TMM62_HUMAN - dbPTM
TMM62_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMM62_HUMAN
UniProt AC Q0P6H9
Protein Name Transmembrane protein 62
Gene Name TMEM62
Organism Homo sapiens (Human).
Sequence Length 643
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MAAVLALRVVAGLAAAALVAMLLEHYGLAGQPSPLPRPAPPRRPHPAPGPGDSNIFWGLQISDIHLSRFRDPGRAVDLEKFCSETIDIIQPALVLATGDLTDAKTKEQLGSRQHEVEWQTYQGILKKTRVMEKTKWLDIKGNHDAFNIPSLDSIKNYYRKYSAVRRDGSFHYVHSTPFGNYSFICVDATVNPGPKRPYNFFGILDKKKMEELLLLAKESSRSNHTIWFGHFTTSTILSPSPGIRSIMSSAIAYLCGHLHTLGGLMPVLHTRHFQGTLELEVGDWKDNRRYRIFAFDHDLFSFADLIFGKWPVVLITNPKSLLYSCGEHEPLERLLHSTHIRVLAFSLSSITSVTVKIDGVHLGQAVHVSGPIFVLKWNPRNYSSGTHNIEVIVQDSAGRSKSVHHIFSVQENNHLSFDPLASFILRTDHYIMARVLFVLIVLSQLTILIIFRYRGYPELKEPSGFINLTSFSLHVLSKINIFYYSVLLLTLYTVLGPWFFGEIIDGKFGCCFSFGIFVNGHFLQGSITFIIGILQLAFFNIPLMAYMCWSLLQRCFGHNFRSHLHQRKYLKIMPVHLLMLLLYIWQVYSCYFLYATYGTLAFLFSPLRTWLTLLTPVLIRYVWTLNSTKFGIFMVQLKSHLSS
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
33PhosphorylationYGLAGQPSPLPRPAP
HCCCCCCCCCCCCCC
31.0524719451
153PhosphorylationFNIPSLDSIKNYYRK
CCCCCHHHHHHHHHH
40.5322210691
180N-linked_GlycosylationVHSTPFGNYSFICVD
EECCCCCCEEEEEEE
29.6519159218
354PhosphorylationLSSITSVTVKIDGVH
HHHCCEEEEEECCEE
18.82-
453PhosphorylationTILIIFRYRGYPELK
HHHHHHHHCCCCCCC
9.5329116813
467N-linked_GlycosylationKEPSGFINLTSFSLH
CCCCCCEECCHHHHH
34.70UniProtKB CARBOHYD
469PhosphorylationPSGFINLTSFSLHVL
CCCCEECCHHHHHHH
24.2029116813
562PhosphorylationCFGHNFRSHLHQRKY
HHCCCHHHHHHHHHH
26.6826074081
569PhosphorylationSHLHQRKYLKIMPVH
HHHHHHHHHHHHHHH
18.5426074081
626N-linked_GlycosylationIRYVWTLNSTKFGIF
HHHHHHCCCCCEEEE
40.01UniProtKB CARBOHYD

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 TMM62_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMM62_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 TMM62_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NPL4_HUMANNPLOC4physical
26186194
UFD1_HUMANUFD1Lphysical
26186194
HERC3_HUMANHERC3physical
26186194

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 TMM62_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-180, AND MASSSPECTROMETRY.

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