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Immunoglobulin superfamily member 1 (IgSF1) (Immunoglobulin-like domain-containing protein 1) (Inhibin-binding protein) (InhBP) (Pituitary gland-specific factor 2) (p120)

 IGSF1_HUMAN             Reviewed;        1336 AA.
Q8N6C5; B5MEG2; H9KV64; O15070; Q9NTC8;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
14-APR-2009, sequence version 3.
25-MAY-2022, entry version 163.
RecName: Full=Immunoglobulin superfamily member 1;
Short=IgSF1;
AltName: Full=Immunoglobulin-like domain-containing protein 1;
AltName: Full=Inhibin-binding protein;
Short=InhBP;
AltName: Full=Pituitary gland-specific factor 2;
AltName: Full=p120;
Flags: Precursor;
Name=IGSF1; Synonyms=IGDC1, KIAA0364, PGSF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9729118; DOI=10.1016/s0378-1119(98)00253-4;
Frattini A., Faranda S., Redolfi E., Allavena P., Vezzoni P.;
"Identification and genomic organization of a gene coding for a new member
of the cell adhesion molecule family mapping to Xq25.";
Gene 214:1-6(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=9521868; DOI=10.1006/geno.1997.5156;
Mazzarella R., Pengue G., Jones J., Jones C., Schlessinger D.;
"Cloning and expression of an immunoglobulin superfamily gene (IGSF1) in
Xq25.";
Genomics 48:157-162(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
TISSUE=Pituitary;
PubMed=11854097; DOI=10.1677/jme.0.0280033;
Tanaka S., Tatsumi K., Okubo K., Itoh K., Kawamoto S., Matsubara K.,
Amino N.;
"Expression profile of active genes in the human pituitary gland.";
J. Mol. Endocrinol. 28:33-44(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII. The
complete sequences of 100 new cDNA clones from brain which can code for
large proteins in vitro.";
DNA Res. 4:141-150(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Liver;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1153-1336.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
FUNCTION, AND INTERACTION WITH ACVR1B; ACVR2A; ACVR2B; ACVRL1 AND BMPR1B.
PubMed=11266516; DOI=10.1210/mend.15.4.0616;
Chapman S.C., Woodruff T.K.;
"Modulation of activin signal transduction by inhibin B and inhibin-binding
protein (INhBP).";
Mol. Endocrinol. 15:668-679(2001).
[9]
INTERACTION WITH HECTD1.
PubMed=12421765; DOI=10.1101/gr.406902;
Nakayama M., Kikuno R., Ohara O.;
"Protein-protein interactions between large proteins: two-hybrid screening
using a functionally classified library composed of long cDNAs.";
Genome Res. 12:1773-1784(2002).
[10]
NEGATIVE INTERACTION WITH INHA.
PubMed=12385827; DOI=10.1016/s0303-7207(02)00227-7;
Chapman S.C., Bernard D.J., Jelen J., Woodruff T.K.;
"Properties of inhibin binding to betaglycan, InhBP/p120 and the activin
type II receptors.";
Mol. Cell. Endocrinol. 196:79-93(2002).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, VARIANTS CHTE 708-ALA--LYS-716
DEL; ASN-765; PHE-858 AND ARG-942, AND CHARACTERIZATION OF 708-ALA--LYS-716
DEL; ASN-765; PHE-858 AND ARG-942.
PubMed=23143598; DOI=10.1038/ng.2453;
Sun Y., Bak B., Schoenmakers N., van Trotsenburg A.S., Oostdijk W.,
Voshol P., Cambridge E., White J.K., le Tissier P., Gharavy S.N.,
Martinez-Barbera J.P., Stokvis-Brantsma W.H., Vulsma T., Kempers M.J.,
Persani L., Campi I., Bonomi M., Beck-Peccoz P., Zhu H., Davis T.M.,
Hokken-Koelega A.C., Del Blanco D.G., Rangasami J.J., Ruivenkamp C.A.,
Laros J.F., Kriek M., Kant S.G., Bosch C.A., Biermasz N.R.,
Appelman-Dijkstra N.M., Corssmit E.P., Hovens G.C., Pereira A.M.,
den Dunnen J.T., Wade M.G., Breuning M.H., Hennekam R.C., Chatterjee K.,
Dattani M.T., Wit J.M., Bernard D.J.;
"Loss-of-function mutations in IGSF1 cause an X-linked syndrome of central
hypothyroidism and testicular enlargement.";
Nat. Genet. 44:1375-1381(2012).
[13]
VARIANT GLY-774.
PubMed=23092983; DOI=10.1038/tp.2012.102;
Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B., Cohen D.,
Faudet A., Bouteiller D., Gilleron M., Jacquette A., Whalen S., Afenjar A.,
Perisse D., Laurent C., Dupuits C., Gautier C., Gerard M., Huguet G.,
Caillet S., Leheup B., Leboyer M., Gillberg C., Delorme R., Bourgeron T.,
Brice A., Depienne C.;
"Analysis of the chromosome X exome in patients with autism spectrum
disorders identified novel candidate genes, including TMLHE.";
Transl. Psychiatry 2:E179-E179(2012).
-!- FUNCTION: Seems to be a coreceptor in inhibin signaling, but seems not
to be a high-affinity inhibin receptor. Antagonizes activin A signaling
in the presence or absence of inhibin B (By similarity). Necessary to
mediate a specific antagonistic effect of inhibin B on activin-
stimulated transcription. {ECO:0000250, ECO:0000269|PubMed:11266516}.
-!- SUBUNIT: Interacts with INHA (By similarity). In PubMed:12385827 does
not interact with INHA; standard receptor binding assay. Interacts with
ACVR1B; the interaction appears to be ligand-dependent as it is
diminished by inhibin B and activin A. Interacts with ACVR2A, ACVR2B,
ACVRL1 and BMPR1B. Interacts with HECTD1. {ECO:0000250,
ECO:0000269|PubMed:11266516, ECO:0000269|PubMed:12421765}.
-!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=InhBP-L, long;
IsoId=Q8N6C5-1; Sequence=Displayed;
Name=2;
IsoId=Q8N6C5-2; Sequence=VSP_031195;
Name=3; Synonyms=InhBP-S, short;
IsoId=Q8N6C5-3; Sequence=VSP_031196, VSP_031197;
Name=4;
IsoId=Q8N6C5-4; Sequence=VSP_044554;
-!- TISSUE SPECIFICITY: Highly expressed in pancreas, testis and fetal
liver. Moderately expressed in heart, prostate and small intestine.
Expressed at very low levels in brain, thymus, ovary, colon, fetal lung
and fetal kidney. Expressed in muscle. Isoform 3 is expressed in
pituitary gland. {ECO:0000269|PubMed:11854097,
ECO:0000269|PubMed:23143598, ECO:0000269|PubMed:9521868}.
-!- DEVELOPMENTAL STAGE: Expressed in embryo Carnegie stage 18 in Rathke's
pouch progenitors. {ECO:0000269|PubMed:23143598}.
-!- DISEASE: Hypothyroidism, central, and testicular enlargement (CHTE)
[MIM:300888]: A disorder characterized by insufficient thyroid gland
stimulation by thyroid stimulating hormone (TSH), resulting from
hypothalamic and/or pituitary dysfunction. CHTE patients have delayed
testosterone increase at puberty with normal testosterone levels in
adulthood, normal testicular volume in childhood and enlarged testicles
in adulthood. {ECO:0000269|PubMed:23143598}. Note=The disease is caused
by variants affecting the gene represented in this entry.
-!- CAUTION: It is uncertain whether Met-1 or Met-12 is the initiator.
{ECO:0000305}.
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EMBL; Y10523; CAA71535.1; -; mRNA.
EMBL; AF034198; AAC52057.1; -; mRNA.
EMBL; AB058894; BAB40235.1; -; mRNA.
EMBL; AB002362; BAA20819.2; -; mRNA.
EMBL; AK226008; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL135784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL590806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL137369; CAB70713.1; -; mRNA.
CCDS; CCDS14629.1; -. [Q8N6C5-1]
CCDS; CCDS14630.1; -. [Q8N6C5-3]
CCDS; CCDS55490.1; -. [Q8N6C5-2]
CCDS; CCDS55491.1; -. [Q8N6C5-4]
RefSeq; NP_001164432.1; NM_001170961.1. [Q8N6C5-4]
RefSeq; NP_001164433.1; NM_001170962.1. [Q8N6C5-2]
RefSeq; NP_001164434.1; NM_001170963.1. [Q8N6C5-3]
RefSeq; NP_001546.2; NM_001555.4. [Q8N6C5-1]
RefSeq; NP_991402.1; NM_205833.3. [Q8N6C5-3]
RefSeq; XP_011529632.1; XM_011531330.1. [Q8N6C5-4]
AlphaFoldDB; Q8N6C5; -.
SMR; Q8N6C5; -.
BioGRID; 109763; 15.
IntAct; Q8N6C5; 7.
MINT; Q8N6C5; -.
STRING; 9606.ENSP00000359940; -.
GlyGen; Q8N6C5; 14 sites.
iPTMnet; Q8N6C5; -.
PhosphoSitePlus; Q8N6C5; -.
BioMuta; IGSF1; -.
DMDM; 226694182; -.
EPD; Q8N6C5; -.
jPOST; Q8N6C5; -.
MassIVE; Q8N6C5; -.
MaxQB; Q8N6C5; -.
PaxDb; Q8N6C5; -.
PeptideAtlas; Q8N6C5; -.
PRIDE; Q8N6C5; -.
ProteomicsDB; 46220; -.
ProteomicsDB; 72153; -. [Q8N6C5-1]
ProteomicsDB; 72154; -. [Q8N6C5-2]
Antibodypedia; 16308; 188 antibodies from 19 providers.
DNASU; 3547; -.
Ensembl; ENST00000361420.8; ENSP00000355010.3; ENSG00000147255.19.
Ensembl; ENST00000370900.5; ENSP00000359937.1; ENSG00000147255.19. [Q8N6C5-3]
Ensembl; ENST00000370901.4; ENSP00000359938.4; ENSG00000147255.19. [Q8N6C5-3]
Ensembl; ENST00000370903.8; ENSP00000359940.3; ENSG00000147255.19. [Q8N6C5-4]
Ensembl; ENST00000370904.6; ENSP00000359941.1; ENSG00000147255.19. [Q8N6C5-2]
Ensembl; ENST00000370910.5; ENSP00000359947.1; ENSG00000147255.19. [Q8N6C5-2]
Ensembl; ENST00000651556.1; ENSP00000498789.1; ENSG00000147255.19.
GeneID; 3547; -.
KEGG; hsa:3547; -.
MANE-Select; ENST00000361420.8; ENSP00000355010.3; NM_001555.5; NP_001546.2.
UCSC; uc004ewd.5; human. [Q8N6C5-1]
CTD; 3547; -.
DisGeNET; 3547; -.
GeneCards; IGSF1; -.
HGNC; HGNC:5948; IGSF1.
HPA; ENSG00000147255; Group enriched (brain, pituitary gland).
MalaCards; IGSF1; -.
MIM; 300137; gene.
MIM; 300888; phenotype.
neXtProt; NX_Q8N6C5; -.
OpenTargets; ENSG00000147255; -.
Orphanet; 329235; X-linked central congenital hypothyroidism with late-onset testicular enlargement.
PharmGKB; PA29761; -.
VEuPathDB; HostDB:ENSG00000147255; -.
eggNOG; ENOG502RYEX; Eukaryota.
GeneTree; ENSGT00980000198504; -.
HOGENOM; CLU_006143_0_0_1; -.
InParanoid; Q8N6C5; -.
OMA; GCGHGCW; -.
OrthoDB; 1327293at2759; -.
PhylomeDB; Q8N6C5; -.
TreeFam; TF336644; -.
PathwayCommons; Q8N6C5; -.
SignaLink; Q8N6C5; -.
BioGRID-ORCS; 3547; 9 hits in 705 CRISPR screens.
ChiTaRS; IGSF1; human.
GeneWiki; IGSF1; -.
GenomeRNAi; 3547; -.
Pharos; Q8N6C5; Tbio.
PRO; PR:Q8N6C5; -.
Proteomes; UP000005640; Chromosome X.
RNAct; Q8N6C5; protein.
Bgee; ENSG00000147255; Expressed in pituitary gland and 160 other tissues.
ExpressionAtlas; Q8N6C5; baseline and differential.
Genevisible; Q8N6C5; HS.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0038102; F:activin receptor antagonist activity; IDA:UniProtKB.
GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
GO; GO:0034711; F:inhibin binding; IDA:UniProtKB.
GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 12.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
Pfam; PF00047; ig; 1.
Pfam; PF13895; Ig_2; 6.
SMART; SM00409; IG; 11.
SMART; SM00408; IGc2; 9.
SUPFAM; SSF48726; SSF48726; 12.
PROSITE; PS50835; IG_LIKE; 6.
1: Evidence at protein level;
Alternative splicing; Congenital hypothyroidism; Disease variant;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1..28
/evidence="ECO:0000255"
CHAIN 29..1336
/note="Immunoglobulin superfamily member 1"
/id="PRO_0000318512"
TOPO_DOM 29..518
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 519..539
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 540..559
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 560..580
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 581..1336
/note="Extracellular"
/evidence="ECO:0000255"
DOMAIN 38..122
/note="Ig-like C2-type 1"
DOMAIN 137..222
/note="Ig-like C2-type 2"
DOMAIN 226..312
/note="Ig-like C2-type 3"
DOMAIN 321..408
/note="Ig-like C2-type 4"
DOMAIN 419..500
/note="Ig-like C2-type 5"
DOMAIN 589..677
/note="Ig-like C2-type 6"
DOMAIN 686..760
/note="Ig-like C2-type 7"
DOMAIN 777..869
/note="Ig-like C2-type 8"
DOMAIN 873..958
/note="Ig-like C2-type 9"
DOMAIN 965..1060
/note="Ig-like C2-type 10"
DOMAIN 1065..1150
/note="Ig-like C2-type 11"
DOMAIN 1161..1242
/note="Ig-like C2-type 12"
REGION 1308..1336
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1313..1330
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
CARBOHYD 53
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 338
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 374
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 381
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 607
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 747
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 798
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 846
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 939
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 986
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1027
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1082
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1147
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1223
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 58..106
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 248..296
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 343..392
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 441..484
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 703..750
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 799..849
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 895..942
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 1087..1134
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 1183..1226
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
VAR_SEQ 24..33
/note="RMSLGMTSIV -> L (in isoform 2)"
/evidence="ECO:0000303|PubMed:9205841,
ECO:0000303|PubMed:9521868"
/id="VSP_031195"
VAR_SEQ 224..242
/note="LYPKPTLTAHPGPIMAPGE -> GCGYGCWHLAIVVPGIMAG (in
isoform 3)"
/evidence="ECO:0000303|PubMed:11854097"
/id="VSP_031196"
VAR_SEQ 243..1336
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:11854097"
/id="VSP_031197"
VAR_SEQ 572
/note="C -> CAISFA (in isoform 4)"
/evidence="ECO:0000303|Ref.5"
/id="VSP_044554"
VARIANT 381
/note="N -> H (in dbSNP:rs6637826)"
/id="VAR_054960"
VARIANT 708..716
/note="Missing (in CHTE; impairs IGSF1 trafficking to the
plasma membrane)"
/evidence="ECO:0000269|PubMed:23143598"
/id="VAR_069268"
VARIANT 765
/note="S -> N (in CHTE; impairs IGSF1 trafficking to the
plasma membrane)"
/evidence="ECO:0000269|PubMed:23143598"
/id="VAR_069269"
VARIANT 774
/note="E -> G"
/evidence="ECO:0000269|PubMed:23092983"
/id="VAR_076256"
VARIANT 858
/note="S -> F (in CHTE; impairs IGSF1 trafficking to the
plasma membrane; dbSNP:rs397514622)"
/evidence="ECO:0000269|PubMed:23143598"
/id="VAR_069270"
VARIANT 942
/note="C -> R (in CHTE; impairs IGSF1 trafficking to the
plasma membrane)"
/evidence="ECO:0000269|PubMed:23143598"
/id="VAR_069271"
CONFLICT 397
/note="T -> A (in Ref. 5; AK226008)"
/evidence="ECO:0000305"
CONFLICT 462
/note="K -> R (in Ref. 1; CAA71535)"
/evidence="ECO:0000305"
CONFLICT 494
/note="I -> M (in Ref. 1; CAA71535)"
/evidence="ECO:0000305"
CONFLICT 757
/note="R -> L (in Ref. 1; CAA71535)"
/evidence="ECO:0000305"
SEQUENCE 1336 AA; 148936 MW; 7D0D2C36FD1CE8B8 CRC64;
MTLDRPGEGA TMLKTFTVLL FCIRMSLGMT SIVMDPQPEL WIESNYPQAP WENITLWCRS
PSRISSKFLL LKDKTQMTWI RPSHKTFQVS FLIGALTESN AGLYRCCYWK ETGWSKPSKV
LELEAPGQLP KPIFWIQAET PALPGCNVNI LCHGWLQDLV FMLFKEGYAE PVDYQVPTGT
MAIFSIDNLT PEDEGVYICR THIQMLPTLW SEPSNPLKLV VAGLYPKPTL TAHPGPIMAP
GESLNLRCQG PIYGMTFALM RVEDLEKSFY HKKTIKNEAN FFFQSLKIQD TGHYLCFYYD
ASYRGSLLSD VLKIWVTDTF PKTWLLARPS AVVQMGQNVS LRCRGPVDGV GLALYKKGED
KPLQFLDATS IDDNTSFFLN NVTYSDTGIY SCHYLLTWKT SIRMPSHNTV ELMVVDKPPK
PSLSAWPSTV FKLGKAITLQ CRVSHPVLEF SLEWEERETF QKFSVNGDFI ISNVDGKGTG
TYSCSYRVET HPNIWSHRSE PLKLMGPAGY LTWNYVLNEA IRLSLIMQLV ALLLVVLWIR
WKCRRLRIRE AWLLGTAQGV TMLFIVTALL CCGLCNGVLI EETEIVMPTP KPELWAETNF
PLAPWKNLTL WCRSPSGSTK EFVLLKDGTG WIATRPASEQ VRAAFPLGAL TQSHTGSYHC
HSWEEMAVSE PSEALELVGT DILPKPVISA SPTIRGQELQ LRCKGWLAGM GFALYKEGEQ
EPVQQLGAVG REAFFTIQRM EDKDEGNYSC RTHTEKRPFK WSEPSEPLEL VIKEMYPKPF
FKTWASPVVT PGARVTFNCS TPHQHMSFIL YKDGSEIASS DRSWASPGAS AAHFLIISVG
IGDGGNYSCR YYDFSIWSEP SDPVELVVTE FYPKPTLLAQ PGPVVFPGKS VILRCQGTFQ
GMRFALLQEG AHVPLQFRSV SGNSADFLLH TVGAEDSGNY SCIYYETTMS NRGSYLSMPL
MIWVTDTFPK PWLFAEPSSV VPMGQNVTLW CRGPVHGVGY ILHKEGEATS MQLWGSTSND
GAFPITNISG TSMGRYSCCY HPDWTSSIKI QPSNTLELLV TGLLPKPSLL AQPGPMVAPG
ENMTLQCQGE LPDSTFVLLK EGAQEPLEQQ RPSGYRADFW MPAVRGEDSG IYSCVYYLDS
TPFAASNHSD SLEIWVTDKP PKPSLSAWPS TMFKLGKDIT LQCRGPLPGV EFVLEHDGEE
APQQFSEDGD FVINNVEGKG IGNYSCSYRL QAYPDIWSEP SDPLELVGAA GPVAQECTVG
NIVRSSLIVV VVVALGVVLA IEWKKWPRLR TRGSETDGRD QTIALEECNQ EGEPGTPANS
PSSTSQRISV ELPVPI


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