S22AG_HUMAN - dbPTM
S22AG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S22AG_HUMAN
UniProt AC Q86VW1
Protein Name Solute carrier family 22 member 16
Gene Name SLC22A16
Organism Homo sapiens (Human).
Sequence Length 577
Subcellular Localization Membrane
Multi-pass membrane protein . Cell membrane . Detected in the plasma membrane of Sertoli cells and in the luminal membrane of epithelial cells in the epididymis.
Protein Description High affinity carnitine transporter; the uptake is partially sodium-ion dependent. Thought to mediate the L-carnitine secretion mechanism from testis epididymal epithelium into the lumen which is involved in the maturation of spermatozoa. Also transports organic cations such as tetraethylammonium (TEA) and doxorubicin. The uptake of TEA is inhibited by various organic cations. The uptake of doxorubicin is sodium-independent..
Protein Sequence MGSRHFEGIYDHVGHFGRFQRVLYFICAFQNISCGIHYLASVFMGVTPHHVCRPPGNVSQVVFHNHSNWSLEDTGALLSSGQKDYVTVQLQNGEIWELSRCSRNKRENTSSLGYEYTGSKKEFPCVDGYIYDQNTWKSTAVTQWNLVCDRKWLAMLIQPLFMFGVLLGSVTFGYFSDRLGRRVVLWATSSSMFLFGIAAAFAVDYYTFMAARFFLAMVASGYLVVGFVYVMEFIGMKSRTWASVHLHSFFAVGTLLVALTGYLVRTWWLYQMILSTVTVPFILCCWVLPETPFWLLSEGRYEEAQKIVDIMAKWNRASSCKLSELLSLDLQGPVSNSPTEVQKHNLSYLFYNWSITKRTLTVWLIWFTGSLGFYSFSLNSVNLGGNEYLNLFLLGVVEIPAYTFVCIAMDKVGRRTVLAYSLFCSALACGVVMVIPQKHYILGVVTAMVGKFAIGAAFGLIYLYTAELYPTIVRSLAVGSGSMVCRLASILAPFSVDLSSIWIFIPQLFVGTMALLSGVLTLKLPETLGKRLATTWEEAAKLESENESKSSKLLLTTNNSGLEKTEAITPRDSGLGE
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_GlycosylationHVCRPPGNVSQVVFH
CCCCCCCCEEEEEEE
35.72UniProtKB CARBOHYD
65N-linked_GlycosylationVSQVVFHNHSNWSLE
EEEEEEECCCCCCHH
28.90UniProtKB CARBOHYD
68N-linked_GlycosylationVVFHNHSNWSLEDTG
EEEECCCCCCHHHHC
25.46UniProtKB CARBOHYD
108N-linked_GlycosylationCSRNKRENTSSLGYE
ECCCCCCCCCCCCCE
49.66UniProtKB CARBOHYD
238PhosphorylationMEFIGMKSRTWASVH
HHHHCCCCCCEEEHH
26.5024719451
345N-linked_GlycosylationPTEVQKHNLSYLFYN
CHHHHHHCEEEEEEC
37.40UniProtKB CARBOHYD
352N-linked_GlycosylationNLSYLFYNWSITKRT
CEEEEEECCCCCCCC
20.77UniProtKB CARBOHYD
475PhosphorylationLYPTIVRSLAVGSGS
HHHHHHHHHCCCCCC
15.13-
535PhosphorylationLGKRLATTWEEAAKL
HHHHHHHCHHHHHHH
25.85-
546N-linked_GlycosylationAAKLESENESKSSKL
HHHHHCCCCCCCCCE
69.03UniProtKB CARBOHYD
556PhosphorylationKSSKLLLTTNNSGLE
CCCCEEEEECCCCCC
27.70-
558N-linked_GlycosylationSKLLLTTNNSGLEKT
CCEEEEECCCCCCEE
35.12UniProtKB CARBOHYD
560PhosphorylationLLLTTNNSGLEKTEA
EEEEECCCCCCEEEC
46.99-
569PhosphorylationLEKTEAITPRDSGLG
CCEEECCCCCCCCCC
21.2224719451

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 S22AG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S22AG_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 S22AG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBP5_HUMANGBP5physical
28514442
ACSM1_HUMANACSM1physical
28514442
TM104_HUMANTMEM104physical
28514442
APBA3_HUMANAPBA3physical
28514442
RAB21_HUMANRAB21physical
28514442
S2546_HUMANSLC25A46physical
28514442
CXG1_HUMANGJC1physical
28514442
MBOA5_HUMANLPCAT3physical
28514442
PXMP2_HUMANPXMP2physical
28514442
MTX3_HUMANMTX3physical
28514442
AT2B2_HUMANATP2B2physical
28514442
TMM56_HUMANTMEM56physical
28514442
S29A1_HUMANSLC29A1physical
28514442
ATLA3_HUMANATL3physical
28514442
S26A2_HUMANSLC26A2physical
28514442
MFSD8_HUMANMFSD8physical
28514442
SPPL3_HUMANSPPL3physical
28514442
SERC1_HUMANSERINC1physical
28514442
TM164_HUMANTMEM164physical
28514442
SNG2_HUMANSYNGR2physical
28514442
KMCP1_HUMANSLC25A30physical
28514442
FND3A_HUMANFNDC3Aphysical
28514442
FLVC1_HUMANFLVCR1physical
28514442
TSN15_HUMANTSPAN15physical
28514442
PAQR1_HUMANADIPOR1physical
28514442
MIC25_HUMANCHCHD6physical
28514442
NOCT_HUMANCCRN4Lphysical
28514442
PLCB_HUMANAGPAT2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of S22AG_HUMAN

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Related Literatures of Post-Translational Modification

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