TM87A_HUMAN - dbPTM
TM87A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM87A_HUMAN
UniProt AC Q8NBN3
Protein Name Transmembrane protein 87A {ECO:0000305}
Gene Name TMEM87A {ECO:0000312|HGNC:HGNC:24522}
Organism Homo sapiens (Human).
Sequence Length 555
Subcellular Localization Golgi apparatus membrane
Multi-pass membrane protein .
Protein Description May be involved in retrograde transport from endosomes to the trans-Golgi network (TGN)..
Protein Sequence MAAAAWLQVLPVILLLLGAHPSPLSFFSAGPATVAAADRSKWHIPIPSGKNYFSFGKILFRNTTIFLKFDGEPCDLSLNITWYLKSADCYNEIYNFKAEEVELYLEKLKEKRGLSGKYQTSSKLFQNCSELFKTQTFSGDFMHRLPLLGEKQEAKENGTNLTFIGDKTAMHEPLQTWQDAPYIFIVHIGISSSKESSKENSLSNLFTMTVEVKGPYEYLTLEDYPLMIFFMVMCIVYVLFGVLWLAWSACYWRDLLRIQFWIGAVIFLGMLEKAVFYAEFQNIRYKGESVQGALILAELLSAVKRSLARTLVIIVSLGYGIVKPRLGVTLHKVVVAGALYLLFSGMEGVLRVTGAQTDLASLAFIPLAFLDTALCWWIFISLTQTMKLLKLRRNIVKLSLYRHFTNTLILAVAASIVFIIWTTMKFRIVTCQSDWRELWVDDAIWRLLFSMILFVIMVLWRPSANNQRFAFSPLSEEEEEDEQKEPMLKESFEGMKMRSTKQEPNGNSKVNKAQEDDLKWVEENVPSSVTDVALPALLDSDEERMITHFERSKME
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
46UbiquitinationRSKWHIPIPSGKNYF
HHCCCCCCCCCCCCE		4.1329967540
48PhosphorylationKWHIPIPSGKNYFSF
CCCCCCCCCCCCEEC		64.2224719451
56UbiquitinationGKNYFSFGKILFRNT
CCCCEECCEEEEECC		18.2029967540
79N-linked_GlycosylationEPCDLSLNITWYLKS
EECEEEEEEEEEECC		26.69UniProtKB CARBOHYD
90UbiquitinationYLKSADCYNEIYNFK
EECCCCCCHHHHCCC		19.1729967540
104PhosphorylationKAEEVELYLEKLKEK
CHHHHHHHHHHHHHH		10.18-
107UbiquitinationEVELYLEKLKEKRGL
HHHHHHHHHHHHCCC		63.3629967540
115PhosphorylationLKEKRGLSGKYQTSS
HHHHCCCCCCCCCHH		35.7429083192
117UbiquitinationEKRGLSGKYQTSSKL
HHCCCCCCCCCHHHH		30.7029967540
118PhosphorylationKRGLSGKYQTSSKLF
HCCCCCCCCCHHHHH		22.1329083192
120PhosphorylationGLSGKYQTSSKLFQN
CCCCCCCCHHHHHHH		31.7029083192
121PhosphorylationLSGKYQTSSKLFQNC
CCCCCCCHHHHHHHH		15.2229083192
122PhosphorylationSGKYQTSSKLFQNCS
CCCCCCHHHHHHHHH		36.4429083192
127N-linked_GlycosylationTSSKLFQNCSELFKT
CHHHHHHHHHHHHCC		24.77UniProtKB CARBOHYD
151UbiquitinationRLPLLGEKQEAKENG
HCCCCCCCHHHHHHC		52.2029967540
157N-linked_GlycosylationEKQEAKENGTNLTFI
CCHHHHHHCCCCEEE		62.9819349973
160N-linked_GlycosylationEAKENGTNLTFIGDK
HHHHHCCCCEEECCC		38.1819349973
168 (in isoform 2)Phosphorylation-33.6722985185
196PhosphorylationGISSSKESSKENSLS
ECCCCCCCCCCCCCC		50.90-
197PhosphorylationISSSKESSKENSLSN
CCCCCCCCCCCCCCC		45.11-
201PhosphorylationKESSKENSLSNLFTM
CCCCCCCCCCCCEEE		33.9827732954
203PhosphorylationSSKENSLSNLFTMTV
CCCCCCCCCCEEEEE		31.1627732954
207PhosphorylationNSLSNLFTMTVEVKG
CCCCCCEEEEEEEEC		18.3327732954
209PhosphorylationLSNLFTMTVEVKGPY
CCCCEEEEEEEECCC		15.5127732954
256UbiquitinationACYWRDLLRIQFWIG
HHHHHHHHHHHHHHH		5.4821890473
257UbiquitinationCYWRDLLRIQFWIGA
HHHHHHHHHHHHHHH		28.1421890473
310PhosphorylationVKRSLARTLVIIVSL
HHHHHHHHHHHHHHC		21.55-
336UbiquitinationTLHKVVVAGALYLLF
CHHHHHHHHHHHHHH		5.9721890473
336 (in isoform 3)Ubiquitination-5.9721890473
337UbiquitinationLHKVVVAGALYLLFS
HHHHHHHHHHHHHHC		12.4221890473
343UbiquitinationAGALYLLFSGMEGVL
HHHHHHHHCCCCCHH		5.6822817900
344UbiquitinationGALYLLFSGMEGVLR
HHHHHHHCCCCCHHH		36.8822817900
348UbiquitinationLLFSGMEGVLRVTGA
HHHCCCCCHHHHCCC		18.1821963094
349UbiquitinationLFSGMEGVLRVTGAQ
HHCCCCCHHHHCCCC		1.6421963094
355UbiquitinationGVLRVTGAQTDLASL
CHHHHCCCCCHHHHH		10.3423503661
356UbiquitinationVLRVTGAQTDLASLA
HHHHCCCCCHHHHHC		36.5723503661
357PhosphorylationLRVTGAQTDLASLAF
HHHCCCCCHHHHHCH		32.23-
360UbiquitinationTGAQTDLASLAFIPL
CCCCCHHHHHCHHHH		12.8123503661
361UbiquitinationGAQTDLASLAFIPLA
CCCCHHHHHCHHHHH		27.7723503661
361PhosphorylationGAQTDLASLAFIPLA
CCCCHHHHHCHHHHH		27.77-
368UbiquitinationSLAFIPLAFLDTALC
HHCHHHHHHHHHHHH		9.5222817900
369UbiquitinationLAFIPLAFLDTALCW
HCHHHHHHHHHHHHH		9.2722817900
371UbiquitinationFIPLAFLDTALCWWI
HHHHHHHHHHHHHHH		24.3922817900
372UbiquitinationIPLAFLDTALCWWIF
HHHHHHHHHHHHHHH		24.5522817900
378UbiquitinationDTALCWWIFISLTQT
HHHHHHHHHHHHHHH		0.6722817900
379UbiquitinationTALCWWIFISLTQTM
HHHHHHHHHHHHHHH		1.6322817900
397UbiquitinationKLRRNIVKLSLYRHF
HHHHHHHHHHHHHHH		28.6722817900
397 (in isoform 1)Ubiquitination-28.6721890473
398UbiquitinationLRRNIVKLSLYRHFT
HHHHHHHHHHHHHHH		2.7121890473
415PhosphorylationLILAVAASIVFIIWT
HHHHHHHHHHHHHHH		15.0030576142
423UbiquitinationIVFIIWTTMKFRIVT
HHHHHHHHCCEEEEE		11.9022817900
423 (in isoform 3)Ubiquitination-11.9021890473
424UbiquitinationVFIIWTTMKFRIVTC
HHHHHHHCCEEEEEE		2.7822817900
428UbiquitinationWTTMKFRIVTCQSDW
HHHCCEEEEEECCCH		3.1921963094
428 (in isoform 3)Ubiquitination-3.1921890473
429UbiquitinationTTMKFRIVTCQSDWR
HHCCEEEEEECCCHH		3.6921963094
435UbiquitinationIVTCQSDWRELWVDD
EEEECCCHHHHHHHH		10.8233845483
435 (in isoform 3)Ubiquitination-10.82-
436UbiquitinationVTCQSDWRELWVDDA
EEECCCHHHHHHHHH		33.8323503661
440UbiquitinationSDWRELWVDDAIWRL
CCHHHHHHHHHHHHH		8.1523503661
441UbiquitinationDWRELWVDDAIWRLL
CHHHHHHHHHHHHHH		28.2123503661
448UbiquitinationDDAIWRLLFSMILFV
HHHHHHHHHHHHHHH		1.9322817900
449UbiquitinationDAIWRLLFSMILFVI
HHHHHHHHHHHHHHH		5.7322817900
451 (in isoform 3)Ubiquitination-2.1221890473
451UbiquitinationIWRLLFSMILFVIMV
HHHHHHHHHHHHHHH		2.1227667366
452UbiquitinationWRLLFSMILFVIMVL
HHHHHHHHHHHHHHH		2.3322817900
458 (in isoform 3)Ubiquitination-2.9721890473
458UbiquitinationMILFVIMVLWRPSAN
HHHHHHHHHHCCCCC		2.9722817900
459UbiquitinationILFVIMVLWRPSANN
HHHHHHHHHCCCCCC		1.4522817900
472PhosphorylationNNQRFAFSPLSEEEE
CCCCEEECCCCHHHH		22.8530266825
475PhosphorylationRFAFSPLSEEEEEDE
CEEECCCCHHHHHHH		46.4723401153
479PhosphorylationSPLSEEEEEDEQKEP
CCCCHHHHHHHHHCC		74.2232142685
484 (in isoform 1)Ubiquitination-62.8321890473
484UbiquitinationEEEEDEQKEPMLKES
HHHHHHHHCCHHHHH		62.8322817900
485UbiquitinationEEEDEQKEPMLKESF
HHHHHHHCCHHHHHH		35.3222817900
487SulfoxidationEDEQKEPMLKESFEG
HHHHHCCHHHHHHCC		9.7721406390
489 (in isoform 1)Ubiquitination-45.0921890473
489UbiquitinationEQKEPMLKESFEGMK
HHHCCHHHHHHCCCC		45.0921906983
490UbiquitinationQKEPMLKESFEGMKM
HHCCHHHHHHCCCCC		57.6121963094
491PhosphorylationKEPMLKESFEGMKMR
HCCHHHHHHCCCCCC		27.3229214152
496UbiquitinationKESFEGMKMRSTKQE
HHHHCCCCCCCCCCC		41.8633845483
497UbiquitinationESFEGMKMRSTKQEP
HHHCCCCCCCCCCCC		2.8023503661
501UbiquitinationGMKMRSTKQEPNGNS
CCCCCCCCCCCCCCC		54.6423503661
502UbiquitinationMKMRSTKQEPNGNSK
CCCCCCCCCCCCCCC		72.0423503661
509UbiquitinationQEPNGNSKVNKAQED
CCCCCCCCCCHHHHH		54.5522817900
510UbiquitinationEPNGNSKVNKAQEDD
CCCCCCCCCHHHHHH		9.9822817900
512UbiquitinationNGNSKVNKAQEDDLK
CCCCCCCHHHHHHHH		55.2021906983
512 (in isoform 1)Ubiquitination-55.2021890473
513UbiquitinationGNSKVNKAQEDDLKW
CCCCCCHHHHHHHHH		16.8822817900
519 (in isoform 1)Ubiquitination-57.0721890473
519UbiquitinationKAQEDDLKWVEENVP
HHHHHHHHHHHHHCC		57.0722817900
520UbiquitinationAQEDDLKWVEENVPS
HHHHHHHHHHHHCCC		15.2822817900
527PhosphorylationWVEENVPSSVTDVAL
HHHHHCCCCHHHCHH		32.9130266825
528PhosphorylationVEENVPSSVTDVALP
HHHHCCCCHHHCHHH		23.9830266825
530PhosphorylationENVPSSVTDVALPAL
HHCCCCHHHCHHHHH		27.0630266825
540PhosphorylationALPALLDSDEERMIT
HHHHHCCCCHHHHHH		47.0622167270
547PhosphorylationSDEERMITHFERSKM
CCHHHHHHHHHHHHC		15.9228450419
552PhosphorylationMITHFERSKME----
HHHHHHHHHCC----		29.2028555341
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 TM87A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TM87A_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 TM87A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADAS_HUMANAGPSphysical
26344197
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 TM87A_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-157 AND ASN-160, 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 SER-540, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND MASSSPECTROMETRY.
"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-540, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND MASSSPECTROMETRY.

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