GLHA_HUMAN - dbPTM
GLHA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLHA_HUMAN
UniProt AC P01215
Protein Name Glycoprotein hormones alpha chain
Gene Name CGA
Organism Homo sapiens (Human).
Sequence Length 116
Subcellular Localization Secreted.
Protein Description
Protein Sequence MDYYRKYAAIFLVTLSVFLHVLHSAPDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS
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
63O-linked_GlycosylationCFSRAYPTPLRSKKT
HHHCCCCCCCCCCCE
23.442538306
63PhosphorylationCFSRAYPTPLRSKKT
HHHCCCCCCCCCCCE
23.4429214152
68AcetylationYPTPLRSKKTMLVQK
CCCCCCCCCEEEEEC
45.928307955
69AcetylationPTPLRSKKTMLVQKN
CCCCCCCCEEEEECC
40.178307955
75AcetylationKKTMLVQKNVTSEST
CCEEEEECCCCCCCE
46.008307955
76N-linked_GlycosylationKTMLVQKNVTSESTC
CEEEEECCCCCCCEE
25.807544284
94PhosphorylationKSYNRVTVMGGFKVE
EECCEEEEEECEEEE
2.842466636
99AcetylationVTVMGGFKVENHTAC
EEEEECEEEECCEEE
52.498307955
102N-linked_GlycosylationMGGFKVENHTACHCS
EECEEEECCEEEEEE
40.5710821673
107N-linked_GlycosylationVENHTACHCSTCYYH
EECCEEEEEEEEEEE
13.1915662415
107N-linked_GlycosylationVENHTACHCSTCYYH
EECCEEEEEEEEEEE
13.1915662415
133N-linked_Glycosylation------------------------
------------------------
15662415
133N-linked_Glycosylation------------------------
------------------------
15662415

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 GLHA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLHA_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 GLHA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTN_HUMANPTNphysical
16169070
FSHB_HUMANFSHBphysical
11222739

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 GLHA_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structure of human follicle-stimulating hormone in complex with itsreceptor.";
Fan Q.R., Hendrickson W.A.;
Nature 433:269-277(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 25-116 IN COMPLEX WITH FSHBAND FSHR, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-76 AND ASN-102.

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