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Indian hedgehog protein (IHH) (HHG-2) [Cleaved into: Indian hedgehog protein N-product; Indian hedgehog protein C-product]

 IHH_HUMAN               Reviewed;         411 AA.
Q14623; B9EGM5; O43322; Q8N4B9;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
19-JUL-2003, sequence version 4.
18-JUL-2018, entry version 195.
RecName: Full=Indian hedgehog protein;
Short=IHH;
AltName: Full=HHG-2;
Contains:
RecName: Full=Indian hedgehog protein N-product;
Contains:
RecName: Full=Indian hedgehog protein C-product;
Flags: Precursor;
Name=IHH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tate G., Kishimoto K., Mitsuya T.;
"Expression of Sonic hedgehog and its receptor Patched/Smoothened in
human cancer cell lines and embryonic organs.";
J. Biochem. Mol. Biol. Biophys. 4:27-34(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 100-411.
TISSUE=Fetal lung;
PubMed=7590746; DOI=10.1006/geno.1995.1104;
Marigo V., Roberts D.J., Lee S.M.K., Tsukurov O., Levi T.,
Gastier J.M., Epstein D.J., Gilbert D.J., Copeland N.G., Seidman C.E.,
Jenkins N.A., Seidman J.G., McMahon A.P., Tabin C.;
"Cloning, expression, and chromosomal location of SHH and IHH: two
human homologues of the Drosophila segment polarity gene hedgehog.";
Genomics 28:44-51(1995).
[5]
NUCLEOTIDE SEQUENCE OF 124-172.
PubMed=7720571;
Chang D.T., Lopez A., von Kessler D.P., Chiang C., Simandl B.K.,
Zhao R., Seldin M.F., Fallon J.F., Beachy P.A.;
"Products, genetic linkage and limb patterning activity of a murine
hedgehog gene.";
Development 120:3339-3353(1994).
[6]
PALMITOYLATION AT CYS-28.
PubMed=9593755; DOI=10.1074/jbc.273.22.14037;
Pepinsky R.B., Zeng C., Wen D., Rayhorn P., Baker D.P., Williams K.P.,
Bixler S.A., Ambrose C.M., Garber E.A., Miatkowski K., Taylor F.R.,
Wang E.A., Galdes A.;
"Identification of a palmitic acid-modified form of human Sonic
hedgehog.";
J. Biol. Chem. 273:14037-14045(1998).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-282.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[8]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 29-193 IN COMPLEXES WITH
CALCIUM IONS; ZINC IONS; BOC AND CDON, DOMAIN, AND INTERACTION WITH
BOC AND CDON.
PubMed=20519495; DOI=10.1074/jbc.M110.131680;
Kavran J.M., Ward M.D., Oladosu O.O., Mulepati S., Leahy D.J.;
"All mammalian Hedgehog proteins interact with cell adhesion molecule,
down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a
conserved manner.";
J. Biol. Chem. 285:24584-24590(2010).
[9]
X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 28-202 OF WILD TYPE AND
VARIANTS BDA1 LYS-95; GLU-100 AND LYS-131 IN COMPLEX WITH ZINC IONS,
FUNCTION, SUBUNIT, INTERACTION WITH PTCH1, SUBCELLULAR LOCATION,
CHOLESTERYLATION, PALMITOYLATION, MUTAGENESIS OF GLU-95, DOMAIN, AND
CHARACTERIZATION OF VARIANTS BDA1 LYS-95; ASN-100; GLU-100 AND
LYS-131.
PubMed=21537345; DOI=10.1038/cr.2011.76;
Ma G., Yu J., Xiao Y., Chan D., Gao B., Hu J., He Y., Guo S., Zhou J.,
Zhang L., Gao L., Zhang W., Kang Y., Cheah K.S., Feng G., Guo X.,
Wang Y., Zhou C.Z., He L.;
"Indian hedgehog mutations causing brachydactyly type A1 impair
Hedgehog signal transduction at multiple levels.";
Cell Res. 21:1343-1357(2011).
[10]
VARIANTS BDA1 LYS-95; GLU-100 AND LYS-131.
PubMed=11455389; DOI=10.1038/ng577;
Gao B., Guo J., She C., Shu A., Yang M., Tan Z., Yang X., Guo S.,
Feng G., He L.;
"Mutations in IHH, encoding Indian hedgehog, cause brachydactyly type
A-1.";
Nat. Genet. 28:386-388(2001).
[11]
VARIANT BDA1 ASN-100.
PubMed=12384778; DOI=10.1007/s00439-002-0815-2;
McCready M.E., Sweeney E., Fryer A.E., Donnai D., Baig A., Racacho L.,
Warman M.L., Hunter A.G.W., Bulman D.E.;
"A novel mutation in the IHH gene causes brachydactyly type A1: a 95-
year-old mystery resolved.";
Hum. Genet. 111:368-375(2002).
[12]
VARIANTS ACFD LEU-46 AND ALA-190.
PubMed=12632327; DOI=10.1086/374318;
Hellemans J., Coucke P.J., Giedion A., De Paepe A., Kramer P.,
Beemer F., Mortier G.R.;
"Homozygous mutations in IHH cause acrocapitofemoral dysplasia, an
autosomal recessive disorder with cone-shaped epiphyses in hands and
hips.";
Am. J. Hum. Genet. 72:1040-1046(2003).
-!- FUNCTION: Intercellular signal essential for a variety of
patterning events during development. Binds to the patched (PTC)
receptor, which functions in association with smoothened (SMO), to
activate the transcription of target genes. Implicated in
endochondral ossification: may regulate the balance between growth
and ossification of the developing bones. Induces the expression
of parathyroid hormone-related protein (PTHRP) (By similarity).
{ECO:0000250, ECO:0000269|PubMed:21537345}.
-!- SUBUNIT: Homooligomer (indian hedgehog protein N-product).
Interacts with BOC and CDON. Interacts with PTCH1.
{ECO:0000269|PubMed:20519495, ECO:0000269|PubMed:21537345}.
-!- SUBCELLULAR LOCATION: Indian hedgehog protein N-product: Cell
membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Extracellular
side {ECO:0000250}. Note=The N-terminal peptide remains associated
with the cell surface. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Indian hedgehog protein C-product: Secreted,
extracellular space {ECO:0000250}. Note=The C-terminal peptide
diffuses from the cell. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21537345}.
-!- TISSUE SPECIFICITY: Expressed in embryonic lung, and in adult
kidney and liver.
-!- DOMAIN: The indian hedgehog protein N-product binds calcium and
zinc ions; this stabilizes the protein fold and is essential for
protein-protein interactions mediated by this domain.
{ECO:0000269|PubMed:20519495, ECO:0000269|PubMed:21537345}.
-!- PTM: The C-terminal domain displays an autoproteolysis activity
and a cholesterol transferase activity. Both activities result in
the cleavage of the full-length protein and covalent attachment of
a cholesterol moiety to the C-terminal of the newly generated N-
terminal fragment (N-product). The N-product is the active species
in both local and long-range signaling, whereas the C-product has
no signaling activity (By similarity). {ECO:0000250}.
-!- PTM: Cholesterylation is required for N-product targeting to lipid
rafts and multimerization. {ECO:0000269|PubMed:21537345}.
-!- PTM: Palmitoylated. N-palmitoylation is required for N-product
multimerization and full activity. {ECO:0000269|PubMed:21537345,
ECO:0000269|PubMed:9593755}.
-!- DISEASE: Brachydactyly A1 (BDA1) [MIM:112500]: A form of
brachydactyly. Brachydactyly defines a group of inherited
malformations characterized by shortening of the digits due to
abnormal development of the phalanges and/or the metacarpals.
Brachydactyly type A1 is characterized by middle phalanges of all
the digits rudimentary or fused with the terminal phalanges. The
proximal phalanges of the thumbs and big toes are short. BDA1
inheritance is autosomal dominant. {ECO:0000269|PubMed:11455389,
ECO:0000269|PubMed:12384778, ECO:0000269|PubMed:21537345}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Acrocapitofemoral dysplasia (ACFD) [MIM:607778]: An
autosomal recessive disorder characterized by short stature of
variable severity with postnatal onset. The most constant
radiographic abnormalities are observed in the tubular bones of
the hands and in the proximal part of the femur. Cone-shaped
epiphyses or a similar epiphyseal configuration with premature
epimetaphyseal fusion result in shortening of the skeletal
components involved. Cone-shaped epiphyses are also present to a
variable extent at the shoulders, knees and ankles.
{ECO:0000269|PubMed:12632327}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000305}.
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EMBL; AB018076; BAA33523.2; -; Genomic_DNA.
EMBL; CH471063; EAW70675.1; -; Genomic_DNA.
EMBL; BC034757; AAH34757.2; -; mRNA.
EMBL; BC136587; AAI36588.1; -; mRNA.
EMBL; BC136588; AAI36589.1; -; mRNA.
EMBL; L38517; AAA62178.1; -; mRNA.
CCDS; CCDS33380.1; -.
RefSeq; NP_002172.2; NM_002181.3.
UniGene; Hs.654504; -.
PDB; 3K7G; X-ray; 1.50 A; B=28-202.
PDB; 3K7H; X-ray; 1.50 A; B=28-202.
PDB; 3K7I; X-ray; 1.44 A; B=28-202.
PDB; 3K7J; X-ray; 1.90 A; B=28-202.
PDB; 3N1F; X-ray; 1.60 A; A/B=29-193.
PDB; 3N1M; X-ray; 1.69 A; B=29-193.
PDB; 3N1O; X-ray; 2.55 A; A/B/C=29-193.
PDB; 3N1P; X-ray; 2.70 A; B=29-193.
PDBsum; 3K7G; -.
PDBsum; 3K7H; -.
PDBsum; 3K7I; -.
PDBsum; 3K7J; -.
PDBsum; 3N1F; -.
PDBsum; 3N1M; -.
PDBsum; 3N1O; -.
PDBsum; 3N1P; -.
ProteinModelPortal; Q14623; -.
SMR; Q14623; -.
BioGrid; 109765; 1.
IntAct; Q14623; 2.
STRING; 9606.ENSP00000295731; -.
MEROPS; C46.003; -.
iPTMnet; Q14623; -.
PhosphoSitePlus; Q14623; -.
BioMuta; IHH; -.
DMDM; 33112634; -.
MaxQB; Q14623; -.
PaxDb; Q14623; -.
PeptideAtlas; Q14623; -.
PRIDE; Q14623; -.
ProteomicsDB; 60073; -.
Ensembl; ENST00000295731; ENSP00000295731; ENSG00000163501.
GeneID; 3549; -.
KEGG; hsa:3549; -.
UCSC; uc002vjo.3; human.
CTD; 3549; -.
DisGeNET; 3549; -.
EuPathDB; HostDB:ENSG00000163501.6; -.
GeneCards; IHH; -.
H-InvDB; HIX0023995; -.
HGNC; HGNC:5956; IHH.
MalaCards; IHH; -.
MIM; 112500; phenotype.
MIM; 600726; gene.
MIM; 607778; phenotype.
neXtProt; NX_Q14623; -.
OpenTargets; ENSG00000163501; -.
Orphanet; 63446; Acrocapitofemoral dysplasia.
Orphanet; 93388; Brachydactyly type A1.
PharmGKB; PA29769; -.
eggNOG; KOG3638; Eukaryota.
eggNOG; ENOG410XQA3; LUCA.
GeneTree; ENSGT00390000001117; -.
HOGENOM; HOG000233428; -.
HOVERGEN; HBG005480; -.
InParanoid; Q14623; -.
KO; K11989; -.
OMA; RPEGKIT; -.
OrthoDB; EOG091G0N90; -.
PhylomeDB; Q14623; -.
TreeFam; TF106458; -.
Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362798; Release of Hh-Np from the secreting cell.
Reactome; R-HSA-5632681; Ligand-receptor interactions.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5635838; Activation of SMO.
Reactome; R-HSA-5658034; HHAT G278V abrogates palmitoylation of Hh-Np.
Reactome; R-HSA-8941284; RUNX2 regulates chondrocyte maturation.
SignaLink; Q14623; -.
SIGNOR; Q14623; -.
EvolutionaryTrace; Q14623; -.
GeneWiki; IHH_(protein); -.
GenomeRNAi; 3549; -.
PRO; PR:Q14623; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163501; -.
CleanEx; HS_IHH; -.
Genevisible; Q14623; HS.
GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0005113; F:patched binding; IPI:UniProtKB.
GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0060220; P:camera-type eye photoreceptor cell fate commitment; IEA:Ensembl.
GO; GO:0051216; P:cartilage development; IMP:AgBase.
GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
GO; GO:0048469; P:cell maturation; IEA:Ensembl.
GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
GO; GO:0003413; P:chondrocyte differentiation involved in endochondral bone morphogenesis; IEA:Ensembl.
GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IEA:Ensembl.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:AgBase.
GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl.
GO; GO:0072498; P:embryonic skeletal joint development; IEA:Ensembl.
GO; GO:0003382; P:epithelial cell morphogenesis; IEA:Ensembl.
GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
GO; GO:0060323; P:head morphogenesis; IEA:Ensembl.
GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0046639; P:negative regulation of alpha-beta T cell differentiation; ISS:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0048074; P:negative regulation of eye pigmentation; IEA:Ensembl.
GO; GO:0033088; P:negative regulation of immature T cell proliferation in thymus; ISS:BHF-UCL.
GO; GO:0033085; P:negative regulation of T cell differentiation in thymus; ISS:BHF-UCL.
GO; GO:0048666; P:neuron development; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0031016; P:pancreas development; IEA:Ensembl.
GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; ISS:BHF-UCL.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:BHF-UCL.
GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
GO; GO:0040008; P:regulation of growth; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
GO; GO:0007224; P:smoothened signaling pathway; IDA:UniProtKB.
GO; GO:0061053; P:somite development; ISS:BHF-UCL.
GO; GO:0030704; P:vitelline membrane formation; IEA:Ensembl.
Gene3D; 3.30.1380.10; -; 1.
InterPro; IPR001657; Hedgehog.
InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
InterPro; IPR000320; Hedgehog_signalling_dom.
InterPro; IPR001767; Hint_dom.
InterPro; IPR003586; Hint_dom_C.
InterPro; IPR003587; Hint_dom_N.
InterPro; IPR036844; Hint_dom_sf.
InterPro; IPR006141; Intein_N.
Pfam; PF01085; HH_signal; 1.
Pfam; PF01079; Hint; 1.
PIRSF; PIRSF009400; Peptidase_C46; 1.
PRINTS; PR00632; SONICHHOG.
SMART; SM00305; HintC; 1.
SMART; SM00306; HintN; 1.
SUPFAM; SSF51294; SSF51294; 1.
SUPFAM; SSF55166; SSF55166; 1.
PROSITE; PS50817; INTEIN_N_TER; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Calcium; Cell membrane;
Complete proteome; Developmental protein; Disease mutation;
Glycoprotein; Hydrolase; Lipoprotein; Membrane; Metal-binding;
Palmitate; Protease; Reference proteome; Secreted; Signal; Zinc.
SIGNAL 1 27 {ECO:0000305}.
CHAIN 28 411 Indian hedgehog protein.
/FTId=PRO_0000013229.
CHAIN 28 202 Indian hedgehog protein N-product.
/FTId=PRO_0000013230.
CHAIN 203 411 Indian hedgehog protein C-product.
/FTId=PRO_0000013231.
METAL 94 94 Calcium 1. {ECO:0000269|PubMed:20519495}.
METAL 95 95 Calcium 1. {ECO:0000269|PubMed:20519495}.
METAL 95 95 Calcium 2. {ECO:0000269|PubMed:20519495}.
METAL 100 100 Calcium 1. {ECO:0000269|PubMed:20519495}.
METAL 130 130 Calcium 1; via carbonyl oxygen.
{ECO:0000269|PubMed:20519495}.
METAL 131 131 Calcium 1. {ECO:0000269|PubMed:20519495}.
METAL 131 131 Calcium 2. {ECO:0000269|PubMed:20519495}.
METAL 134 134 Calcium 2. {ECO:0000269|PubMed:20519495}.
METAL 136 136 Calcium 2. {ECO:0000269|PubMed:20519495}.
METAL 145 145 Zinc. {ECO:0000269|PubMed:20519495,
ECO:0000269|PubMed:21537345}.
METAL 152 152 Zinc. {ECO:0000269|PubMed:20519495,
ECO:0000269|PubMed:21537345}.
METAL 187 187 Zinc. {ECO:0000269|PubMed:20519495,
ECO:0000269|PubMed:21537345}.
SITE 202 203 Cleavage; by autolysis. {ECO:0000250}.
SITE 248 248 Involved in cholesterol transfer.
{ECO:0000250}.
SITE 272 272 Involved in auto-cleavage. {ECO:0000250}.
SITE 275 275 Essential for auto-cleavage.
{ECO:0000250}.
LIPID 28 28 N-palmitoyl cysteine.
{ECO:0000305|PubMed:9593755}.
LIPID 202 202 Cholesterol glycine ester. {ECO:0000250}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
VARIANT 46 46 P -> L (in ACFD; dbSNP:rs121917856).
{ECO:0000269|PubMed:12632327}.
/FTId=VAR_015981.
VARIANT 95 95 E -> K (in BDA1; decreases the stability
of the indian hedgehog protein N-product;
dbSNP:rs121917852).
{ECO:0000269|PubMed:11455389,
ECO:0000269|PubMed:21537345}.
/FTId=VAR_015982.
VARIANT 100 100 D -> E (in BDA1; decreases the stability
of the indian hedgehog protein N-product;
dbSNP:rs121917854).
{ECO:0000269|PubMed:11455389,
ECO:0000269|PubMed:21537345}.
/FTId=VAR_015983.
VARIANT 100 100 D -> N (in BDA1; decreases the stability
of the indian hedgehog protein N-product;
dbSNP:rs121917855).
{ECO:0000269|PubMed:12384778,
ECO:0000269|PubMed:21537345}.
/FTId=VAR_015984.
VARIANT 131 131 E -> K (in BDA1; no effect on the
stability of the indian hedgehog protein
N-product; dbSNP:rs121917853).
{ECO:0000269|PubMed:11455389,
ECO:0000269|PubMed:21537345}.
/FTId=VAR_015985.
VARIANT 190 190 V -> A (in ACFD; dbSNP:rs121917857).
{ECO:0000269|PubMed:12632327}.
/FTId=VAR_015986.
MUTAGEN 95 95 E->G: Increases the lysosomal degradation
of the indian hedgehog protein N-product.
{ECO:0000269|PubMed:21537345}.
CONFLICT 100 100 D -> R (in Ref. 4; AAA62178).
{ECO:0000305}.
CONFLICT 246 246 F -> L (in Ref. 1; BAA33523).
{ECO:0000305}.
CONFLICT 309 309 V -> A (in Ref. 1; BAA33523).
{ECO:0000305}.
STRAND 52 56 {ECO:0000244|PDB:3K7I}.
TURN 61 64 {ECO:0000244|PDB:3K7I}.
STRAND 73 75 {ECO:0000244|PDB:3N1P}.
HELIX 76 80 {ECO:0000244|PDB:3K7I}.
STRAND 89 91 {ECO:0000244|PDB:3K7I}.
STRAND 96 98 {ECO:0000244|PDB:3K7I}.
HELIX 99 101 {ECO:0000244|PDB:3K7I}.
HELIX 105 121 {ECO:0000244|PDB:3K7I}.
STRAND 127 131 {ECO:0000244|PDB:3K7I}.
HELIX 144 147 {ECO:0000244|PDB:3K7I}.
STRAND 150 155 {ECO:0000244|PDB:3K7I}.
HELIX 160 162 {ECO:0000244|PDB:3K7I}.
HELIX 163 172 {ECO:0000244|PDB:3K7I}.
STRAND 176 182 {ECO:0000244|PDB:3K7I}.
STRAND 185 189 {ECO:0000244|PDB:3K7I}.
STRAND 193 195 {ECO:0000244|PDB:3K7I}.
SEQUENCE 411 AA; 45251 MW; 4DA90C83F5ABF758 CRC64;
MSPARLRPRL HFCLVLLLLL VVPAAWGCGP GRVVGSRRRP PRKLVPLAYK QFSPNVPEKT
LGASGRYEGK IARSSERFKE LTPNYNPDII FKDEENTGAD RLMTQRCKDR LNSLAISVMN
QWPGVKLRVT EGWDEDGHHS EESLHYEGRA VDITTSDRDR NKYGLLARLA VEAGFDWVYY
ESKAHVHCSV KSEHSAAAKT GGCFPAGAQV RLESGARVAL SAVRPGDRVL AMGEDGSPTF
SDVLIFLDRE PHRLRAFQVI ETQDPPRRLA LTPAHLLFTA DNHTEPAARF RATFASHVQP
GQYVLVAGVP GLQPARVAAV STHVALGAYA PLTKHGTLVV EDVVASCFAA VADHHLAQLA
FWPLRLFHSL AWGSWTPGEG VHWYPQLLYR LGRLLLEEGS FHPLGMSGAG S


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