P09529 (INHBB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inhibin beta B chain

Alternative name(s):
Activin beta-B chain

Gene names

Name:

INHBB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Dimeric, linked by one or more disulfide bonds. Inhibin A is a dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B. Activin A is a homodimer of beta-A. Activin B is a homodimer of beta-B. Activin AB is a dimer of beta-A and beta-B. Interacts with FST and FSTL3. Ref.8
Subcellular location	Secreted.
Sequence similarities	Belongs to the TGF-beta family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Growth factor Hormone
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activin receptor signaling pathway Inferred from direct assay PubMed 16650820. Source: UniProtKB cellular response to insulin stimulus Inferred from sequence or structural similarity. Source: UniProtKB cellular response to leptin stimulus Inferred from electronic annotation. Source: Compara cellular response to starvation Inferred from sequence or structural similarity. Source: UniProtKB defense response Traceable author statement PubMed 3122219. Source: UniProtKB fat cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB growth Inferred from electronic annotation. Source: InterPro negative regulation of follicle-stimulating hormone secretion Inferred from physical interaction PubMed 3122219. Source: UniProtKB negative regulation of hepatocyte growth factor biosynthetic process Inferred from direct assay PubMed 12419948. Source: UniProtKB negative regulation of insulin secretion Inferred from sequence or structural similarity. Source: UniProtKB oocyte development Inferred from electronic annotation. Source: Compara ovarian follicle development Non-traceable author statement PubMed 12790766. Source: UniProtKB positive regulation of follicle-stimulating hormone secretion Inferred from physical interaction PubMed 3122219. Source: UniProtKB positive regulation of ovulation Inferred from sequence or structural similarity. Source: UniProtKB regulation of apoptotic process Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular region Traceable author statement PubMed 3122219. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay PubMed 16650820. Source: UniProtKB
Molecular_function	cytokine activity Traceable author statement PubMed 3122219. Source: UniProtKB hormone activity Traceable author statement PubMed 3122219. Source: UniProtKB host cell surface receptor binding Traceable author statement PubMed 12456957. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Propeptide	29 – 292	264	Potential		PRO_0000033722
	Chain	293 – 407	115	Inhibin beta B chain		PRO_0000033723
Amino acid modifications
	Glycosylation	93	1	N-linked (GlcNAc...) Potential
	Disulfide bond	296 ↔ 304		By similarity
	Disulfide bond	303 ↔ 372		By similarity
	Disulfide bond	332 ↔ 404		By similarity
	Disulfide bond	336 ↔ 406		By similarity
	Disulfide bond	371		Interchain By similarity
Experimental info
	Sequence conflict	39	1	P → Q in AAH30029. Ref.4
	Sequence conflict	47	1	S → A in AAA59170. Ref.5
	Sequence conflict	295	1	E → G AA sequence Ref.7
	Sequence conflict	326	1	G → S in AAH30029. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P09529 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 90316C83597BA6B4	FASTA	407	45,122
	10 20 30 40 50 60 MDGLPGRALG AACLLLLAAG WLGPEAWGSP TPPPTPAAPP PPPPPGSPGG SQDTCTSCGG 70 80 90 100 110 120 FRRPEELGRV DGDFLEAVKR HILSRLQMRG RPNITHAVPK AAMVTALRKL HAGKVREDGR 130 140 150 160 170 180 VEIPHLDGHA SPGADGQERV SEIISFAETD GLASSRVRLY FFISNEGNQN LFVVQASLWL 190 200 210 220 230 240 YLKLLPYVLE KGSRRKVRVK VYFQEQGHGD RWNMVEKRVD LKRSGWHTFP LTEAIQALFE 250 260 270 280 290 300 RGERRLNLDV QCDSCQELAV VPVFVDPGEE SHRPFVVVQA RLGDSRHRIR KRGLECDGRT 310 320 330 340 350 360 NLCCRQQFFI DFRLIGWNDW IIAPTGYYGN YCEGSCPAYL AGVPGSASSF HTAVVNQYRM 370 380 390 400 RGLNPGTVNS CCIPTKLSTM SMLYFDDEYN IVKRDVPNMI VEECGCA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Activin B: precursor sequences, genomic structure and in vitro activities." Mason A.J., Berkemeier L.M., Schmelzer C.H., Schwall R.H. Mol. Endocrinol. 3:1352-1358(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Characterization and regulation of testicular inhibin beta-subunit mRNA." Feng Z.M., Bardin C.W., Chen C.L. Mol. Endocrinol. 3:939-948(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-407.
[6]	"Structure of two human ovarian inhibins." Mason A.J., Niall H.D., Seeburg P.H. Biochem. Biophys. Res. Commun. 135:957-964(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 55-407.
[7]	"Purification and characterization of recombinant human activin B." Schmelzer C.H., Burton L.E., Tamony C.M., Schwall R.H., Mason A.J., Liegeois N. Biochim. Biophys. Acta 1039:135-141(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 293-307.
[8]	"Differential binding and neutralization of activins A and B by follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG)." Schneyer A., Schoen A., Quigg A., Sidis Y. Endocrinology 144:1671-1674(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FST AND FSTL3.
+	Additional computationally mapped references.

Web resources

Wikipedia

Inhibin entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	M31669, M31668 Genomic DNA. Translation: AAA59451.1. AC012363 Genomic DNA. Translation: AAY14801.1. CH471103 Genomic DNA. Translation: EAW95243.1. BC030029 mRNA. Translation: AAH30029.1. M31682 mRNA. Translation: AAA59170.1. M13437 mRNA. Translation: AAA59169.1.
IPI	IPI00297026.
PIR	A40150.
RefSeq	NP_002184.2. NM_002193.2.
UniGene	Hs.1735.
3D structure databases
ProteinModelPortal	P09529.
ModBase	Search...
Protein-protein interaction databases
IntAct	P09529. 1 interaction.
STRING	9606.ENSP00000295228.
PTM databases
PhosphoSite	P09529.
Polymorphism databases
DMDM	1708437.
Proteomic databases
PaxDb	P09529.
PRIDE	P09529.
Protocols and materials databases
DNASU	3625.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000295228; ENSP00000295228; ENSG00000163083.
GeneID	3625.
KEGG	hsa:3625.
UCSC	uc002tmn.2. human.
Organism-specific databases
CTD	3625.
GeneCards	GC02P121198.
H-InvDB	HIX0002419.
HGNC	HGNC:6067. INHBB.
HPA	HPA035386.
MIM	147390. gene.
neXtProt	NX_P09529.
PharmGKB	PA29878.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG278663.
HOGENOM	HOG000220890.
HOVERGEN	HBG105613.
InParanoid	P09529.
KO	K04667.
OMA	FVVVQAR.
OrthoDB	EOG42JNRM.
PhylomeDB	P09529.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
Bgee	P09529.
CleanEx	HS_INHBB.
Genevestigator	P09529.
GermOnline	ENSG00000163083. Homo sapiens.
Family and domain databases
InterPro	IPR000381. Inhibin_betaB. IPR001839. TGF-b_C. IPR001111. TGF-b_N. IPR015615. TGF-beta-rel. IPR017948. TGFb_CS. [Graphical view]
PANTHER	PTHR11848. PTHR11848. 1 hit. PTHR11848:SF29. PTHR11848:SF29. 1 hit.
Pfam	PF00019. TGF_beta. 1 hit. PF00688. TGFb_propeptide. 1 hit. [Graphical view]
PRINTS	PR00671. INHIBINBB.
SMART	SM00204. TGFB. 1 hit. [Graphical view]
PROSITE	PS00250. TGF_BETA_1. 1 hit. PS51362. TGF_BETA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	3625.
NextBio	14185.
SOURCE	Search...

Entry information

Entry name

INHBB_HUMAN

Accession

Primary (citable) accession number: P09529
Secondary accession number(s): Q53T31, Q8N1D3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.