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Q92542 (NICA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nicastrin
Gene names
Name:NCSTN
Synonyms:KIAA0253
ORF Names:UNQ1874/PRO4317
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length709 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). It probably represents a stabilizing cofactor required for the assembly of the gamma-secretase complex.

Subunit structure

Component of the gamma-secretase complex, a complex composed of a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal complex is sufficient for secretase activity, although other components may exist. Binds to proteolytic processed C-terminal fragments C83 and C99 of the amyloid precursor protein (APP).

Subcellular location

Membrane; Single-pass type I membrane protein Potential. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.9 Ref.13

Tissue specificity

Widely expressed. Ref.8

Induction

Constitutively expressed in neural cells. Ref.8

Involvement in disease

Acne inversa, familial, 1 (ACNINV1) [MIM:142690]: A chronic relapsing inflammatory disease of the hair follicles characterized by recurrent draining sinuses, painful skin abscesses, and disfiguring scars. Manifestations typically appear after puberty.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.18 Ref.19

Sequence similarities

Belongs to the nicastrin family.

Ontologies

Keywords
   Biological processNotch signaling pathway
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch receptor processing

Traceable author statement PubMed 15274632. Source: HGNC

Notch signaling pathway

Traceable author statement. Source: Reactome

T cell proliferation

Inferred from electronic annotation. Source: Ensembl

amyloid precursor protein catabolic process

Traceable author statement PubMed 15274632. Source: HGNC

apoptotic signaling pathway

Traceable author statement. Source: Reactome

beta-amyloid metabolic process

Inferred from electronic annotation. Source: Ensembl

epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

membrane protein ectodomain proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

membrane protein intracellular domain proteolysis

Traceable author statement. Source: Reactome

myeloid cell homeostasis

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of catalytic activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein processing

Inferred from sequence or structural similarity. Source: UniProtKB

proteolysis

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

integral component of membrane

Non-traceable author statement Ref.1. Source: UniProtKB

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionendopeptidase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 12297508. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92542-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q92542-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.
     21-29: LSFCVLLAG → MDFNLILES
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 709676Nicastrin
PRO_0000019681

Regions

Topological domain34 – 669636Extracellular Potential
Transmembrane670 – 69021Helical; Potential
Topological domain691 – 70919Cytoplasmic Potential

Amino acid modifications

Glycosylation451N-linked (GlcNAc...) Ref.14
Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Ref.14
Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation3871N-linked (GlcNAc...) Ref.12 Ref.14
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4351N-linked (GlcNAc...) Potential
Glycosylation4641N-linked (GlcNAc...) Potential
Glycosylation5061N-linked (GlcNAc...) Potential
Glycosylation5301N-linked (GlcNAc...) Potential
Glycosylation5621N-linked (GlcNAc...) Potential
Glycosylation5731N-linked (GlcNAc...) Potential
Glycosylation5801N-linked (GlcNAc...) Potential
Glycosylation6121N-linked (GlcNAc...) Ref.15

Natural variations

Alternative sequence1 – 2020Missing in isoform 2.
VSP_008385
Alternative sequence21 – 299LSFCVLLAG → MDFNLILES in isoform 2.
VSP_008386
Natural variant751V → I.
Corresponds to variant rs12045198 [ dbSNP | Ensembl ].
VAR_050274
Natural variant771E → D.
Corresponds to variant rs35603924 [ dbSNP | Ensembl ].
VAR_050275
Natural variant2111P → R in ACNINV1. Ref.19
VAR_067756

Experimental info

Mutagenesis336 – 3372DY → AA: Increases production of amyloid beta (beta-APP40 and beta-APP42) in APP processing. Ref.1
Sequence conflict6571R → H in AAH47621. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: C8C0EAEAD89E976A

FASTA70978,411
        10         20         30         40         50         60 
MATAGGGSGA DPGSRGLLRL LSFCVLLAGL CRGNSVERKI YIPLNKTAPC VRLLNATHQI 

        70         80         90        100        110        120 
GCQSSISGDT GVIHVVEKEE DLQWVLTDGP NPPYMVLLES KHFTRDLMEK LKGRTSRIAG 

       130        140        150        160        170        180 
LAVSLTKPSP ASGFSPSVQC PNDGFGVYSN SYGPEFAHCR EIQWNSLGNG LAYEDFSFPI 

       190        200        210        220        230        240 
FLLEDENETK VIKQCYQDHN LSQNGSAPTF PLCAMQLFSH MHAVISTATC MRRSSIQSTF 

       250        260        270        280        290        300 
SINPEIVCDP LSDYNVWSML KPINTTGTLK PDDRVVVAAT RLDSRSFFWN VAPGAESAVA 

       310        320        330        340        350        360 
SFVTQLAAAE ALQKAPDVTT LPRNVMFVFF QGETFDYIGS SRMVYDMEKG KFPVQLENVD 

       370        380        390        400        410        420 
SFVELGQVAL RTSLELWMHT DPVSQKNESV RNQVEDLLAT LEKSGAGVPA VILRRPNQSQ 

       430        440        450        460        470        480 
PLPPSSLQRF LRARNISGVV LADHSGAFHN KYYQSIYDTA ENINVSYPEW LSPEEDLNFV 

       490        500        510        520        530        540 
TDTAKALADV ATVLGRALYE LAGGTNFSDT VQADPQTVTR LLYGFLIKAN NSWFQSILRQ 

       550        560        570        580        590        600 
DLRSYLGDGP LQHYIAVSSP TNTTYVVQYA LANLTGTVVN LTREQCQDPS KVPSENKDLY 

       610        620        630        640        650        660 
EYSWVQGPLH SNETDRLPRC VRSTARLARA LSPAFELSQW SSTEYSTWTE SRWKDIRARI 

       670        680        690        700 
FLIASKELEL ITLTVGFGIL IFSLIVTYCI NAKADVLFIA PREPGAVSY 

« Hide

Isoform 2 [UniParc].

Checksum: 58A8EE3F50F93459
Show »

FASTA68976,744

References

« Hide 'large scale' references
[1]"Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing."
Yu G., Nishimura M., Arawaka S., Levitan D., Zhang L., Tandon A., Song Y.-Q., Rogaeva E., Chen F., Kawarai T., Supala A., Levesque L., Yu H., Yang D.-S., Holmes E., Milman P., Liang Y., Zhang D.M. expand/collapse author list , Xu D.H., Sato C., Rogaev E., Smith M., Janus C., Zhang Y., Aebersold R., Farrer L.S., Sorbi S., Bruni A., Fraser P.E., St George-Hyslop P.H.
Nature 407:48-54(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF 336-ASP-TYR-337.
Tissue: Embryonic kidney.
[2]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[7]"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-709 (ISOFORM 1).
Tissue: Bone marrow.
[8]"Nicastrin, a key regulator of presenilin function, is expressed constitutively in human neural cell lines."
Satoh J., Kuroda Y.
Neuropathology 21:115-122(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[9]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[10]"Gamma-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2."
Kimberly W.T., LaVoie M.J., Ostaszewski B.L., Ye W., Wolfe M.S., Selkoe D.J.
Proc. Natl. Acad. Sci. U.S.A. 100:6382-6387(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF A GAMMA-SECRETASE COMPLEX WITH PEN2; PSEN1/PSEN2 AND APH1A.
[11]"Reconstitution of gamma-secretase activity."
Edbauer D., Winkler E., Regula J.T., Pesold B., Steiner H., Haass C.
Nat. Cell Biol. 5:486-488(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY OF A GAMMA-SECRETASE COMPLEX.
[12]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-387.
[13]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[14]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45; ASN-187 AND ASN-387.
Tissue: Liver.
[15]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-612.
Tissue: Leukemic T-cell.
[16]"Gamma-secretase gene mutations in familial acne inversa."
Wang B., Yang W., Wen W., Sun J., Su B., Liu B., Ma D., Lv D., Wen Y., Qu T., Chen M., Sun M., Shen Y., Zhang X.
Science 330:1065-1065(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ACNINV1.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Confirmation by exome sequencing of the pathogenic role of NCSTN mutations in acne inversa (hidradenitis suppurativa)."
Liu Y., Gao M., Lv Y.M., Yang X., Ren Y.Q., Jiang T., Zhang X., Guo B.R., Li M., Zhang Q., Zhang P., Zhou F.S., Chen G., Yin X.Y., Zuo X.B., Sun L.D., Zheng X.D., Zhang S.M. expand/collapse author list , Liu J.J., Zhou Y., Li Y.R., Wang J., Wang J., Yang H.M., Yang S., Li R.Q., Zhang X.J.
J. Invest. Dermatol. 131:1570-1572(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ACNINV1.
[19]"Two novel mutations of the nicastrin gene in Chinese patients with acne inversa."
Li C.R., Jiang M.J., Shen D.B., Xu H.X., Wang H.S., Yao X., Zhang Y., Zhou W.Q., Wang B.
Br. J. Dermatol. 165:415-418(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ACNINV1 ARG-211.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF240468 mRNA. Translation: AAG11412.1.
AY359120 mRNA. Translation: AAQ89478.1.
AK314764 mRNA. Translation: BAG37302.1.
AL445230 Genomic DNA. Translation: CAI15009.1.
AL445230 Genomic DNA. Translation: CAI15010.1.
CH471121 Genomic DNA. Translation: EAW52720.1.
CH471121 Genomic DNA. Translation: EAW52721.1.
CH471121 Genomic DNA. Translation: EAW52722.1.
BC047621 mRNA. Translation: AAH47621.1.
D87442 mRNA. Translation: BAA13383.1.
CCDSCCDS1203.1. [Q92542-1]
RefSeqNP_001277113.1. NM_001290184.1. [Q92542-2]
NP_001277115.1. NM_001290186.1.
NP_056146.1. NM_015331.2. [Q92542-1]
UniGeneHs.517249.

3D structure databases

ProteinModelPortalQ92542.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116961. 75 interactions.
DIPDIP-36336N.
IntActQ92542. 13 interactions.
MINTMINT-3048708.
STRING9606.ENSP00000294785.

Chemistry

BindingDBQ92542.
ChEMBLCHEMBL2094135.

PTM databases

PhosphoSiteQ92542.

Polymorphism databases

DMDM12231037.

Proteomic databases

MaxQBQ92542.
PaxDbQ92542.
PRIDEQ92542.

Protocols and materials databases

DNASU23385.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294785; ENSP00000294785; ENSG00000162736. [Q92542-1]
ENST00000368063; ENSP00000357042; ENSG00000162736. [Q92542-2]
ENST00000392212; ENSP00000376047; ENSG00000162736. [Q92542-2]
GeneID23385.
KEGGhsa:23385.
UCSCuc001fvx.3. human. [Q92542-1]
uc001fvy.3. human. [Q92542-2]

Organism-specific databases

CTD23385.
GeneCardsGC01P160313.
HGNCHGNC:17091. NCSTN.
HPACAB021982.
HPA051793.
MIM142690. phenotype.
605254. gene.
neXtProtNX_Q92542.
Orphanet387. Hidradenitis suppurativa.
PharmGKBPA142671271.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253370.
HOGENOMHOG000044212.
HOVERGENHBG006497.
InParanoidQ92542.
KOK06171.
OMAHMHAVIS.
OrthoDBEOG77WWCF.
PhylomeDBQ92542.
TreeFamTF317086.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.
REACT_691. A third proteolytic cleavage releases NICD.
SignaLinkQ92542.

Gene expression databases

ArrayExpressQ92542.
BgeeQ92542.
CleanExHS_NCSTN.
GenevestigatorQ92542.

Family and domain databases

InterProIPR008710. Nicastrin.
[Graphical view]
PANTHERPTHR21092. PTHR21092. 1 hit.
PfamPF05450. Nicastrin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNicastrin.
GenomeRNAi23385.
NextBio45500.
PROQ92542.
SOURCESearch...

Entry information

Entry nameNICA_HUMAN
AccessionPrimary (citable) accession number: Q92542
Secondary accession number(s): Q5T207, Q5T208, Q86VV5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 11, 2001
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM