGILHHLNQKATKKGEQELAEVKVEAIPNCKSEEETSPLVTHQNPAGPVASAPELESKESVL
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-------MEKSNETN
-------CCCCCCCC		15.3422814378
4Phosphorylation----MEKSNETNGYL
----CCCCCCCCCCC		26.9621945579
7Phosphorylation-MEKSNETNGYLDSA
-CCCCCCCCCCCCHH		37.8921945579
10PhosphorylationKSNETNGYLDSAQAG
CCCCCCCCCCHHHCC		14.9221945579
13PhosphorylationETNGYLDSAQAGPAA
CCCCCCCHHHCCCCC		21.4921945579
27PhosphorylationAGPGAPGTAAGRARR
CCCCCCCCHHHHHHH		16.5721945579
35S-palmitoylationAAGRARRCAGFLRRQ
HHHHHHHHHHHHHHH		3.4629575903
66PhosphorylationGAALRGLSLSRTQVT
HHHHHCCCCCCCCCC		27.4224719451
68PhosphorylationALRGLSLSRTQVTYL
HHHCCCCCCCCCCEE		29.8817081983
143PhosphorylationAFIIKPGSGAQTLQS
HHHCCCCCCCCHHHH		39.2126552605
147PhosphorylationKPGSGAQTLQSSDLG
CCCCCCCHHHHCCCC		26.6526552605
150PhosphorylationSGAQTLQSSDLGLED
CCCCHHHHCCCCCCC		29.0026552605
151PhosphorylationGAQTLQSSDLGLEDS
CCCHHHHCCCCCCCC		24.7226552605
158PhosphorylationSDLGLEDSGPPPVPK
CCCCCCCCCCCCCCH		43.7726552605
182UbiquitinationARNLFPSNLVVAAFR
HHHHCCHHHHHHHHH		36.7723503661
185UbiquitinationLFPSNLVVAAFRTYA
HCCHHHHHHHHHHHC		3.4223503661
186UbiquitinationFPSNLVVAAFRTYAT
CCHHHHHHHHHHHCC		8.0633845483
195UbiquitinationFRTYATDYKVVTQNS
HHHHCCCCEEEEECC		11.0021963094
196UbiquitinationRTYATDYKVVTQNSS
HHHCCCCEEEEECCC		32.7929967540
201N-linked_GlycosylationDYKVVTQNSSSGNVT
CCEEEEECCCCCCCC		34.2019349973
201N-linked_GlycosylationDYKVVTQNSSSGNVT
CCEEEEECCCCCCCC		34.2019349973
203UbiquitinationKVVTQNSSSGNVTHE
EEEEECCCCCCCCCC		50.2221963094
206N-linked_GlycosylationTQNSSSGNVTHEKIP
EECCCCCCCCCCCCC		37.1519349973
206N-linked_GlycosylationTQNSSSGNVTHEKIP
EECCCCCCCCCCCCC		37.1519349973
208PhosphorylationNSSSGNVTHEKIPIG
CCCCCCCCCCCCCCC		28.4632142685
209PhosphorylationSSSGNVTHEKIPIGT
CCCCCCCCCCCCCCC		30.0332142685
230UbiquitinationILGLVLFALVLGVAL
HHHHHHHHHHHHHHH		7.8121963094
242PhosphorylationVALKKLGSEGEDLIR
HHHHHHCCCHHHHHH		53.52-
260UbiquitinationSLNEATMVLVSWIMW
HHHHHHHHHHHHHHH		4.0823503661
263UbiquitinationEATMVLVSWIMWYVP
HHHHHHHHHHHHHHC		13.5123503661
264UbiquitinationATMVLVSWIMWYVPV
HHHHHHHHHHHHHCH		4.1333845483
273UbiquitinationMWYVPVGIMFLVGSK
HHHHCHHHHHHHCCC		1.4721963094
281UbiquitinationMFLVGSKIVEMKDII
HHHHCCCHHCHHHHE		3.2121963094
286PhosphorylationSKIVEMKDIIVLVTS
CCHHCHHHHEEHHHC		34.2432142685
287PhosphorylationKIVEMKDIIVLVTSL
CHHCHHHHEEHHHCC		1.6432142685
308UbiquitinationSILGHVIHGGIVLPL
HHHHHHHHHCHHHHH		27.6021963094
480UbiquitinationILHHLNQKATKKGEQ
HHHHHHHHCCHHCHH		57.8823503661
483UbiquitinationHLNQKATKKGEQELA
HHHHHCCHHCHHHHH		64.7423503661
484UbiquitinationLNQKATKKGEQELAE
HHHHCCHHCHHHHHH		64.4233845483
493UbiquitinationEQELAEVKVEAIPNC
HHHHHHEEEEECCCC		26.3421906983
501UbiquitinationVEAIPNCKSEEETSP
EEECCCCCCCCCCCC		68.4921963094
502PhosphorylationEAIPNCKSEEETSPL
EECCCCCCCCCCCCC		53.0623401153
506PhosphorylationNCKSEEETSPLVTHQ
CCCCCCCCCCCCCCC		38.6423401153
507PhosphorylationCKSEEETSPLVTHQN
CCCCCCCCCCCCCCC		21.3729255136
511PhosphorylationEETSPLVTHQNPAGP
CCCCCCCCCCCCCCC		25.9825159151
521PhosphorylationNPAGPVASAPELESK
CCCCCCCCCCHHCCC		44.5924972180
527PhosphorylationASAPELESKESVL--
CCCCHHCCCCCCC--		55.1129255136
528UbiquitinationSAPELESKESVL---
CCCHHCCCCCCC---		44.6321906983
530PhosphorylationPELESKESVL-----
CHHCCCCCCC-----		32.2425056879
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 SATT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of SATT_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
DB00160L-Alanine
Regulatory Network of SATT_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201 AND ASN-206, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND MASSSPECTROMETRY.

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