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Q8N608 (DPP10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inactive dipeptidyl peptidase 10
Alternative name(s):
Dipeptidyl peptidase IV-related protein 3
Short name=DPRP-3
Dipeptidyl peptidase X
Short name=DPP X
Dipeptidyl peptidase-like protein 2
Short name=DPL2
Gene names
Name:DPP10
Synonyms:DPRP3, KIAA1492
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length796 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has no dipeptidyl aminopeptidase activity. May modulate cell surface expression and activity of the potassium channels KCND1 and KCND2. Ref.2 Ref.9 Ref.10

Subunit structure

May form oligomers. Interacts with KCND1 Probable. Interacts with KCND2. Ref.3 Ref.9

Subcellular location

Membrane; Single-pass type II membrane protein Ref.2 Ref.3.

Tissue specificity

Found in serum, T-cells and brain (at protein level). Expressed in brain, pancreas, spinal cord and adrenal glands. Ref.2 Ref.3

Post-translational modification

N-glycosylation is important for cell surface expression, specially at Asn-257, which is crucial.

Involvement in disease

Asthma (ASTHMA) [MIM:600807]: The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with wheezing due to spasmodic contraction of the bronchi.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.3 Ref.12

Sequence similarities

Belongs to the peptidase S9B family. DPPIV subfamily.

Caution

Gly-651 is present instead of the conserved Ser which is expected to be an active site residue suggesting that this protein has no peptidase activity.

Sequence caution

The sequence BAA96016.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAsthma
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay Ref.2. Source: MGI

   Molecular_functionserine-type peptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist, which may have different subcellular locations.
Isoform 1 (identifier: Q8N608-1)

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: Q8N608-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MNQTASVSHHIKCQPSKTIK → MRKVESRGEGGRE
Isoform 3 (identifier: Q8N608-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MNQTASVSHHIKCQPSKTIK → MTAAKQEPQPTPGARASQAQPADQ
Isoform 4 (identifier: Q8N608-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 796796Inactive dipeptidyl peptidase 10
PRO_0000122417

Regions

Topological domain1 – 3434Cytoplasmic Potential
Transmembrane35 – 5521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain56 – 796741Extracellular Potential
Region1 – 5656Mediates effects on KCND2

Amino acid modifications

Modified residue1381Phosphotyrosine Ref.11
Modified residue1431Phosphotyrosine Ref.11
Glycosylation901N-linked (GlcNAc...) Ref.13
Glycosylation1111N-linked (GlcNAc...) Ref.13
Glycosylation1191N-linked (GlcNAc...) Ref.13
Glycosylation2571N-linked (GlcNAc...) Ref.13
Glycosylation3421N-linked (GlcNAc...) Ref.13
Glycosylation7481N-linked (GlcNAc...) Ref.13

Natural variations

Alternative sequence1 – 5050Missing in isoform 4.
VSP_047152
Alternative sequence1 – 2020MNQTA…SKTIK → MRKVESRGEGGRE in isoform 2.
VSP_013873
Alternative sequence1 – 2020MNQTA…SKTIK → MTAAKQEPQPTPGARASQAQ PADQ in isoform 3.
VSP_044466
Natural variant3401A → P. Ref.1 Ref.5
Corresponds to variant rs2053724 [ dbSNP | Ensembl ].
VAR_057061
Natural variant4011V → I. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs1446495 [ dbSNP | Ensembl ].
VAR_059759
Natural variant5171S → N.
Corresponds to variant rs13421193 [ dbSNP | Ensembl ].
VAR_057062

Experimental info

Mutagenesis2571N → Q: Abolishes sorting to the cell surface and dimerization. Ref.13
Sequence conflict2881V → M in AAO17263. Ref.2
Sequence conflict2881V → M in BAF82656. Ref.5
Sequence conflict2881V → M in AAH30832. Ref.7
Sequence conflict6871F → L in AAQ91190. Ref.1
Isoform 3:
Sequence conflict41A → M in ABI16086. Ref.4

Sequences

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

Last modified May 18, 2010. Version 2.
Checksum: 072CBD67D1FB478E

FASTA79690,888
        10         20         30         40         50         60 
MNQTASVSHH IKCQPSKTIK ELGSNSPPQR NWKGIAIALL VILVVCSLIT MSVILLTPDE 

        70         80         90        100        110        120 
LTNSSETRLS LEDLFRKDFV LHDPEARWIN DTDVVYKSEN GHVIKLNIET NATTLLLENT 

       130        140        150        160        170        180 
TFVTFKASRH SVSPDLKYVL LAYDVKQIFH YSYTASYVIY NIHTREVWEL NPPEVEDSVL 

       190        200        210        220        230        240 
QYAAWGVQGQ QLIYIFENNI YYQPDIKSSS LRLTSSGKEE IIFNGIADWL YEEELLHSHI 

       250        260        270        280        290        300 
AHWWSPDGER LAFLMINDSL VPTMVIPRFT GALYPKGKQY PYPKAGQVNP TIKLYVVNLY 

       310        320        330        340        350        360 
GPTHTLELMP PDSFKSREYY ITMVKWVSNT KTVVRWLNRA QNISILTVCE TTTGACSKKY 

       370        380        390        400        410        420 
EMTSDTWLSQ QNEEPVFSRD GSKFFMTVPV KQGGRGEFHH VAMFLIQSKS EQITVRHLTS 

       430        440        450        460        470        480 
GNWEVIKILA YDETTQKIYF LSTESSPRGR QLYSASTEGL LNRQCISCNF MKEQCTYFDA 

       490        500        510        520        530        540 
SFSPMNQHFL LFCEGPRVPV VSLHSTDNPA KYFILESNSM LKEAILKKKI GKPEIKILHI 

       550        560        570        580        590        600 
DDYELPLQLS LPKDFMDRNQ YALLLIMDEE PGGQLVTDKF HIDWDSVLID MDNVIVARFD 

       610        620        630        640        650        660 
GRGSGFQGLK ILQEIHRRLG SVEVKDQITA VKFLLKLPYI DSKRLSIFGK GYGGYIASMI 

       670        680        690        700        710        720 
LKSDEKLFKC GSVVAPITDL KLYASAFSER YLGMPSKEES TYQAASVLHN VHGLKEENIL 

       730        740        750        760        770        780 
IIHGTADTKV HFQHSAELIK HLIKAGVNYT MQVYPDEGHN VSEKSKYHLY STILKFFSDC 

       790 
LKEEISVLPQ EPEEDE 

« Hide

Isoform 2 [UniParc].

Checksum: F1746DDCA46C0744
Show »

FASTA78990,140
Isoform 3 [UniParc].

Checksum: C837D61773C3E890
Show »

FASTA80091,129
Isoform 4 [UniParc].

Checksum: F71826F40623C64D
Show »

FASTA74685,480

References

« Hide 'large scale' references
[1]"Dipeptidyl peptidase IV gene family. The DPIV family."
Chen T., Ajami K., McCaughan G.W., Gorrell M.D., Abbott C.A.
Adv. Exp. Med. Biol. 524:79-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS PRO-340 AND ILE-401.
Tissue: Brain.
[2]"Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases."
Qi S.Y., Riviere P.J., Trojnar J., Junien J.-L., Akinsanya K.O.
Biochem. J. 373:179-189(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT ILE-401.
Tissue: Hypothalamus.
[3]"Positional cloning of a novel gene influencing asthma from chromosome 2q14."
Allen M., Heinzmann A., Noguchi E., Abecasis G., Broxholme J., Ponting C.P., Bhattacharyya S., Tinsley J., Zhang Y., Holt R., Jones E.Y., Lench N., Carey A., Jones H., Dickens N.J., Dimon C., Nicholls R., Baker C. expand/collapse author list , Xue L., Townsend E., Kabesch M., Weiland S.K., Carr D., von Mutius E., Adcock I.M., Barnes P.J., Lathrop G.M., Edwards M., Moffatt M.F., Cookson W.O.C.M.
Nat. Genet. 35:258-263(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN ASTHMA, VARIANT ILE-401.
[4]"Species and tissue differences in the expression of DPPY splicing variants."
Takimoto K., Hayashi Y., Ren X., Yoshimura N.
Biochem. Biophys. Res. Commun. 348:1094-1100(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT ILE-401, ALTERNATIVE SPLICING.
[5]"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS PRO-340 AND ILE-401.
Tissue: Brain.
[6]"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), VARIANT ILE-401.
Tissue: Hippocampus.
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 1), VARIANT ILE-401.
Tissue: Brain.
[9]"Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase 10 (DPP10)."
Jerng H.H., Qian Y., Pfaffinger P.J.
Biophys. J. 87:2380-2396(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, GLYCOSYLATION, INTERACTION WITH KCND1 AND KCND2.
[10]"DPP10 modulates Kv4-mediated A-type potassium channels."
Zagha E., Ozaita A., Chang S.Y., Nadal M.S., Lin U., Saganich M.J., McCormack T., Akinsanya K.O., Qi S.Y., Rudy B.
J. Biol. Chem. 280:18853-18861(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-138 AND TYR-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Positionally cloned asthma susceptibility gene polymorphisms and disease risk in the British 1958 Birth Cohort."
Blakey J.D., Sayers I., Ring S.M., Strachan D.P., Hall I.P.
Thorax 64:381-387(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
[13]"N-glycosylation of the mammalian dipeptidyl aminopeptidase-like protein 10 (DPP10) regulates trafficking and interaction with Kv4 channels."
Cotella D., Radicke S., Cipriani V., Cavaletto M., Merlin S., Follenzi A., Ravens U., Wettwer E., Santoro C., Sblattero D.
Int. J. Biochem. Cell Biol. 44:876-885(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-90; ASN-111; ASN-119; ASN-257; ASN-342 AND ASN-748, MUTAGENESIS OF ASN-257.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY387785 mRNA. Translation: AAQ91190.1.
AY172661 mRNA. Translation: AAO17263.2.
AB040925 mRNA. Translation: BAA96016.2. Different initiation.
DQ857322 mRNA. Translation: ABI16086.1.
AK289967 mRNA. Translation: BAF82656.1.
AC010885 Genomic DNA. No translation available.
AC012071 Genomic DNA. No translation available.
AC016721 Genomic DNA. Translation: AAY15025.1.
AC017040 Genomic DNA. Translation: AAY15032.1.
AC066593 Genomic DNA. No translation available.
AC067947 Genomic DNA. Translation: AAY14685.1.
AC068542 Genomic DNA. No translation available.
AC093610 Genomic DNA. No translation available.
AC105422 Genomic DNA. Translation: AAY24120.1.
AC116620 Genomic DNA. No translation available.
AC118276 Genomic DNA. No translation available.
AC118664 Genomic DNA. No translation available.
BC030832 mRNA. Translation: AAH30832.1.
CCDSCCDS33278.1. [Q8N608-2]
CCDS46400.1. [Q8N608-1]
CCDS54388.1. [Q8N608-3]
CCDS54389.1. [Q8N608-4]
RefSeqNP_001004360.2. NM_001004360.3.
NP_001171505.1. NM_001178034.1.
NP_065919.2. NM_020868.3.
UniGeneHs.580539.

3D structure databases

ProteinModelPortalQ8N608.
SMRQ8N608. Positions 66-782.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121672. 4 interactions.
IntActQ8N608. 1 interaction.
STRING9606.ENSP00000386565.

Protein family/group databases

MEROPSS09.974.

PTM databases

PhosphoSiteQ8N608.

Polymorphism databases

DMDM296434483.

Proteomic databases

MaxQBQ8N608.
PaxDbQ8N608.
PRIDEQ8N608.

Protocols and materials databases

DNASU57628.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310323; ENSP00000309066; ENSG00000175497. [Q8N608-2]
ENST00000393147; ENSP00000376855; ENSG00000175497. [Q8N608-3]
ENST00000409163; ENSP00000387038; ENSG00000175497. [Q8N608-4]
ENST00000410059; ENSP00000386565; ENSG00000175497. [Q8N608-1]
GeneID57628.
KEGGhsa:57628.
UCSCuc002tle.3. human. [Q8N608-3]

Organism-specific databases

CTD57628.
GeneCardsGC02P115295.
HGNCHGNC:20823. DPP10.
HPAHPA048767.
MIM600807. phenotype.
608209. gene.
neXtProtNX_Q8N608.
PharmGKBPA134991647.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1506.
HOVERGENHBG105877.
OMANWEVIKI.
OrthoDBEOG7H791M.
PhylomeDBQ8N608.
TreeFamTF313309.

Gene expression databases

ArrayExpressQ8N608.
BgeeQ8N608.
CleanExHS_DPP10.
GenevestigatorQ8N608.

Family and domain databases

Gene3D2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

ChiTaRSDPP10. human.
GeneWikiDPP10.
GenomeRNAi57628.
NextBio35535176.
PROQ8N608.
SOURCESearch...

Entry information

Entry nameDPP10_HUMAN
AccessionPrimary (citable) accession number: Q8N608
Secondary accession number(s): A8K1Q2 expand/collapse secondary AC list , J3KPP2, J3KQ46, Q0GLB8, Q53QT3, Q53S86, Q53SL8, Q53SS4, Q6TTV4, Q86YR9, Q9P236
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 109 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

Peptidase families

Classification of peptidase families and list of entries

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 2

Human chromosome 2: entries, gene names and cross-references to MIM