S22A5_HUMAN - dbPTM
S22A5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S22A5_HUMAN
UniProt AC O76082
Protein Name Solute carrier family 22 member 5
Gene Name SLC22A5
Organism Homo sapiens (Human).
Sequence Length 557
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Also relative uptake activity ratio of carnitine to TEA is 11.3..
Protein Sequence MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFTGLSSVFLIATPEHRCRVPDAANLSSAWRNHTVPLRLRDGREVPHSCRRYRLATIANFSALGLEPGRDVDLGQLEQESCLDGWEFSQDVYLSTIVTEWNLVCEDDWKAPLTISLFFVGVLLGSFISGQLSDRFGRKNVLFVTMGMQTGFSFLQIFSKNFEMFVVLFVLVGMGQISNYVAAFVLGTEILGKSVRIIFSTLGVCIFYAFGYMVLPLFAYFIRDWRMLLVALTMPGVLCVALWWFIPESPRWLISQGRFEEAEVIIRKAAKANGIVVPSTIFDPSELQDLSSKKQQSHNILDLLRTWNIRMVTIMSIMLWMTISVGYFGLSLDTPNLHGDIFVNCFLSAMVEVPAYVLAWLLLQYLPRRYSMATALFLGGSVLLFMQLVPPDLYYLATVLVMVGKFGVTAAFSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFLPESFGTPLPDTIDQMLRVKGMKHRKTPSHTRMLKDGQERPTILKSTAF
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
57N-linked_GlycosylationCRVPDAANLSSAWRN
CCCCCCCCCCHHHHC		42.0219349973
57N-linked_GlycosylationCRVPDAANLSSAWRN
CCCCCCCCCCHHHHC		42.0219349973
64N-linked_GlycosylationNLSSAWRNHTVPLRL
CCCHHHHCCCCCCEE		25.20UniProtKB CARBOHYD
64N-linked_GlycosylationNLSSAWRNHTVPLRL
CCCHHHHCCCCCCEE		25.2019349973
88PhosphorylationCRRYRLATIANFSAL
CCHHHHHEEECHHHC		25.80-
91N-linked_GlycosylationYRLATIANFSALGLE
HHHHEEECHHHCCCC		27.7919349973
91N-linked_GlycosylationYRLATIANFSALGLE
HHHHEEECHHHCCCC		27.7919349973
93PhosphorylationLATIANFSALGLEPG
HHEEECHHHCCCCCC		23.53-
93UbiquitinationLATIANFSALGLEPG
HHEEECHHHCCCCCC		23.5323503661
96UbiquitinationIANFSALGLEPGRDV
EECHHHCCCCCCCCC		27.9323503661
118UbiquitinationESCLDGWEFSQDVYL
CHHCCCCCCCCCCHH		40.7322817900
119UbiquitinationSCLDGWEFSQDVYLS
HHCCCCCCCCCCHHH		6.8322817900
123UbiquitinationGWEFSQDVYLSTIVT
CCCCCCCCHHHHEEE		3.9223503661
126UbiquitinationFSQDVYLSTIVTEWN
CCCCCHHHHEEECEE		9.8223503661
148UbiquitinationKAPLTISLFFVGVLL
CCCCCHHHHHHHHHH		3.2322817900
149UbiquitinationAPLTISLFFVGVLLG
CCCCHHHHHHHHHHH		3.5822817900
176PhosphorylationRKNVLFVTMGMQTGF
CCCEEEEEECCCCCC		10.7320049867
181PhosphorylationFVTMGMQTGFSFLQI
EEEECCCCCCCHHHH		31.1620049867
184PhosphorylationMGMQTGFSFLQIFSK
ECCCCCCCHHHHHHC		26.7920049867
190PhosphorylationFSFLQIFSKNFEMFV
CCHHHHHHCCHHHHH		28.4624719451
209PhosphorylationLVGMGQISNYVAAFV
HHCCCHHHHHHHHHH		17.7720049867
211PhosphorylationGMGQISNYVAAFVLG
CCCHHHHHHHHHHHC		5.6720049867
217 (in isoform 2)Ubiquitination-5.9221906983
219PhosphorylationVAAFVLGTEILGKSV
HHHHHHCHHHCCHHH		18.7220049867
225PhosphorylationGTEILGKSVRIIFST
CHHHCCHHHHHHHHH		18.1520049867
299UbiquitinationEAEVIIRKAAKANGI
CHHHHHHHHHHHCCE		42.1423503661
302UbiquitinationVIIRKAAKANGIVVP
HHHHHHHHHCCEECC		47.4423503661
323UbiquitinationSELQDLSSKKQQSHN
HHHHHHHHHHHHHHC		51.6923503661
324UbiquitinationELQDLSSKKQQSHNI
HHHHHHHHHHHHHCH		51.7522817900
324 (in isoform 1)Ubiquitination-51.7521906983
325UbiquitinationLQDLSSKKQQSHNIL
HHHHHHHHHHHHCHH		56.3622817900
326UbiquitinationQDLSSKKQQSHNILD
HHHHHHHHHHHCHHH		54.4623503661
337UbiquitinationNILDLLRTWNIRMVT
CHHHHHHHHCHHHHH		23.8823503661
347UbiquitinationIRMVTIMSIMLWMTI
HHHHHHHHHHHHHHH		10.8621963094
348UbiquitinationRMVTIMSIMLWMTIS
HHHHHHHHHHHHHHH		1.1332015554
349UbiquitinationMVTIMSIMLWMTISV
HHHHHHHHHHHHHHH		1.5522817900
367UbiquitinationGLSLDTPNLHGDIFV
CCCCCCCCCCCCHHH		46.9223503661
377UbiquitinationGDIFVNCFLSAMVEV
CCHHHHHHHHHHHHH		5.2121963094
468PhosphorylationMGVGVSSTASRLGSI
CCCCCCCHHHHHHHH		22.58-
470PhosphorylationVGVSSTASRLGSILS
CCCCCHHHHHHHHHC		28.29-
474PhosphorylationSTASRLGSILSPYFV
CHHHHHHHHHCHHHH		25.58-
486PhosphorylationYFVYLGAYDRFLPYI
HHHHHCCCHHHHHHH		13.0724260401
543UbiquitinationPSHTRMLKDGQERPT
CCHHEECCCCCCCCC		50.9323503661
550PhosphorylationKDGQERPTILKSTAF
CCCCCCCCCCCCCCC		45.2010072434
553UbiquitinationQERPTILKSTAF---
CCCCCCCCCCCC---		41.7421963094
553 (in isoform 1)Ubiquitination-41.7421906983
554PhosphorylationERPTILKSTAF----
CCCCCCCCCCC----		22.8626425664
567Ubiquitination-----------------
-----------------		23503661
577Ubiquitination---------------------------
---------------------------		21963094
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 S22A5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S22A5_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 S22A5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HMCS1_HUMANHMGCS1physical
28514442
Drug and Disease Associations
Kegg Disease
H00286 Crohn's disease
H00525 Disorders of fatty-acid oxidation, including: Medium-chain (MC) acyl-CoA dehydrogenase (AD) deficien
OMIM Disease
212140Systemic primary carnitine deficiency (CDSP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB08842Acetylcarnitine
DB00345Aminohippurate
DB00182Amphetamine
DB00415Ampicillin
DB08795Azidocillin
DB01053Benzylpenicillin
DB01140Cefadroxil
DB00456Cefalotin
DB00535Cefdinir
DB01413Cefepime
DB00671Cefixime
DB01333Cefradine
DB00438Ceftazidime
DB00567Cephalexin
DB00689Cephaloglycin
DB00122Choline
DB00501Cimetidine
DB00575Clonidine
DB00148Creatine
DB01000Cyclacillin
DB00970Dactinomycin
DB01151Desipramine
DB01075Diphenhydramine
DB00988Dopamine
DB00668Epinephrine
DB00695Furosemide
DB00536Guanidine
DB00667Histamine Phosphate
DB00332Ipratropium bromide
DB00125L-Arginine
DB00583L-Carnitine
DB00281Lidocaine
DB00978Lomefloxacin
DB06691Mepyramine
DB01577Methamphetamine
DB00627Niacin
DB00184Nicotine
DB00368Norepinephrine
DB01059Norfloxacin
DB01165Ofloxacin
DB01032Probenecid
DB01035Procainamide
DB00908Quinidine
DB00468Quinine
DB01208Sparfloxacin
DB00152Thiamine
DB01409Tiotropium
DB00313Valproic Acid
DB00661Verapamil
Regulatory Network of S22A5_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-57 AND ASN-91, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-486, AND MASSSPECTROMETRY.

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