GHR_HUMAN - dbPTM
GHR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GHR_HUMAN
UniProt AC P10912
Protein Name Growth hormone receptor
Gene Name GHR
Organism Homo sapiens (Human).
Sequence Length 638
Subcellular Localization Cell membrane
Single-pass type I membrane protein. On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway..
Isoform 2: Cell membrane
Single-pass type I membrane p
Protein Description Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to the JAK2/STAT5 pathway (By similarity).; The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling.; Isoform 2 up-regulates the production of GHBP and acts as a negative inhibitor of GH signaling..
Protein Sequence MDLWQLLLTLALAGSSDAFSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFYFPWLLIIIFGIFGLTVMLFVFLFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIHDSYKPEFHSDDSWVEFIELDIDEPDEKTEESDTDRLLSSDHEKSHSNLGVKDGDSGRTSCCEPDILETDFNANDIHEGTSEVAQPQRLKGEADLLCLDQKNQNNSPYHDACPATQQPSVIQAEKNKPQPLPTEGAESTHQAAHIQLSNPSSLSNIDFYAQVSDITPAGSVVLSPGQKNKAGMSQCDMHPEMVSLCQENFLMDNAYFCEADAKKCIPVAPHIKVESHIQPSLNQEDIYITTESLTTAAGRPGTGEHVPGSEMPVPDYTSIHIVQSPQGLILNATALPLPDKEFLSSCGYVSTDQLNKIMP
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
30O-linked_GlycosylationEATAAILSRAPWSLQ
HHHHHHHHCCCCCCC		21.93OGP
46N-linked_GlycosylationVNPGLKTNSSKEPKF
CCCCCCCCCCCCCCC		42.57UniProtKB CARBOHYD
76PhosphorylationTDEVHHGTKNLGPIQ
ECCCCCCCCCCCCEE		16.65-
115N-linked_GlycosylationGENSCYFNSSFTSIW
CCCCCCCCCCCCEEE		15.40UniProtKB CARBOHYD
156N-linked_GlycosylationPDPPIALNWTLLNVS
CCCCEECCEEEEEEE		22.21UniProtKB CARBOHYD
161N-linked_GlycosylationALNWTLLNVSLTGIH
ECCEEEEEEEECCCC		25.17UniProtKB CARBOHYD
200N-linked_GlycosylationELQYKEVNETKWKMM
EEEECCCCCCCCEEC		52.92UniProtKB CARBOHYD
218PhosphorylationLTTSVPVYSLKVDKE
CCCCCEEEEEECCCE		11.38-
219PhosphorylationTTSVPVYSLKVDKEY
CCCCEEEEEECCCEE		23.1924719451
224UbiquitinationVYSLKVDKEYEVRVR
EEEEECCCEEEEEEE		66.25-
226PhosphorylationSLKVDKEYEVRVRSK
EEECCCEEEEEEEEC		26.01-
288PhosphorylationMLFVFLFSKQQRIKM
HHHHHHHCCCCCEEE		31.5324719451
324PhosphorylationGKLEEVNTILAIHDS
CCHHHHHEEEEEECC		23.6522210691
331PhosphorylationTILAIHDSYKPEFHS
EEEEEECCCCCCCCC		22.3924275569
332PhosphorylationILAIHDSYKPEFHSD
EEEEECCCCCCCCCC		36.309121492
341PhosphorylationPEFHSDDSWVEFIEL
CCCCCCCCCEEEEEE		37.708421103
357PhosphorylationIDEPDEKTEESDTDR
CCCCCCCCCCCHHHH		42.83-
367PhosphorylationSDTDRLLSSDHEKSH
CHHHHHHCCCCHHHH		38.0122817900
368PhosphorylationDTDRLLSSDHEKSHS
HHHHHHCCCCHHHHC		42.8522817900
373PhosphorylationLSSDHEKSHSNLGVK
HCCCCHHHHCCCCCC		29.2126437602
375PhosphorylationSDHEKSHSNLGVKDG
CCCHHHHCCCCCCCC		40.6226437602
487PhosphorylationSLSNIDFYAQVSDIT
HHCCCEEEEEECCCC		7.749121492
534PhosphorylationNFLMDNAYFCEADAK
CCCCCCEEEECCCHH		18.288647880
566PhosphorylationSLNQEDIYITTESLT
CCCCCCEEEEEHHHH		12.448647880
595PhosphorylationSEMPVPDYTSIHIVQ
CCCCCCCCCEEEEEE		9.05-
627PhosphorylationEFLSSCGYVSTDQLN
HHHHHCCCCCHHHHH		8.788647880
629PhosphorylationLSSCGYVSTDQLNKI
HHHCCCCCHHHHHHC		20.1327251275
630PhosphorylationSSCGYVSTDQLNKIM
HHCCCCCHHHHHHCC		20.0927251275
637PhosphorylationTDQLNKIMP------
HHHHHHCCC------		3.2627251275
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
332YPhosphorylationKinaseJAK2O60674
PhosphoELM
487YPhosphorylationKinaseJAK2O60674
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseSOCS2O14508
PMID:21980433
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:23607312
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GHR_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 GHR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SGTA_HUMANSGTAphysical
12735788
JAK2_HUMANJAK2physical
7540178
CISH_HUMANCISHphysical
10585430
SOCS1_HUMANSOCS1physical
10585430
SOCS3_HUMANSOCS3physical
10585430
SOCS2_HUMANSOCS2physical
10585430
STAT3_HUMANSTAT3physical
8923468
STA5B_HUMANSTAT5Bphysical
8923468
JAK2_HUMANJAK2physical
8063815
JAK1_HUMANJAK1physical
10502458
JAK2_HUMANJAK2physical
10502458
TYK2_HUMANTYK2physical
10502458
PTN2_HUMANPTPN2physical
12907755
PTPRB_HUMANPTPRBphysical
12907755
PTN1_HUMANPTPN1physical
12907755
DUS7_HUMANDUSP7physical
12907755
PTN9_HUMANPTPN9physical
12907755
PTN3_HUMANPTPN3physical
12907755
PTN13_HUMANPTPN13physical
12907755
CHIP_HUMANSTUB1physical
22433856
JAK2_HUMANJAK2physical
21347402
SOCS2_HUMANSOCS2physical
12135564
SKP1_HUMANSKP1physical
23607312
FBW1A_HUMANBTRCphysical
23607312
GHR_HUMANGHRphysical
24280222
FBW1B_HUMANFBXW11physical
24280222
JAK2_HUMANJAK2physical
24280222
Drug and Disease Associations
Kegg Disease
H00254 Pituitary Dwarfism (PD); Isolated growth hormone deficiency (IGHD); Short Stature and Pituitary Defe
OMIM Disease
262500Laron syndrome (LARS)
604271Growth hormone insensitivity, partial (GHIP)
Kegg Drug
D02691 Somatropin (genetical recombination) (JAN); Human growth hormone (JAN); Somatropin (USP/INN); Asella
D05394 Pegvisomant (genetical recombination) (JAN); Pegvisomant (USAN/INN); Somavent (TN)
D05884 Somatrem (genetical recombination) (JAN); Somatrem (USAN); Protropin (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GHR_HUMAN

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Related Literatures of Post-Translational Modification

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