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O43462

- MBTP2_HUMAN

UniProt

O43462 - MBTP2_HUMAN

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Protein

Membrane-bound transcription factor site-2 protease

Gene

MBTPS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Intramembrane proteolysis of sterol-regulatory element-binding proteins (SREBPs) within the first transmembrane segment thereby releasing the N-terminal segment with a portion of the transmembrane segment attached. Site-2 cleavage comes after site-1 cleavage which takes place in the lumenal loop.

Catalytic activityi

Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-DRSRILL-|-CVLTFLCLSFNPLTSLLQWGGA-505. The residues Asn-Pro, 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi171 – 1711Zinc; catalytic
Active sitei172 – 1721
Metal bindingi175 – 1751Zinc; catalytic

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: ProtInc

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. cholesterol metabolic process Source: ProtInc
  4. endoplasmic reticulum unfolded protein response Source: Reactome
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.85. 2681.
ReactomeiREACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_18348. ATF6-alpha activates chaperones.

Protein family/group databases

MEROPSiM50.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-bound transcription factor site-2 protease (EC:3.4.24.85)
Alternative name(s):
Endopeptidase S2P
Sterol regulatory element-binding proteins intramembrane protease
Short name:
SREBPs intramembrane protease
Gene namesi
Name:MBTPS2
Synonyms:S2P
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:15455. MBTPS2.

Subcellular locationi

Membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cytoplasm 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33Cytoplasmic1 Publication
Transmembranei4 – 2421HelicalSequence AnalysisAdd
BLAST
Topological domaini25 – 7450Lumenal1 PublicationAdd
BLAST
Transmembranei75 – 9521HelicalSequence AnalysisAdd
BLAST
Transmembranei96 – 10712HelicalSequence AnalysisAdd
BLAST
Topological domaini108 – 14437Lumenal1 PublicationAdd
BLAST
Transmembranei145 – 16925HelicalSequence AnalysisAdd
BLAST
Transmembranei174 – 18613HelicalSequence AnalysisAdd
BLAST
Transmembranei187 – 20923HelicalSequence AnalysisAdd
BLAST
Transmembranei229 – 25123HelicalSequence AnalysisAdd
BLAST
Topological domaini252 – 446195Lumenal1 PublicationAdd
BLAST
Transmembranei447 – 46418HelicalSequence AnalysisAdd
BLAST
Transmembranei465 – 47612HelicalSequence AnalysisAdd
BLAST
Topological domaini477 – 49216LumenalSequence AnalysisAdd
BLAST
Transmembranei493 – 51321HelicalSequence AnalysisAdd
BLAST
Topological domaini514 – 5196CytoplasmicSequence Analysis

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. Golgi membrane Source: Reactome
  3. integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

IFAP syndrome with or without BRESHECK syndrome (IFAPS) [MIM:308205]: A syndrome characterized by a peculiar triad of follicular ichthyosis, total or subtotal atrichia, and photophobia of varying degree. Histopathologically, the epidermal granular layer is generally well-preserved or thickened at the infundibulum. Hair follicles are poorly developed and tend to be surrounded by an inflammatory infiltrate. A subgroup of patients is described with lamellar rather than follicular ichthyosis. Non-consistent features may include growth and psychomotor retardation, aganglionic megacolon, seizures and nail dystrophy.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti87 – 871M → I in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
VAR_063054
Natural varianti226 – 2261W → L in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
VAR_063055
Natural varianti227 – 2271H → L in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
VAR_063056
Natural varianti429 – 4291R → H in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
VAR_063057
Natural varianti475 – 4751F → S in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
VAR_063058
Olmsted syndrome, X-linked (OLMSX) [MIM:300918]: A rare congenital disorder characterized by bilateral mutilating palmoplantar keratoderma and periorificial keratotic plaques with severe itching at all lesions. Diffuse alopecia, constriction of digits, and onychodystrophy have also been reported. Infections and squamous cell carcinomas can arise on the keratotic areas. The digital constriction may progress to autoamputation of fingers and toes.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti464 – 4641F → S in OLMSX. 1 Publication
VAR_071323
Keratosis follicularis spinulosa decalvans X-linked (KFSDX) [MIM:308800]: A rare disorder affecting the skin and the eye. Affected men show thickening of the skin of the neck, ears, and extremities, especially the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti508 – 5081N → S in KFSDX; sterol responsiveness is reduced by half. 1 Publication
VAR_064409

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi171 – 1711H → F: Loss of activity. 1 Publication
Mutagenesisi172 – 1721E → A or Q: Loss of activity. 1 Publication
Mutagenesisi172 – 1721E → D: Partial loss of activity. 1 Publication
Mutagenesisi175 – 1751H → F: Loss of activity. 1 Publication
Mutagenesisi467 – 4671D → N: Loss of activity. 1 Publication

Keywords - Diseasei

Disease mutation, Ichthyosis, Palmoplantar keratoderma

Organism-specific databases

MIMi300918. phenotype.
308205. phenotype.
308800. phenotype.
Orphaneti85284. BRESEK syndrome.
2273. Ichthyosis follicularis - alopecia - photophobia.
2340. Keratosis follicularis spinulosa decalvans.
659. Mutilating palmoplantar keratoderma with periorificial keratotic plaques.
PharmGKBiPA30672.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519Membrane-bound transcription factor site-2 proteasePRO_0000088482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi337 – 3371N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO43462.
PaxDbiO43462.
PRIDEiO43462.

PTM databases

PhosphoSiteiO43462.

Expressioni

Tissue specificityi

Expressed in heart, brain, placenta, lung, liver, muscle, kidney and pancreas.

Gene expression databases

BgeeiO43462.
CleanExiHS_MBTPS2.
ExpressionAtlasiO43462. baseline and differential.
GenevestigatoriO43462.

Organism-specific databases

HPAiCAB009486.
HPA005494.

Interactioni

Protein-protein interaction databases

BioGridi119495. 4 interactions.
STRINGi9606.ENSP00000368798.

Structurei

3D structure databases

ProteinModelPortaliO43462.
SMRiO43462. Positions 252-298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi109 – 13628Poly-SerAdd
BLAST
Compositional biasi285 – 386102Cys-richAdd
BLAST
Compositional biasi380 – 3845Poly-Ser

Sequence similaritiesi

Belongs to the peptidase M50A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0750.
GeneTreeiENSGT00510000048066.
HOGENOMiHOG000231255.
HOVERGENiHBG006397.
InParanoidiO43462.
KOiK07765.
OMAiHLQYTVS.
OrthoDBiEOG7WMCJB.
PhylomeDBiO43462.
TreeFamiTF314478.

Family and domain databases

InterProiIPR001193. MBTPS2.
IPR001478. PDZ.
IPR008915. Peptidase_M50.
[Graphical view]
PANTHERiPTHR13325. PTHR13325. 1 hit.
PfamiPF02163. Peptidase_M50. 1 hit.
[Graphical view]
PRINTSiPR01000. SREBPS2PTASE.
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43462-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIPVSLVVVV VGGWTVVYLT DLVLKSSVYF KHSYEDWLEN NGLSISPFHI
60 70 80 90 100
RWQTAVFNRA FYSWGRRKAR MLYQWFNFGM VFGVIAMFSS FFLLGKTLMQ
110 120 130 140 150
TLAQMMADSP SSYSSSSSSS SSSSSSSSSS SSSSSSLHNE QVLQVVVPGI
160 170 180 190 200
NLPVNQLTYF FTAVLISGVV HEIGHGIAAI REQVRFNGFG IFLFIIYPGA
210 220 230 240 250
FVDLFTTHLQ LISPVQQLRI FCAGIWHNFV LALLGILALV LLPVILLPFY
260 270 280 290 300
YTGVGVLITE VAEDSPAIGP RGLFVGDLVT HLQDCPVTNV QDWNECLDTI
310 320 330 340 350
AYEPQIGYCI SASTLQQLSF PVRAYKRLDG STECCNNHSL TDVCFSYRNN
360 370 380 390 400
FNKRLHTCLP ARKAVEATQV CRTNKDCKKS SSSSFCIIPS LETHTRLIKV
410 420 430 440 450
KHPPQIDMLY VGHPLHLHYT VSITSFIPRF NFLSIDLPVV VETFVKYLIS
460 470 480 490 500
LSGALAIVNA VPCFALDGQW ILNSFLDATL TSVIGDNDVK DLIGFFILLG
510
GSVLLAANVT LGLWMVTAR
Length:519
Mass (Da):57,444
Last modified:June 1, 1998 - v1
Checksum:i247D69E0FD7747BD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti87 – 871M → I in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
VAR_063054
Natural varianti226 – 2261W → L in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
VAR_063055
Natural varianti227 – 2271H → L in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
VAR_063056
Natural varianti429 – 4291R → H in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
VAR_063057
Natural varianti464 – 4641F → S in OLMSX. 1 Publication
VAR_071323
Natural varianti475 – 4751F → S in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
VAR_063058
Natural varianti508 – 5081N → S in KFSDX; sterol responsiveness is reduced by half. 1 Publication
VAR_064409

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019612 mRNA. Translation: AAC51937.1.
U73479 Genomic DNA. Translation: AAD08632.1.
U72788 Genomic DNA. Translation: AAD08631.1.
CCDSiCCDS14201.1.
RefSeqiNP_056968.1. NM_015884.3.
UniGeneiHs.443490.

Genome annotation databases

EnsembliENST00000379484; ENSP00000368798; ENSG00000012174.
GeneIDi51360.
KEGGihsa:51360.
UCSCiuc004dae.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019612 mRNA. Translation: AAC51937.1 .
U73479 Genomic DNA. Translation: AAD08632.1 .
U72788 Genomic DNA. Translation: AAD08631.1 .
CCDSi CCDS14201.1.
RefSeqi NP_056968.1. NM_015884.3.
UniGenei Hs.443490.

3D structure databases

ProteinModelPortali O43462.
SMRi O43462. Positions 252-298.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119495. 4 interactions.
STRINGi 9606.ENSP00000368798.

Protein family/group databases

MEROPSi M50.001.

PTM databases

PhosphoSitei O43462.

Proteomic databases

MaxQBi O43462.
PaxDbi O43462.
PRIDEi O43462.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379484 ; ENSP00000368798 ; ENSG00000012174 .
GeneIDi 51360.
KEGGi hsa:51360.
UCSCi uc004dae.3. human.

Organism-specific databases

CTDi 51360.
GeneCardsi GC0XP021857.
HGNCi HGNC:15455. MBTPS2.
HPAi CAB009486.
HPA005494.
MIMi 300294. gene.
300918. phenotype.
308205. phenotype.
308800. phenotype.
neXtProti NX_O43462.
Orphaneti 85284. BRESEK syndrome.
2273. Ichthyosis follicularis - alopecia - photophobia.
2340. Keratosis follicularis spinulosa decalvans.
659. Mutilating palmoplantar keratoderma with periorificial keratotic plaques.
PharmGKBi PA30672.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0750.
GeneTreei ENSGT00510000048066.
HOGENOMi HOG000231255.
HOVERGENi HBG006397.
InParanoidi O43462.
KOi K07765.
OMAi HLQYTVS.
OrthoDBi EOG7WMCJB.
PhylomeDBi O43462.
TreeFami TF314478.

Enzyme and pathway databases

BRENDAi 3.4.24.85. 2681.
Reactomei REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_18348. ATF6-alpha activates chaperones.

Miscellaneous databases

ChiTaRSi MBTPS2. human.
GenomeRNAii 51360.
NextBioi 54814.
PROi O43462.
SOURCEi Search...

Gene expression databases

Bgeei O43462.
CleanExi HS_MBTPS2.
ExpressionAtlasi O43462. baseline and differential.
Genevestigatori O43462.

Family and domain databases

InterProi IPR001193. MBTPS2.
IPR001478. PDZ.
IPR008915. Peptidase_M50.
[Graphical view ]
PANTHERi PTHR13325. PTHR13325. 1 hit.
Pfami PF02163. Peptidase_M50. 1 hit.
[Graphical view ]
PRINTSi PR01000. SREBPS2PTASE.
SUPFAMi SSF50156. SSF50156. 1 hit.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs."
    Rawson R.B., Zelenski N.G., Nijhawan D., Ye J., Sakai J., Hasan M.T., Chang T.Y., Brown M.S., Goldstein J.L.
    Mol. Cell 1:47-57(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF HIS-171; GLU-172; HIS-175 AND ASP-467.
    Tissue: Fibroblast.
  2. "The DNA sequence of the human X chromosome."
    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.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins."
    Zelenski N.G., Rawson R.B., Brown M.S., Goldstein J.L.
    J. Biol. Chem. 274:21973-21980(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY, GLYCOSYLATION AT ASN-337.
  4. "Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease."
    Ye J., Dave U.P., Grishin N.V., Goldstein J.L., Brown M.S.
    Proc. Natl. Acad. Sci. U.S.A. 97:5123-5128(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "IFAP syndrome is caused by deficiency in MBTPS2, an intramembrane zinc metalloprotease essential for cholesterol homeostasis and ER stress response."
    Oeffner F., Fischer G., Happle R., Konig A., Betz R.C., Bornholdt D., Neidel U., Boente Mdel C., Redler S., Romero-Gomez J., Salhi A., Vera-Casano A., Weirich C., Grzeschik K.H.
    Am. J. Hum. Genet. 84:459-467(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, VARIANTS IFAPS ILE-87; LEU-226; LEU-227; HIS-429 AND SER-475, CHARACTERIZATION OF VARIANTS IFAPS ILE-87; LEU-226; LEU-227; HIS-429 AND SER-475.
  6. Cited for: VARIANT KFSDX SER-508, CHARACTERIZATION OF VARIANT KFSDX SER-508.
  7. "A missense mutation in the MBTPS2 gene underlies the X-linked form of Olmsted syndrome."
    Haghighi A., Scott C.A., Poon D.S., Yaghoobi R., Saleh-Gohari N., Plagnol V., Kelsell D.P.
    J. Invest. Dermatol. 133:571-573(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN OLMSX, VARIANT OLMSX SER-464.

Entry informationi

Entry nameiMBTP2_HUMAN
AccessioniPrimary (citable) accession number: O43462
Secondary accession number(s): Q9UM70, Q9UMD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: November 26, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3