TM9S4_HUMAN - dbPTM
TM9S4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM9S4_HUMAN
UniProt AC Q92544
Protein Name Transmembrane 9 superfamily member 4
Gene Name TM9SF4
Organism Homo sapiens (Human).
Sequence Length 642
Subcellular Localization Membrane
Multi-pass membrane protein . Golgi apparatus . Early endosome .
Protein Description Associates with proteins harboring glycine-rich transmembrane domains and ensures their efficient localization to the cell surface. [PubMed: 25999474 Regulates the assembly and activity of V-ATPase in colon cancer cells via its interaction with V-type proton ATPase subunit H (ATP6V1H) and contributes to V-ATPase-mediated pH alterations in cancer cells which play an important role in drug resistance and invasiveness of colon cancer cells]
Protein Sequence MATAMDWLPWSLLLFSLMCETSAFYVPGVAPINFHQNDPVEIKAVKLTSSRTQLPYEYYSLPFCQPSKITYKAENLGEVLRGDRIVNTPFQVLMNSEKKCEVLCSQSNKPVTLTVEQSRLVAERITEDYYVHLIADNLPVATRLELYSNRDSDDKKKEKDVQFEHGYRLGFTDVNKIYLHNHLSFILYYHREDMEEDQEHTYRVVRFEVIPQSIRLEDLKADEKSSCTLPEGTNSSPQEIDPTKENQLYFTYSVHWEESDIKWASRWDTYLTMSDVQIHWFSIINSVVVVFFLSGILSMIIIRTLRKDIANYNKEDDIEDTMEESGWKLVHGDVFRPPQYPMILSSLLGSGIQLFCMILIVIFVAMLGMLSPSSRGALMTTACFLFMFMGVFGGFSAGRLYRTLKGHRWKKGAFCTATLYPGVVFGICFVLNCFIWGKHSSGAVPFPTMVALLCMWFGISLPLVYLGYYFGFRKQPYDNPVRTNQIPRQIPEQRWYMNRFVGILMAGILPFGAMFIELFFIFSAIWENQFYYLFGFLFLVFIILVVSCSQISIVMVYFQLCAEDYRWWWRNFLVSGGSAFYVLVYAIFYFVNKLDIVEFIPSLLYFGYTALMVLSFWLLTGTIGFYAAYMFVRKIYAAVKID
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
46UbiquitinationPVEIKAVKLTSSRTQ
CEEEEEEEEECCCCC		51.40-
68UbiquitinationLPFCQPSKITYKAEN
CCCCCCCCCEEEECC		45.83-
72 (in isoform 1)Ubiquitination-40.3421906983
72UbiquitinationQPSKITYKAENLGEV
CCCCCEEEECCHHHH		40.3421890473
81MethylationENLGEVLRGDRIVNT
CCHHHHHCCCCEECC		50.58115918601
88PhosphorylationRGDRIVNTPFQVLMN
CCCCEECCCHHHHCC		18.00-
98UbiquitinationQVLMNSEKKCEVLCS
HHHCCCCCCEEEEEC		63.65-
109AcetylationVLCSQSNKPVTLTVE
EEECCCCCCEEEEEE		46.2226051181
112O-linked_GlycosylationSQSNKPVTLTVEQSR
CCCCCCEEEEEEHHH		25.82OGP
126PhosphorylationRLVAERITEDYYVHL
HHHHHHCCCCCHHHH		29.0824043423
129PhosphorylationAERITEDYYVHLIAD
HHHCCCCCHHHHHHC		10.9324043423
130PhosphorylationERITEDYYVHLIADN
HHCCCCCHHHHHHCC		8.1724043423
142PhosphorylationADNLPVATRLELYSN
HCCCCCCCHHHHCCC		35.7024043423
147PhosphorylationVATRLELYSNRDSDD
CCCHHHHCCCCCCCC		8.4321406692
148PhosphorylationATRLELYSNRDSDDK
CCHHHHCCCCCCCCC		37.7021406692
159UbiquitinationSDDKKKEKDVQFEHG
CCCCHHHHCCCCCCC		72.57-
178PhosphorylationFTDVNKIYLHNHLSF
CCCCCEEEECCHHHE		11.97-
188PhosphorylationNHLSFILYYHREDME
CHHHEEEEEEHHCCH		7.75-
189PhosphorylationHLSFILYYHREDMEE
HHHEEEEEEHHCCHH		7.31-
201PhosphorylationMEEDQEHTYRVVRFE
CHHHHCCEEEEEEEE		16.5720068231
202PhosphorylationEEDQEHTYRVVRFEV
HHHHCCEEEEEEEEE		11.8820068231
220 (in isoform 1)Ubiquitination-67.1421906983
220UbiquitinationSIRLEDLKADEKSSC
EECHHHHCCCCCCCC		67.1421890473
224UbiquitinationEDLKADEKSSCTLPE
HHHCCCCCCCCCCCC		48.49-
233O-linked_GlycosylationSCTLPEGTNSSPQEI
CCCCCCCCCCCCCCC		30.20OGP
312PhosphorylationLRKDIANYNKEDDIE
HHHHHHCCCCCCCHH		20.7022817900
314 (in isoform 1)Ubiquitination-52.7621906983
314UbiquitinationKDIANYNKEDDIEDT
HHHHCCCCCCCHHHH		52.7621890473
340PhosphorylationDVFRPPQYPMILSSL
CCCCCCCHHHHHHHH		10.6724043423
345PhosphorylationPQYPMILSSLLGSGI
CCHHHHHHHHHCCHH		14.1724043423
346PhosphorylationQYPMILSSLLGSGIQ
CHHHHHHHHHCCHHH		24.9424043423
350PhosphorylationILSSLLGSGIQLFCM
HHHHHHCCHHHHHHH		32.4622210691
371PhosphorylationVAMLGMLSPSSRGAL
HHHHHCCCHHHHHHH		17.5320068231
373PhosphorylationMLGMLSPSSRGALMT
HHHCCCHHHHHHHHH		29.3222210691
374PhosphorylationLGMLSPSSRGALMTT
HHCCCHHHHHHHHHH		37.8128176443
396PhosphorylationMGVFGGFSAGRLYRT
HHHHCCCCHHHHHHH		32.8418452278
474UbiquitinationGYYFGFRKQPYDNPV
HHHHCCCCCCCCCCC		54.0521890473
474 (in isoform 1)Ubiquitination-54.0521906983
636PhosphorylationYMFVRKIYAAVKID-
HHHHHHHHHHHCCC-		7.4922817900
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 TM9S4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TM9S4_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 TM9S4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TMX2_HUMANTMX2physical
22939629
UCRI_HUMANUQCRFS1physical
22939629
ERMP1_HUMANERMP1physical
26344197
LMAN2_HUMANLMAN2physical
26344197
RAB1A_HUMANRAB1Aphysical
26344197
STX12_HUMANSTX12physical
26344197
STX7_HUMANSTX7physical
26344197
CALD1_HUMANCALD1physical
26496610
H15_HUMANHIST1H1Bphysical
26496610
KDM5A_HUMANKDM5Aphysical
26496610
RPN2_HUMANRPN2physical
26496610
S10A6_HUMANS100A6physical
26496610
CMC1_HUMANSLC25A12physical
26496610
OASL_HUMANOASLphysical
26496610
RIOK3_HUMANRIOK3physical
26496610
H1X_HUMANH1FXphysical
26496610
PHF14_HUMANPHF14physical
26496610
ABCF2_HUMANABCF2physical
26496610
SCAM3_HUMANSCAMP3physical
26496610
ATP5H_HUMANATP5Hphysical
26496610
SAC1_HUMANSACM1Lphysical
26496610
MKRN2_HUMANMKRN2physical
26496610
ITSN2_HUMANITSN2physical
26496610
FCF1_HUMANFCF1physical
26496610
SIR6_HUMANSIRT6physical
26496610
T161A_HUMANTMEM161Aphysical
26496610
CDA7L_HUMANCDCA7Lphysical
26496610
ZC3HF_HUMANZC3H15physical
26496610
RPAP3_HUMANRPAP3physical
26496610
CEP44_HUMANCEP44physical
26496610
RN170_HUMANRNF170physical
26496610
SP14L_HUMANSP140Lphysical
26496610
H2AV_HUMANH2AFVphysical
26496610
ZN800_HUMANZNF800physical
26496610
NSE2_HUMANNSMCE2physical
26496610
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
There are no disease associations of PTM sites.
Regulatory Network of TM9S4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-312, AND MASSSPECTROMETRY.

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