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Q14703

- MBTP1_HUMAN

UniProt

Q14703 - MBTP1_HUMAN

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Protein

Membrane-bound transcription factor site-1 protease

Gene
MBTPS1, KIAA0091, S1P, SKI1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Serine protease that catalyzes the first step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs). Other known substrates are BDNF, GNPTAB and ATF6. Cleaves after hydrophobic or small residues, provided that Arg or Lys is in position P4. Cleaves known substrates after Arg-Ser-Val-Leu (SERBP-2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr (BDNF) and its own propeptide after Arg-Arg-Leu-Leu. Mediates the protein cleavage of GNPTAB into subunit alpha and beta, thereby participating in biogenesis of lysosomes.1 Publication

Catalytic activityi

Processes precursors containing basic and hydrophobic/aliphatic residues at P4 and P2, respectively, with a relatively relaxed acceptance of amino acids at P1 and P3.

Cofactori

Calcium.

Enzyme regulationi

Inhibited by divalent copper and zinc ions, but not by nickel or cobalt. Inhibited by its prosegment, but not smaller fragments thereof.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei186 – 1872Cleavage; by autolysis
Active sitei218 – 2181Charge relay system By similarity
Active sitei249 – 2491Charge relay system By similarity
Active sitei414 – 4141Charge relay system By similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: UniProtKB

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: UniProtKB-KW
  4. endoplasmic reticulum unfolded protein response Source: Reactome
  5. lipid metabolic process Source: RefGenome
  6. lysosome organization Source: UniProtKB
  7. proteolysis Source: UniProtKB
  8. regulation of transcription factor import into nucleus Source: Ensembl
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_18348. ATF6-alpha activates chaperones.
SignaLinkiQ14703.

Protein family/group databases

MEROPSiS08.063.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-bound transcription factor site-1 protease (EC:3.4.21.112)
Alternative name(s):
Endopeptidase S1P
Subtilisin/kexin-isozyme 1
Short name:
SKI-1
Gene namesi
Name:MBTPS1
Synonyms:KIAA0091, S1P, SKI1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:15456. MBTPS1.

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein
Note: May sort to other organelles, including lysosomal and/or endosomal compartments.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini187 – 998812Lumenal Reviewed predictionAdd
BLAST
Transmembranei999 – 102123Helical; Reviewed predictionAdd
BLAST
Topological domaini1022 – 105231Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: ProtInc
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. Golgi apparatus Source: RefGenome
  4. Golgi membrane Source: Reactome
  5. Golgi stack Source: Ensembl
  6. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30671.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Add
BLAST
Propeptidei18 – 186169PRO_0000027051Add
BLAST
Chaini187 – 1052866Membrane-bound transcription factor site-1 proteasePRO_0000027052Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi236 – 2361N-linked (GlcNAc...) Reviewed prediction
Glycosylationi305 – 3051N-linked (GlcNAc...) Reviewed prediction
Glycosylationi515 – 5151N-linked (GlcNAc...) Reviewed prediction
Glycosylationi728 – 7281N-linked (GlcNAc...) Reviewed prediction
Glycosylationi939 – 9391N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

The 148 kDa zymogen is processed progressively into two membrane-bound 120 and 106 kDa forms in the endoplasmic reticulum, and late into a secreted 98 kDa form. The propeptide is autocatalytically removed through an intramolecular cleavage after Leu-186. Further cleavage generates 14, 10, and 8 kDa intermediates.

Keywords - PTMi

Autocatalytic cleavage, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ14703.
PaxDbiQ14703.
PRIDEiQ14703.

PTM databases

PhosphoSiteiQ14703.

Miscellaneous databases

PMAP-CutDBQ14703.

Expressioni

Tissue specificityi

Widely expressed.

Inductioni

Down-regulated by sterols.

Gene expression databases

ArrayExpressiQ14703.
BgeeiQ14703.
CleanExiHS_MBTPS1.
GenevestigatoriQ14703.

Organism-specific databases

HPAiHPA006239.

Interactioni

Protein-protein interaction databases

BioGridi114259. 11 interactions.
IntActiQ14703. 7 interactions.
MINTiMINT-6774172.
STRINGi9606.ENSP00000344223.

Structurei

3D structure databases

ProteinModelPortaliQ14703.
SMRiQ14703. Positions 53-473.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni218 – 414197Serine proteaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1023 – 105028Arg/Lys/Pro-rich (basic)Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S8 family.

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1404.
HOGENOMiHOG000030053.
HOVERGENiHBG052421.
InParanoidiQ14703.
KOiK08653.
OMAiLPERMEG.
OrthoDBiEOG7TBC1F.
PhylomeDBiQ14703.
TreeFamiTF324501.

Family and domain databases

Gene3Di3.40.50.200. 2 hits.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 2 hits.
PROSITEiPS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q14703-1 [UniParc]FASTAAdd to Basket

« Hide

MKLVNIWLLL LVVLLCGKKH LGDRLEKKSF EKAPCPGCSH LTLKVEFSST     50
VVEYEYIVAF NGYFTAKARN SFISSALKSS EVDNWRIIPR NNPSSDYPSD 100
FEVIQIKEKQ KAGLLTLEDH PNIKRVTPQR KVFRSLKYAE SDPTVPCNET 150
RWSQKWQSSR PLRRASLSLG SGFWHATGRH SSRRLLRAIP RQVAQTLQAD 200
VLWQMGYTGA NVRVAVFDTG LSEKHPHFKN VKERTNWTNE RTLDDGLGHG 250
TFVAGVIASM RECQGFAPDA ELHIFRVFTN NQVSYTSWFL DAFNYAILKK 300
IDVLNLSIGG PDFMDHPFVD KVWELTANNV IMVSAIGNDG PLYGTLNNPA 350
DQMDVIGVGG IDFEDNIARF SSRGMTTWEL PGGYGRMKPD IVTYGAGVRG 400
SGVKGGCRAL SGTSVASPVV AGAVTLLVST VQKRELVNPA SMKQALIASA 450
RRLPGVNMFE QGHGKLDLLR AYQILNSYKP QASLSPSYID LTECPYMWPY 500
CSQPIYYGGM PTVVNVTILN GMGVTGRIVD KPDWQPYLPQ NGDNIEVAFS 550
YSSVLWPWSG YLAISISVTK KAASWEGIAQ GHVMITVASP AETESKNGAE 600
QTSTVKLPIK VKIIPTPPRS KRVLWDQYHN LRYPPGYFPR DNLRMKNDPL 650
DWNGDHIHTN FRDMYQHLRS MGYFVEVLGA PFTCFDASQY GTLLMVDSEE 700
EYFPEEIAKL RRDVDNGLSL VIFSDWYNTS VMRKVKFYDE NTRQWWMPDT 750
GGANIPALNE LLSVWNMGFS DGLYEGEFTL ANHDMYYASG CSIAKFPEDG 800
VVITQTFKDQ GLEVLKQETA VVENVPILGL YQIPAEGGGR IVLYGDSNCL 850
DDSHRQKDCF WLLDALLQYT SYGVTPPSLS HSGNRQRPPS GAGSVTPERM 900
EGNHLHRYSK VLEAHLGDPK PRPLPACPRL SWAKPQPLNE TAPSNLWKHQ 950
KLLSIDLDKV VLPNFRSNRP QVRPLSPGES GAWDIPGGIM PGRYNQEVGQ 1000
TIPVFAFLGA MVVLAFFVVQ INKAKSRPKR RKPRVKRPQL MQQVHPPKTP 1050
SV 1052
Length:1,052
Mass (Da):117,749
Last modified:November 1, 1996 - v1
Checksum:iCA6F013588595B45
GO

Sequence cautioni

The sequence BAA07653.2 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61I → T.
Corresponds to variant rs34701895 [ dbSNP | Ensembl ].
VAR_051822
Natural varianti90 – 901R → G.
Corresponds to variant rs34076105 [ dbSNP | Ensembl ].
VAR_051823

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti843 – 8431L → Q in BAF84462. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D42053 mRNA. Translation: BAA07653.2. Different initiation.
AK291773 mRNA. Translation: BAF84462.1.
AC040169 Genomic RNA. No translation available.
BC114555 mRNA. Translation: AAI14556.1.
BC114961 mRNA. Translation: AAI14962.1.
AL133583 mRNA. Translation: CAB63727.1.
CCDSiCCDS10941.1.
PIRiT43492.
RefSeqiNP_003782.1. NM_003791.3.
UniGeneiHs.75890.

Genome annotation databases

EnsembliENST00000343411; ENSP00000344223; ENSG00000140943.
GeneIDi8720.
KEGGihsa:8720.
UCSCiuc002fhh.3. human.

Polymorphism databases

DMDMi17368466.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D42053 mRNA. Translation: BAA07653.2 . Different initiation.
AK291773 mRNA. Translation: BAF84462.1 .
AC040169 Genomic RNA. No translation available.
BC114555 mRNA. Translation: AAI14556.1 .
BC114961 mRNA. Translation: AAI14962.1 .
AL133583 mRNA. Translation: CAB63727.1 .
CCDSi CCDS10941.1.
PIRi T43492.
RefSeqi NP_003782.1. NM_003791.3.
UniGenei Hs.75890.

3D structure databases

ProteinModelPortali Q14703.
SMRi Q14703. Positions 53-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114259. 11 interactions.
IntActi Q14703. 7 interactions.
MINTi MINT-6774172.
STRINGi 9606.ENSP00000344223.

Chemistry

BindingDBi Q14703.
ChEMBLi CHEMBL5916.

Protein family/group databases

MEROPSi S08.063.

PTM databases

PhosphoSitei Q14703.

Polymorphism databases

DMDMi 17368466.

Proteomic databases

MaxQBi Q14703.
PaxDbi Q14703.
PRIDEi Q14703.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343411 ; ENSP00000344223 ; ENSG00000140943 .
GeneIDi 8720.
KEGGi hsa:8720.
UCSCi uc002fhh.3. human.

Organism-specific databases

CTDi 8720.
GeneCardsi GC16M084087.
HGNCi HGNC:15456. MBTPS1.
HPAi HPA006239.
MIMi 603355. gene.
neXtProti NX_Q14703.
PharmGKBi PA30671.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1404.
HOGENOMi HOG000030053.
HOVERGENi HBG052421.
InParanoidi Q14703.
KOi K08653.
OMAi LPERMEG.
OrthoDBi EOG7TBC1F.
PhylomeDBi Q14703.
TreeFami TF324501.

Enzyme and pathway databases

Reactomei REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_18348. ATF6-alpha activates chaperones.
SignaLinki Q14703.

Miscellaneous databases

ChiTaRSi MBTPS1. human.
GenomeRNAii 8720.
NextBioi 32705.
PMAP-CutDB Q14703.
PROi Q14703.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14703.
Bgeei Q14703.
CleanExi HS_MBTPS1.
Genevestigatori Q14703.

Family and domain databases

Gene3Di 3.40.50.200. 2 hits.
InterProi IPR000209. Peptidase_S8/S53_dom.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
[Graphical view ]
PANTHERi PTHR10795. PTHR10795. 1 hit.
Pfami PF00082. Peptidase_S8. 1 hit.
[Graphical view ]
PRINTSi PR00723. SUBTILISIN.
SUPFAMi SSF52743. SSF52743. 2 hits.
PROSITEi PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic structure and chromosomal mapping of the human site-1 protease (S1P) gene."
    Nakajima T., Iwaki K., Kodama T., Inazawa J., Emi M.
    J. Hum. Genet. 45:212-217(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Myeloid.
  2. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  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.
    , 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].
    Tissue: Placenta.
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 735-1052.
    Tissue: Testis.
  7. "Biosynthesis and enzymatic characterization of human SKI-1/S1P and the processing of its inhibitory prosegment."
    Toure B.B., Munzer J.S., Basak A., Benjannet S., Rochemont J., Lazure C., Chretien M., Seidah N.G.
    J. Biol. Chem. 275:2349-2358(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Mammalian subtilisin/kexin isozyme SKI-1: a widely expressed proprotein convertase with a unique cleavage specificity and cellular localization."
    Seidah N.G., Mowla S.J., Hamelin J., Mamarbachi A.M., Benjannet S., Toure B.B., Basak A., Munzer J.S., Marcinkiewicz J., Zhong M., Barale J.-C., Lazure C., Murphy R.A., Chretien M., Marcinkiewicz M.
    Proc. Natl. Acad. Sci. U.S.A. 96:1321-1326(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "A key enzyme in the biogenesis of lysosomes is a protease that regulates cholesterol metabolism."
    Marschner K., Kollmann K., Schweizer M., Braulke T., Pohl S.
    Science 333:87-90(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMBTP1_HUMAN
AccessioniPrimary (citable) accession number: Q14703
Secondary accession number(s): A8K6V8, Q24JQ2, Q9UF67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 135 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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

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