INHA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: INHA_HUMAN
• UniProt AC: P05111
• Protein Name: Inhibin alpha chain
• Gene Name: INHA
• Organism: Homo sapiens (Human).
• Sequence Length: 366
• Subcellular Localization: Secreted.
• Protein Description: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins..
• Protein Sequence: MVLHLLLFLLLTPQGGHSCQGLELARELVLAKVRALFLDALGPPAVTREGGDPGVRRLPRRHALGGFTHRGSEPEEEEDVSQAILFPATDASCEDKSAARGLAQEAEEGLFRYMFRPSQHTRSRQVTSAQLWFHTGLDRQGTAASNSSEPLLGLLALSPGGPVAVPMSLGHAPPHWAVLHLATSALSLLTHPVLVLLLRCPLCTCSARPEATPFLVAHTRTRPPSGGERARRSTPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIPPNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI

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
146	N-linked_Glycosylation	RQGTAASNSSEPLLG CCCCCCCCCCCCCHH	44.84	UniProtKB CARBOHYD
219	Phosphorylation	TPFLVAHTRTRPPSG CCEEEEECCCCCCCC	24.81	27251275
221	Phosphorylation	FLVAHTRTRPPSGGE EEEEECCCCCCCCCC	49.00	27251275
225	Phosphorylation	HTRTRPPSGGERARR ECCCCCCCCCCCCCC	63.21	-
233	Phosphorylation	GGERARRSTPLMSWP CCCCCCCCCCCCCCC	28.90	22817900
234	Phosphorylation	GERARRSTPLMSWPW CCCCCCCCCCCCCCC	20.73	22817900
244	Phosphorylation	MSWPWSPSALRLLQR CCCCCCHHHHHHHHC	34.13	22817900
268	N-linked_Glycosylation	NCHRVALNISFQELG CCCEEEEEEEHHHHC	20.37	8885240
302	N-linked_Glycosylation	CGLHIPPNLSLPVPG CCCCCCCCCCCCCCC	36.59	8885240
302	N-linked_Glycosylation	CGLHIPPNLSLPVPG CCCCCCCCCCCCCCC	36.59	8885240

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of INHA_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of INHA_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of INHA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIAH1_HUMAN	SIAH1	physical	25416956
GRP78_HUMAN	HSPA5	physical	26186194
PDIA3_HUMAN	PDIA3	physical	26186194
CALR_HUMAN	CALR	physical	26186194
NEMO_HUMAN	IKBKG	physical	26186194
PDIA3_HUMAN	PDIA3	physical	28514442
CALR_HUMAN	CALR	physical	28514442
GRP78_HUMAN	HSPA5	physical	28514442
NEMO_HUMAN	IKBKG	physical	28514442

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Characterization and determination of the biological activities ofnoncleavable high molecular weight forms of inhibin A and activin A.";
Mason A.J., Farnworth P.G., Sullivan J.;
Mol. Endocrinol. 10:1055-1065(1996).
Cited for: PARTIAL PROTEIN SEQUENCE, PROTEOLYTIC PROCESSING, GLYCOSYLATION ATASN-268 AND ASN-302, AND MUTAGENESIS.
PubMed: 8885240