SOMA_HUMAN - dbPTM
SOMA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SOMA_HUMAN
UniProt AC P01241
Protein Name Somatotropin
Gene Name GH1
Organism Homo sapiens (Human).
Sequence Length 217
Subcellular Localization Secreted.
Protein Description Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues..
Protein Sequence MATGSRTSLLLAFGLLCLPWLQEGSAFPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
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
3Phosphorylation-----MATGSRTSLL
-----CCCCCHHHHH		34.1024043423
5Phosphorylation---MATGSRTSLLLA
---CCCCCHHHHHHH		28.2024043423
7Phosphorylation-MATGSRTSLLLAFG
-CCCCCHHHHHHHHH		25.9824043423
8PhosphorylationMATGSRTSLLLAFGL
CCCCCHHHHHHHHHH		18.8624043423
14SulfoxidationTSLLLAFGLLCLPWL
HHHHHHHHHHHHHHH		16.4821249719
25PhosphorylationLPWLQEGSAFPTIPL
HHHHHCCCCCCCCCH		26.4524043423
29PhosphorylationQEGSAFPTIPLSRLF
HCCCCCCCCCHHHHC		28.8624043423
33PhosphorylationAFPTIPLSRLFDNAM
CCCCCCHHHHCHHHH		22.9124043423
64AcetylationFEEAYIPKEQKYSFL
HHHHHCCHHHHCCCH		64.323122756
68PhosphorylationYIPKEQKYSFLQNPQ
HCCHHHHCCCHHCCC		12.3519702290
77PhosphorylationFLQNPQTSLCFSESI
CHHCCCCCEEEECCC		20.2115717326
81PhosphorylationPQTSLCFSESIPTPS
CCCCEEEECCCCCCC		29.4514997482
93PhosphorylationTPSNREETQQKSNLE
CCCCHHHHHHHHHHH		31.39-
96AcetylationNREETQQKSNLELLR
CHHHHHHHHHHHHHH		31.343122756
96MethylationNREETQQKSNLELLR
CHHHHHHHHHHHHHH		31.3415707495
97PhosphorylationREETQQKSNLELLRI
HHHHHHHHHHHHHHH		42.16-
125SulfoxidationFLRSVFANSLVYGAS
HHHHHHCCHHHHCCC		25.1421249719
126PhosphorylationLRSVFANSLVYGASD
HHHHHCCHHHHCCCC		18.7829691806
129PhosphorylationVFANSLVYGASDSNV
HHCCHHHHCCCCCCH		16.5629691806
132PhosphorylationNSLVYGASDSNVYDL
CHHHHCCCCCCHHHH		36.8929691806
134PhosphorylationLVYGASDSNVYDLLK
HHHCCCCCCHHHHHH		26.2129691806
137PhosphorylationGASDSNVYDLLKDLE
CCCCCCHHHHHHHHH		12.7229691806
141AcetylationSNVYDLLKDLEEGIQ
CCHHHHHHHHHHHHH		68.513122756
163DeamidationDGSPRTGQIFKQTYS
CCCCCCCHHHHHHHH		37.017028740
163Deamidated glutamineDGSPRTGQIFKQTYS
CCCCCCCHHHHHHHH		37.01-
166AcetylationPRTGQIFKQTYSKFD
CCCCHHHHHHHHCCC		43.273122756
174PhosphorylationQTYSKFDTNSHNDDA
HHHHCCCCCCCCHHH		41.5829691806
176PhosphorylationYSKFDTNSHNDDALL
HHCCCCCCCCHHHHH		26.2629691806
178Deamidated asparagineKFDTNSHNDDALLKN
CCCCCCCCHHHHHHH		48.99-
178DeamidationKFDTNSHNDDALLKN
CCCCCCCCHHHHHHH		48.997028740
194AcetylationGLLYCFRKDMDKVET
CEEEEEECCHHHHHH		36.833122756
198AcetylationCFRKDMDKVETFLRI
EEECCHHHHHHHHHH		35.023122756
214PhosphorylationQCRSVEGSCGF----
HHHCCCCCCCC----		9.5029691806
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 SOMA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SOMA_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 SOMA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LKHA4_HUMANLTA4Hphysical
17353931
STRAP_HUMANSTRAPphysical
17353931
GHR_HUMANGHRphysical
7862673
SHC1_HUMANSHC1physical
7535773
GHR_HUMANGHRphysical
17500058
GHR_HUMANGHRphysical
24280222
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
262400Growth hormone deficiency, isolated, 1A (IGHD1A)
612781Growth hormone deficiency, isolated, 1B (IGHD1B)
262650Kowarski syndrome (KWKS)
173100Growth hormone deficiency, isolated, 2 (IGHD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SOMA_HUMAN

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Related Literatures of Post-Translational Modification
Deamidation
ReferencePubMed
"Altered proteolytic cleavage of human growth hormone as a result ofdeamidation.";
Lewis U.J., Singh R.N., Bonewald L.F., Seavey B.K.;
J. Biol. Chem. 256:11645-11650(1981).
Cited for: DEAMIDATION AT GLN-163 AND ASN-178.
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-176, ANDMASS SPECTROMETRY.
"Identification and characterization of phosphorylated proteins in thehuman pituitary.";
Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.;
Proteomics 4:587-598(2004).
Cited for: PHOSPHORYLATION AT SER-132 AND SER-176.

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