OSTM1_HUMAN - dbPTM
OSTM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSTM1_HUMAN
UniProt AC Q86WC4
Protein Name Osteopetrosis-associated transmembrane protein 1
Gene Name OSTM1
Organism Homo sapiens (Human).
Sequence Length 334
Subcellular Localization Lysosome membrane
Single-pass type I membrane protein . Requires CLCN7 to travel to lysosomes.
Protein Description Required for osteoclast and melanocyte maturation and function..
Protein Sequence MEPGPTAAQRRCSLPPWLPLGLLLWSGLALGALPFGSSPHRVFHDLLSEQQLLEVEDLSLSLLQGGGLGPLSLPPDLPDLDPECRELLLDFANSSAELTGCLVRSARPVRLCQTCYPLFQQVVSKMDNISRAAGNTSESQSCARSLLMADRMQIVVILSEFFNTTWQEANCANCLTNNSEELSNSTVYFLNLFNHTLTCFEHNLQGNAHSLLQTKNYSEVCKNCREAYKTLSSLYSEMQKMNELENKAEPGTHLCIDVEDAMNITRKLWSRTFNCSVPCSDTVPVIAVSVFILFLPVVFYLSSFLHSEQKKRKLILPKRLKSSTSFANIQENSN
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
93N-linked_GlycosylationELLLDFANSSAELTG
HHHHHHHHCCHHHHC		36.17UniProtKB CARBOHYD
114PhosphorylationRPVRLCQTCYPLFQQ
CHHHHHHHHHHHHHH		17.0121082442
116PhosphorylationVRLCQTCYPLFQQVV
HHHHHHHHHHHHHHH		13.3221082442
125UbiquitinationLFQQVVSKMDNISRA
HHHHHHHCHHHHHHH		38.3723503661
128N-linked_GlycosylationQVVSKMDNISRAAGN
HHHHCHHHHHHHCCC		30.54UniProtKB CARBOHYD
135N-linked_GlycosylationNISRAAGNTSESQSC
HHHHHCCCCCHHHHH		35.39UniProtKB CARBOHYD
163N-linked_GlycosylationVILSEFFNTTWQEAN
HHHHHHHCCHHHHHH		41.75UniProtKB CARBOHYD
177N-linked_GlycosylationNCANCLTNNSEELSN
HHHHHHCCCCHHHHH		36.76UniProtKB CARBOHYD
184N-linked_GlycosylationNNSEELSNSTVYFLN
CCCHHHHHCHHHHHH		55.08UniProtKB CARBOHYD
194N-linked_GlycosylationVYFLNLFNHTLTCFE
HHHHHHHCHHHHHHH		30.33UniProtKB CARBOHYD
216N-linked_GlycosylationHSLLQTKNYSEVCKN
HHHHHCCCHHHHHHH		49.29UniProtKB CARBOHYD
222UbiquitinationKNYSEVCKNCREAYK
CCHHHHHHHHHHHHH		65.34-
228PhosphorylationCKNCREAYKTLSSLY
HHHHHHHHHHHHHHH		10.3526074081
229UbiquitinationKNCREAYKTLSSLYS
HHHHHHHHHHHHHHH		50.46-
230PhosphorylationNCREAYKTLSSLYSE
HHHHHHHHHHHHHHH		21.1326074081
232PhosphorylationREAYKTLSSLYSEMQ
HHHHHHHHHHHHHHH		24.4326074081
233PhosphorylationEAYKTLSSLYSEMQK
HHHHHHHHHHHHHHH		34.1426074081
235PhosphorylationYKTLSSLYSEMQKMN
HHHHHHHHHHHHHHH		12.4426074081
236PhosphorylationKTLSSLYSEMQKMNE
HHHHHHHHHHHHHHH		31.7026074081
240UbiquitinationSLYSEMQKMNELENK
HHHHHHHHHHHHHHC		42.24-
263N-linked_GlycosylationIDVEDAMNITRKLWS
EEHHHHHHHHHHHHH		33.91UniProtKB CARBOHYD
274N-linked_GlycosylationKLWSRTFNCSVPCSD
HHHHHCCCCCCCCCC		19.28UniProtKB CARBOHYD
318UbiquitinationKRKLILPKRLKSSTS
HHHCCCCHHHCCCCC		67.9022817900
321MethylationLILPKRLKSSTSFAN
CCCCHHHCCCCCCCC		46.5224498891
321UbiquitinationLILPKRLKSSTSFAN
CCCCHHHCCCCCCCC		46.5221906983
322PhosphorylationILPKRLKSSTSFANI
CCCHHHCCCCCCCCH		43.3625159151
323PhosphorylationLPKRLKSSTSFANIQ
CCHHHCCCCCCCCHH		26.8725159151
324PhosphorylationPKRLKSSTSFANIQE
CHHHCCCCCCCCHHC		34.6525159151
325PhosphorylationKRLKSSTSFANIQEN
HHHCCCCCCCCHHCC		25.0625159151
333PhosphorylationFANIQENSN------
CCCHHCCCC------		43.0730266825
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 OSTM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSTM1_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 OSTM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RGS17_HUMANRGS17physical
12826607
RGS20_HUMANRGS20physical
12826607
RGS19_HUMANRGS19physical
12826607
GPSM1_HUMANGPSM1physical
12826607
Drug and Disease Associations
Kegg Disease
H00436 Osteopetrosis, including: Osteopetrosis, severe neonatal or infantile forms; Osteopetrosis, intermed
OMIM Disease
259720Osteopetrosis, autosomal recessive 5 (OPTB5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OSTM1_HUMAN

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Related Literatures of Post-Translational Modification
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-322 AND SER-325, ANDMASS SPECTROMETRY.
"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-322; SER-323; SER-325AND SER-333, AND MASS SPECTROMETRY.
"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-322; SER-323; SER-325AND SER-333, AND MASS SPECTROMETRY.

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