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Protein

Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating

Gene

NSDHL

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

Functioni

Involved in the sequential removal of two C-4 methyl groups in post-squalene cholesterol biosynthesis.1 Publication

Catalytic activityi

A 3-beta-hydroxysteroid-4-alpha-carboxylate + NAD(P)+ = a 3-oxosteroid + CO2 + NAD(P)H.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei172 – 1721Proton acceptorBy similarity
Binding sitei176 – 1761NADBy similarity

GO - Molecular functioni

  1. 3-beta-hydroxy-delta5-steroid dehydrogenase activity Source: ProtInc
  2. sterol-4-alpha-carboxylate 3-dehydrogenase (decarboxylating) activity Source: UniProtKB-EC

GO - Biological processi

  1. cholesterol biosynthetic process Source: Reactome
  2. hair follicle development Source: Ensembl
  3. labyrinthine layer blood vessel development Source: Ensembl
  4. small molecule metabolic process Source: Reactome
  5. smoothened signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS07423-MONOMER.
ReactomeiREACT_9405. Cholesterol biosynthesis.
UniPathwayiUPA00770; UER00757.

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (EC:1.1.1.170)
Alternative name(s):
Protein H105e3
Gene namesi
Name:NSDHL
Synonyms:H105E3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:13398. NSDHL.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Single-pass membrane protein 1 Publication. Lipid droplet 1 Publication
Note: Trafficking through the Golgi is necessary for ER membrane localization.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei298 – 31821HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: LIFEdb
  2. endoplasmic reticulum membrane Source: Reactome
  3. integral component of membrane Source: UniProtKB-KW
  4. intracellular membrane-bounded organelle Source: HPA
  5. lipid particle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital hemidysplasia with ichthyosiform erythroderma and limb defects (CHILD)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn X-linked dominant disorder of lipid metabolism with disturbed cholesterol biosynthesis, which typically results in male lethality. Clinically, it is characterized by congenital, unilateral, ichthyosisform erythroderma with striking lateralization, sharp midline demarcation, and ipsilateral limb defects and hypoplasia of the body. Limbs defects range from hypoplasia of digits or ribs to complete amelia, often including scoliosis.

See also OMIM:308050
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051A → V in CHILD. 1 Publication
VAR_010207
Natural varianti182 – 1821A → P in CHILD. 1 Publication
VAR_065289
Natural varianti205 – 2051G → S in CHILD. 1 Publication
VAR_010208
CK syndrome (CKS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by mild to severe cognitive impairment, seizures, microcephaly, cerebral cortical malformations, dysmorphic facial features, and thin body habitus.

See also OMIM:300831
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti232 – 2321Missing in CKS; temperature-sensitive hypomorphic mutation; able to correctly fold and function at 30 degrees Celsius; impaired function at 37 degrees Celsius due to abnormal folding and protein degradation. 1 Publication
VAR_065290

Keywords - Diseasei

Disease mutation, Ichthyosis, Mental retardation

Organism-specific databases

MIMi300831. phenotype.
308050. phenotype.
Orphaneti139. CHILD syndrome.
251383. CK syndrome.
PharmGKBiPA134959020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 373373Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylatingPRO_0000087799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ15738.
PaxDbiQ15738.
PeptideAtlasiQ15738.
PRIDEiQ15738.

2D gel databases

REPRODUCTION-2DPAGEQ15738.

PTM databases

PhosphoSiteiQ15738.

Expressioni

Tissue specificityi

Brain, heart, liver, lung, kidney, skin and placenta.

Gene expression databases

BgeeiQ15738.
CleanExiHS_NSDHL.
ExpressionAtlasiQ15738. baseline and differential.
GenevestigatoriQ15738.

Organism-specific databases

HPAiHPA000248.
HPA000571.

Interactioni

Protein-protein interaction databases

BioGridi119131. 11 interactions.
IntActiQ15738. 1 interaction.
MINTiMINT-5001307.
STRINGi9606.ENSP00000359297.

Structurei

3D structure databases

ProteinModelPortaliQ15738.
SMRiQ15738. Positions 39-366.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi359 – 3624Prevents secretion from ER

Sequence similaritiesi

Belongs to the 3-beta-HSD family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0451.
GeneTreeiENSGT00550000074557.
HOGENOMiHOG000167989.
HOVERGENiHBG054675.
InParanoidiQ15738.
KOiK07748.
OMAiEPMRDQV.
PhylomeDBiQ15738.
TreeFamiTF354279.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002225. 3Beta_OHSteriod_DH/Estase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01073. 3Beta_HSD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15738-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPAVSEPMR DQVARTHLTE DTPKVNADIE KVNQNQAKRC TVIGGSGFLG
60 70 80 90 100
QHMVEQLLAR GYAVNVFDIQ QGFDNPQVRF FLGDLCSRQD LYPALKGVNT
110 120 130 140 150
VFHCASPPPS SNNKELFYRV NYIGTKNVIE TCKEAGVQKL ILTSSASVIF
160 170 180 190 200
EGVDIKNGTE DLPYAMKPID YYTETKILQE RAVLGANDPE KNFLTTAIRP
210 220 230 240 250
HGIFGPRDPQ LVPILIEAAR NGKMKFVIGN GKNLVDFTFV ENVVHGHILA
260 270 280 290 300
AEQLSRDSTL GGKAFHITND EPIPFWTFLS RILTGLNYEA PKYHIPYWVA
310 320 330 340 350
YYLALLLSLL VMVISPVIQL QPTFTPMRVA LAGTFHYYSC ERAKKAMGYQ
360 370
PLVTMDDAME RTVQSFRHLR RVK
Length:373
Mass (Da):41,900
Last modified:May 29, 2000 - v2
Checksum:i30A6E5CE91ED1C77
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051A → V in CHILD. 1 Publication
VAR_010207
Natural varianti182 – 1821A → P in CHILD. 1 Publication
VAR_065289
Natural varianti205 – 2051G → S in CHILD. 1 Publication
VAR_010208
Natural varianti232 – 2321Missing in CKS; temperature-sensitive hypomorphic mutation; able to correctly fold and function at 30 degrees Celsius; impaired function at 37 degrees Celsius due to abnormal folding and protein degradation. 1 Publication
VAR_065290

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47105 mRNA. Translation: AAC50558.2.
U82671 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72898.1.
CH471172 Genomic DNA. Translation: EAW72899.1.
BC000245 mRNA. Translation: AAH00245.1.
BC007816 mRNA. Translation: AAH07816.1.
CCDSiCCDS14717.1.
RefSeqiNP_001123237.1. NM_001129765.1.
NP_057006.1. NM_015922.2.
XP_006724887.1. XM_006724824.1.
UniGeneiHs.57698.

Genome annotation databases

EnsembliENST00000370274; ENSP00000359297; ENSG00000147383.
ENST00000440023; ENSP00000391854; ENSG00000147383.
GeneIDi50814.
KEGGihsa:50814.
UCSCiuc004fgs.1. human.

Polymorphism databases

DMDMi8488997.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47105 mRNA. Translation: AAC50558.2.
U82671 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72898.1.
CH471172 Genomic DNA. Translation: EAW72899.1.
BC000245 mRNA. Translation: AAH00245.1.
BC007816 mRNA. Translation: AAH07816.1.
CCDSiCCDS14717.1.
RefSeqiNP_001123237.1. NM_001129765.1.
NP_057006.1. NM_015922.2.
XP_006724887.1. XM_006724824.1.
UniGeneiHs.57698.

3D structure databases

ProteinModelPortaliQ15738.
SMRiQ15738. Positions 39-366.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119131. 11 interactions.
IntActiQ15738. 1 interaction.
MINTiMINT-5001307.
STRINGi9606.ENSP00000359297.

PTM databases

PhosphoSiteiQ15738.

Polymorphism databases

DMDMi8488997.

2D gel databases

REPRODUCTION-2DPAGEQ15738.

Proteomic databases

MaxQBiQ15738.
PaxDbiQ15738.
PeptideAtlasiQ15738.
PRIDEiQ15738.

Protocols and materials databases

DNASUi50814.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370274; ENSP00000359297; ENSG00000147383.
ENST00000440023; ENSP00000391854; ENSG00000147383.
GeneIDi50814.
KEGGihsa:50814.
UCSCiuc004fgs.1. human.

Organism-specific databases

CTDi50814.
GeneCardsiGC0XP151999.
GeneReviewsiNSDHL.
HGNCiHGNC:13398. NSDHL.
HPAiHPA000248.
HPA000571.
MIMi300275. gene.
300831. phenotype.
308050. phenotype.
neXtProtiNX_Q15738.
Orphaneti139. CHILD syndrome.
251383. CK syndrome.
PharmGKBiPA134959020.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0451.
GeneTreeiENSGT00550000074557.
HOGENOMiHOG000167989.
HOVERGENiHBG054675.
InParanoidiQ15738.
KOiK07748.
OMAiEPMRDQV.
PhylomeDBiQ15738.
TreeFamiTF354279.

Enzyme and pathway databases

UniPathwayiUPA00770; UER00757.
BioCyciMetaCyc:HS07423-MONOMER.
ReactomeiREACT_9405. Cholesterol biosynthesis.

Miscellaneous databases

GeneWikiiNSDHL.
GenomeRNAii50814.
NextBioi53261.
PROiQ15738.
SOURCEiSearch...

Gene expression databases

BgeeiQ15738.
CleanExiHS_NSDHL.
ExpressionAtlasiQ15738. baseline and differential.
GenevestigatoriQ15738.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002225. 3Beta_OHSteriod_DH/Estase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01073. 3Beta_HSD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Levin M.L., Herman G.E.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  7. "A comparative transcription map of the murine bare patches (Bpa) and striated (Str) critical regions and human Xq28."
    Levin M.L., Chatterjee A., Pragliola A., Worley K.C., Wehnert M., Zhuchenko O., Smith R.F., Lee C.C., Herman G.E.
    Genome Res. 6:465-477(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 224-373.
    Tissue: Heart.
  8. "NSDHL, an enzyme involved in cholesterol biosynthesis, traffics through the Golgi and accumulates on ER membranes and on the surface of lipid droplets."
    Caldas H., Herman G.E.
    Hum. Mol. Genet. 12:2981-2991(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ER RETENTION MOTIF.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Mutations in the NSDHL gene, encoding a 3beta-hydroxysteroid dehydrogenase, cause CHILD syndrome."
    Konig A., Happle R., Bornholdt D., Engel H., Grzeschik K.H.
    Am. J. Med. Genet. 90:339-346(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CHILD VAL-105 AND SER-205.
  14. "A novel missense mutation of NSDHL in an unusual case of CHILD syndrome showing bilateral, almost symmetric involvement."
    Konig A., Happle R., Fink-Puches R., Soyer H.P., Bornholdt D., Engel H., Grzeschik K.H.
    J. Am. Acad. Dermatol. 46:594-596(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CHILD PRO-182.
  15. Cited for: VARIANT CKS LYS-232 DEL, CHARACTERIZATION OF VARIANT CKS LYS-232 DEL.

Entry informationi

Entry nameiNSDHL_HUMAN
AccessioniPrimary (citable) accession number: Q15738
Secondary accession number(s): D3DWT6, O00344
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: May 29, 2000
Last modified: March 3, 2015
This is version 139 of the entry and version 2 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.