INHBE_HUMAN
ID INHBE_HUMAN Reviewed; 350 AA.
AC P58166;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Inhibin beta E chain;
DE AltName: Full=Activin beta-E chain;
DE Flags: Precursor;
GN Name=INHBE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=12242034; DOI=10.1016/s0303-7207(02)00157-0;
RA Hashimoto O., Tsuchida K., Ushiro Y., Hosoi Y., Hoshi N., Sugino H.,
RA Hasegawa Y.;
RT "cDNA cloning and expression of human activin betaE subunit.";
RL Mol. Cell. Endocrinol. 194:117-122(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-62 AND HIS-215.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Inhibins and activins inhibit and activate, respectively, the
CC secretion of follitropin by the pituitary gland. Inhibins/activins are
CC involved in regulating a number of diverse functions such as
CC hypothalamic and pituitary hormone secretion, gonadal hormone
CC secretion, germ cell development and maturation, erythroid
CC differentiation, insulin secretion, nerve cell survival, embryonic
CC axial development or bone growth, depending on their subunit
CC composition. Inhibins appear to oppose the functions of activins.
CC -!- SUBUNIT: Homodimeric or heterodimeric through association with alpha
CC and beta subunits, linked by one or more disulfide bonds. Inhibins are
CC heterodimers of one alpha and one beta subunit. Activins are homo- or
CC heterodimers of beta subunits only (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; AF412024; AAN03682.1; -; mRNA.
DR EMBL; AK075285; BAC11521.1; -; mRNA.
DR EMBL; BC005161; AAH05161.1; -; mRNA.
DR CCDS; CCDS8939.1; -.
DR RefSeq; NP_113667.1; NM_031479.4.
DR AlphaFoldDB; P58166; -.
DR SMR; P58166; -.
DR BioGRID; 123742; 48.
DR IntAct; P58166; 12.
DR STRING; 9606.ENSP00000266646; -.
DR GlyConnect; 2094; 3 N-Linked glycans (1 site).
DR GlyGen; P58166; 2 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P58166; -.
DR PhosphoSitePlus; P58166; -.
DR BioMuta; INHBE; -.
DR DMDM; 14285500; -.
DR MassIVE; P58166; -.
DR MaxQB; P58166; -.
DR PaxDb; P58166; -.
DR PeptideAtlas; P58166; -.
DR PRIDE; P58166; -.
DR ProteomicsDB; 57050; -.
DR Antibodypedia; 16213; 136 antibodies from 19 providers.
DR DNASU; 83729; -.
DR Ensembl; ENST00000266646.3; ENSP00000266646.2; ENSG00000139269.3.
DR GeneID; 83729; -.
DR KEGG; hsa:83729; -.
DR MANE-Select; ENST00000266646.3; ENSP00000266646.2; NM_031479.5; NP_113667.1.
DR UCSC; uc001snw.4; human.
DR CTD; 83729; -.
DR DisGeNET; 83729; -.
DR GeneCards; INHBE; -.
DR HGNC; HGNC:24029; INHBE.
DR HPA; ENSG00000139269; Tissue enriched (liver).
DR MIM; 612031; gene.
DR neXtProt; NX_P58166; -.
DR OpenTargets; ENSG00000139269; -.
DR PharmGKB; PA134898991; -.
DR VEuPathDB; HostDB:ENSG00000139269; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000162107; -.
DR HOGENOM; CLU_020515_5_0_1; -.
DR InParanoid; P58166; -.
DR OMA; ETPLCCR; -.
DR OrthoDB; 1385831at2759; -.
DR PhylomeDB; P58166; -.
DR TreeFam; TF318514; -.
DR PathwayCommons; P58166; -.
DR Reactome; R-HSA-209822; Glycoprotein hormones.
DR SignaLink; P58166; -.
DR BioGRID-ORCS; 83729; 51 hits in 1077 CRISPR screens.
DR ChiTaRS; INHBE; human.
DR GenomeRNAi; 83729; -.
DR Pharos; P58166; Tbio.
DR PRO; PR:P58166; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P58166; protein.
DR Bgee; ENSG00000139269; Expressed in right lobe of liver and 82 other tissues.
DR ExpressionAtlas; P58166; baseline and differential.
DR Genevisible; P58166; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001318; Inhibin_betaC.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR PRINTS; PR00672; INHIBINBC.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Growth factor; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..236
FT /evidence="ECO:0000255"
FT /id="PRO_0000033736"
FT CHAIN 237..350
FT /note="Inhibin beta E chain"
FT /id="PRO_0000033737"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 240..248
FT /evidence="ECO:0000250"
FT DISULFID 247..315
FT /evidence="ECO:0000250"
FT DISULFID 276..347
FT /evidence="ECO:0000250"
FT DISULFID 280..349
FT /evidence="ECO:0000250"
FT DISULFID 314
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VARIANT 62
FT /note="R -> T (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036198"
FT VARIANT 215
FT /note="Q -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036199"
SQ SEQUENCE 350 AA; 38561 MW; A49C1495677E3E6F CRC64;
MRLPDVQLWL VLLWALVRAQ GTGSVCPSCG GSKLAPQAER ALVLELAKQQ ILDGLHLTSR
PRITHPPPQA ALTRALRRLQ PGSVAPGNGE EVISFATVTD STSAYSSLLT FHLSTPRSHH
LYHARLWLHV LPTLPGTLCL RIFRWGPRRR RQGSRTLLAE HHITNLGWHT LTLPSSGLRG
EKSGVLKLQL DCRPLEGNST VTGQPRRLLD TAGHQQPFLE LKIRANEPGA GRARRRTPTC
EPATPLCCRR DHYVDFQELG WRDWILQPEG YQLNYCSGQC PPHLAGSPGI AASFHSAVFS
LLKANNPWPA STSCCVPTAR RPLSLLYLDH NGNVVKTDVP DMVVEACGCS
