INHBA_HUMAN - dbPTM
INHBA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INHBA_HUMAN
UniProt AC P08476
Protein Name Inhibin beta A chain
Gene Name INHBA
Organism Homo sapiens (Human).
Sequence Length 426
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 MPLLWLRGFLLASCWIIVRSSPTPGSEGHSAAPDCPSCALAALPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEEEGEGKKKGGGEGGAGADEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
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_GlycosylationTPGSEGHSAAPDCPS
CCCCCCCCCCCCCCC
36.66OGP
50PhosphorylationLPKDVPNSQPEMVEA
CCCCCCCCCHHHHHH
40.8329978859
50O-linked_GlycosylationLPKDVPNSQPEMVEA
CCCCCCCCCHHHHHH
40.8330379171
94UbiquitinationIRKLHVGKVGENGYV
HHHCCCCCCCCCCCE
46.08-
125PhosphorylationEQTSEIITFAESGTA
HHHHHHHHHHHHCCC
23.5829759185
129PhosphorylationEIITFAESGTARKTL
HHHHHHHHCCCCEEE
37.7125219547
131PhosphorylationITFAESGTARKTLHF
HHHHHHCCCCEEEEE
32.3525219547
135PhosphorylationESGTARKTLHFEISK
HHCCCCEEEEEEEEC
21.6629759185
141PhosphorylationKTLHFEISKEGSDLS
EEEEEEEECCCCCCE
19.9125219547
165N-linked_GlycosylationFLKVPKANRTRTKVT
EEECCCCCCCCCEEE
52.57UniProtKB CARBOHYD
172PhosphorylationNRTRTKVTIRLFQQQ
CCCCCEEEEEHHHHC
11.2624719451
188PhosphorylationHPQGSLDTGEEAEEV
CCCCCCCCCHHHHHH
52.3524961811
207PhosphorylationERSELLLSEKVVDAR
CHHEEHHEEEECCCC
35.0324719451
226PhosphorylationHVFPVSSSIQRLLDQ
EEEECCHHHHHHHHC
18.4221406692
400PhosphorylationPTKLRPMSMLYYDDG
CCCCCCCEEEEEECC
14.3328270605
403PhosphorylationLRPMSMLYYDDGQNI
CCCCEEEEEECCCCE
9.0128270605
404PhosphorylationRPMSMLYYDDGQNII
CCCEEEEEECCCCEE
12.0028270605

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 INHBA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INHBA_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 INHBA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AVR2A_HUMANACVR2Aphysical
9202237
AVR2B_HUMANACVR2Bphysical
9202237
ACV1B_HUMANACVR1Bphysical
9202237

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INHBA_HUMAN

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Related Literatures of Post-Translational Modification

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