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P24158

- PRTN3_HUMAN

UniProt

P24158 - PRTN3_HUMAN

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Protein

Myeloblastin

Gene
PRTN3, MBN
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Polymorphonuclear leukocyte serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) and causes emphysema when administered by tracheal insufflation to hamsters.

Catalytic activityi

Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-|-Xaa- > -Val-|-Xaa-.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711Charge relay system
Active sitei118 – 1181Charge relay system
Active sitei203 – 2031Charge relay system

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. serine-type endopeptidase activity Source: InterPro
  3. serine-type peptidase activity Source: ProtInc

GO - Biological processi

  1. collagen catabolic process Source: UniProtKB-KW
  2. mature dendritic cell differentiation Source: UniProtKB
  3. negative regulation of phagocytosis Source: UniProtKB
  4. positive regulation of cell proliferation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Collagen degradation

Enzyme and pathway databases

BRENDAi3.4.21.76. 2681.

Protein family/group databases

MEROPSiS01.134.

Names & Taxonomyi

Protein namesi
Recommended name:
Myeloblastin (EC:3.4.21.76)
Alternative name(s):
AGP7
C-ANCA antigen
Leukocyte proteinase 3
Short name:
PR-3
Short name:
PR3
Neutrophil proteinase 4
Short name:
NP-4
P29
Wegener autoantigen
Gene namesi
Name:PRTN3
Synonyms:MBN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9495. PRTN3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular space Source: UniProt
  3. extracellular vesicular exosome Source: UniProt
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

Orphaneti900. Granulomatosis with polyangiitis.
PharmGKBiPA33842.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Add
BLAST
Propeptidei26 – 272PRO_0000027707
Chaini28 – 248221MyeloblastinPRO_0000027708Add
BLAST
Propeptidei249 – 2568PRO_0000027709

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 72
Glycosylationi129 – 1291N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi152 ↔ 209
Glycosylationi174 – 1741N-linked (GlcNAc...)
Disulfide bondi182 ↔ 188
Disulfide bondi199 ↔ 224

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP24158.
PeptideAtlasiP24158.
PRIDEiP24158.

Expressioni

Gene expression databases

BgeeiP24158.
CleanExiHS_PRTN3.
GenevestigatoriP24158.

Organism-specific databases

HPAiCAB017558.
HPA005938.

Interactioni

Protein-protein interaction databases

BioGridi111638. 6 interactions.
IntActiP24158. 2 interactions.
MINTiMINT-4054660.

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 476
Beta strandi56 – 627
Beta strandi65 – 684
Helixi70 – 734
Beta strandi74 – 763
Helixi78 – 803
Beta strandi81 – 866
Beta strandi98 – 10710
Turni112 – 1154
Beta strandi120 – 1267
Beta strandi151 – 16010
Beta strandi162 – 1643
Beta strandi171 – 1788
Beta strandi186 – 1905
Beta strandi192 – 1954
Beta strandi206 – 2094
Beta strandi212 – 2198
Beta strandi221 – 2233
Beta strandi227 – 2293
Beta strandi231 – 2355
Helixi236 – 2394
Helixi240 – 2478

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FUJX-ray2.20A/B/C/D28-248[»]
ProteinModelPortaliP24158.
SMRiP24158. Positions 28-248.

Miscellaneous databases

EvolutionaryTraceiP24158.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 248221Peptidase S1Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
HOVERGENiHBG013304.
InParanoidiP24158.
KOiK01350.
OMAiHFSVAQV.
OrthoDBiEOG7MKW6Q.
PhylomeDBiP24158.
TreeFamiTF335284.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P24158-1 [UniParc]FASTAAdd to Basket

« Hide

MAHRPPSPAL ASVLLALLLS GAARAAEIVG GHEAQPHSRP YMASLQMRGN    50
PGSHFCGGTL IHPSFVLTAA HCLRDIPQRL VNVVLGAHNV RTQEPTQQHF 100
SVAQVFLNNY DAENKLNDVL LIQLSSPANL SASVATVQLP QQDQPVPHGT 150
QCLAMGWGRV GAHDPPAQVL QELNVTVVTF FCRPHNICTF VPRRKAGICF 200
GDSGGPLICD GIIQGIDSFV IWGCATRLFP DFFTRVALYV DWIRSTLRRV 250
EAKGRP 256
Length:256
Mass (Da):27,807
Last modified:December 15, 1998 - v3
Checksum:iCBECA36D8C4B2A40
GO

Sequence cautioni

The sequence AAA36342.1 differs from that shown. Reason: Frameshift at positions 34 and 39.
The sequence CAA39598.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191V → I.7 Publications
Corresponds to variant rs351111 [ dbSNP | Ensembl ].
VAR_011691
Natural varianti135 – 1351A → T.4 Publications
Corresponds to variant rs1042281 [ dbSNP | Ensembl ].
VAR_011713
Natural varianti136 – 1361T → S.4 Publications
Corresponds to variant rs1042282 [ dbSNP | Ensembl ].
VAR_011714

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → R in CAA39203. 1 Publication
Sequence conflicti38 – 381S → I AA sequence 1 Publication
Sequence conflicti40 – 401P → PI AA sequence 1 Publication
Sequence conflicti46 – 461Q → E AA sequence 1 Publication
Sequence conflicti46 – 461Q → E AA sequence 1 Publication
Sequence conflicti48 – 481R → A AA sequence 1 Publication
Sequence conflicti64 – 641S → D AA sequence 1 Publication
Sequence conflicti70 – 701A → P in AAA59558. 1 Publication
Sequence conflicti255 – 2551Missing in CAA39203. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M75154 mRNA. Translation: AAA59558.1.
AC004799 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69591.1.
BC096183 mRNA. Translation: AAH96183.1.
BC096184 mRNA. Translation: AAH96184.1.
BC096185 mRNA. Translation: AAH96185.1.
BC096186 mRNA. Translation: AAH96186.1.
M96628 Genomic DNA. Translation: AAB59364.1.
AH005293 Genomic DNA. Translation: AAB59493.1.
M97911 Genomic DNA. No translation available.
AH007523 Genomic DNA. Translation: AAD21524.1.
X56606 mRNA. Translation: CAA39943.1.
X55668 mRNA. Translation: CAA39203.1.
M29142 mRNA. Translation: AAA36342.1. Frameshift.
X56132 mRNA. Translation: CAA39597.1.
X56132 mRNA. Translation: CAA39598.1. Different initiation.
CCDSiCCDS32860.1.
PIRiA45080. PRHU3.
RefSeqiNP_002768.3. NM_002777.3.
UniGeneiHs.928.

Genome annotation databases

EnsembliENST00000234347; ENSP00000234347; ENSG00000196415.
GeneIDi5657.
KEGGihsa:5657.
UCSCiuc002lqa.1. human.

Polymorphism databases

DMDMi6174926.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Proteinase 3 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M75154 mRNA. Translation: AAA59558.1 .
AC004799 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69591.1 .
BC096183 mRNA. Translation: AAH96183.1 .
BC096184 mRNA. Translation: AAH96184.1 .
BC096185 mRNA. Translation: AAH96185.1 .
BC096186 mRNA. Translation: AAH96186.1 .
M96628 Genomic DNA. Translation: AAB59364.1 .
AH005293 Genomic DNA. Translation: AAB59493.1 .
M97911 Genomic DNA. No translation available.
AH007523 Genomic DNA. Translation: AAD21524.1 .
X56606 mRNA. Translation: CAA39943.1 .
X55668 mRNA. Translation: CAA39203.1 .
M29142 mRNA. Translation: AAA36342.1 . Frameshift.
X56132 mRNA. Translation: CAA39597.1 .
X56132 mRNA. Translation: CAA39598.1 . Different initiation.
CCDSi CCDS32860.1.
PIRi A45080. PRHU3.
RefSeqi NP_002768.3. NM_002777.3.
UniGenei Hs.928.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FUJ X-ray 2.20 A/B/C/D 28-248 [» ]
ProteinModelPortali P24158.
SMRi P24158. Positions 28-248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111638. 6 interactions.
IntActi P24158. 2 interactions.
MINTi MINT-4054660.

Chemistry

BindingDBi P24158.
ChEMBLi CHEMBL3900.

Protein family/group databases

MEROPSi S01.134.

Polymorphism databases

DMDMi 6174926.

Proteomic databases

PaxDbi P24158.
PeptideAtlasi P24158.
PRIDEi P24158.

Protocols and materials databases

DNASUi 5657.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000234347 ; ENSP00000234347 ; ENSG00000196415 .
GeneIDi 5657.
KEGGi hsa:5657.
UCSCi uc002lqa.1. human.

Organism-specific databases

CTDi 5657.
GeneCardsi GC19P000840.
HGNCi HGNC:9495. PRTN3.
HPAi CAB017558.
HPA005938.
MIMi 177020. gene.
neXtProti NX_P24158.
Orphaneti 900. Granulomatosis with polyangiitis.
PharmGKBi PA33842.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOVERGENi HBG013304.
InParanoidi P24158.
KOi K01350.
OMAi HFSVAQV.
OrthoDBi EOG7MKW6Q.
PhylomeDBi P24158.
TreeFami TF335284.

Enzyme and pathway databases

BRENDAi 3.4.21.76. 2681.

Miscellaneous databases

EvolutionaryTracei P24158.
GeneWikii Proteinase_3.
GenomeRNAii 5657.
NextBioi 21988.
PROi P24158.
SOURCEi Search...

Gene expression databases

Bgeei P24158.
CleanExi HS_PRTN3.
Genevestigatori P24158.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Wegener autoantigen and myeloblastin are encoded by a single mRNA."
    Labbaye C., Musette P., Cayre Y.E.
    Proc. Natl. Acad. Sci. U.S.A. 88:9253-9256(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-119; THR-135 AND SER-136.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-119.
  4. "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], VARIANT ILE-119.
  5. "Three human elastase-like genes coordinately expressed in the myelomonocyte lineage are organized as a single genetic locus on 19pter."
    Zimmer M., Medcalf R.L., Fink T.M., Mattmann C., Lichter P., Jenne D.E.
    Proc. Natl. Acad. Sci. U.S.A. 89:8215-8219(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20 AND 22-256.
  6. "Structure, chromosomal assignment, and expression of the gene for proteinase-3. The Wegener's granulomatosis autoantigen."
    Sturrock A.B., Franklin K.F., Rao G., Marshall B.C., Rebentisch M.B., Lemons R.S., Hoidal J.R.
    J. Biol. Chem. 267:21193-21199(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-254, VARIANTS THR-135 AND SER-136.
  7. "Donor-recipient polymorphism of the proteinase 3 gene: a potential target for T-cell alloresponses to myeloid leukemia."
    Clave E., Molldrem J., Hensel N., Raptis A., Barrett A.J.
    J. Immunother. 22:1-6(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200, VARIANT ILE-119.
  8. "Wegener's autoantigen and leukemia."
    Musette P., Labbaye C., Dorner M.H., Cayre Y.E., Casanova J.-L., Kourilsky P.
    Blood 77:1398-1399(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-42.
  9. "Cloning of cDNA for proteinase 3: a serine protease, antibiotic, and autoantigen from human neutrophils."
    Campanelli D., Melchior M., Fu Y., Nakata M., Shuman H., Nathan C., Gabay J.E.
    J. Exp. Med. 172:1709-1715(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-256, PROTEIN SEQUENCE OF 28-71; 156-181 AND 196-219.
  10. "Down-regulation of a serine protease, myeloblastin, causes growth arrest and differentiation of promyelocytic leukemia cells."
    Bories D., Raynal M.-C., Solomon D.H., Darzynkiewicz Z., Cayre Y.E.
    Cell 59:959-968(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-256, VARIANTS ILE-119; THR-135 AND SER-136.
  11. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-256, PROTEIN SEQUENCE OF 28-48, VARIANTS ILE-119; THR-135 AND SER-136, IDENTITY OF WEGENER'S AUTOANTIGEN WITH PR-3.
  12. "Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties."
    Rao N.V., Wehner N.G., Marshall B.C., Gray W.R., Gray B.H., Hoidal J.R.
    J. Biol. Chem. 266:9540-9548(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-67 AND 228-244.
  13. "Characterization of two azurphil granule proteases with active-site homology to neutrophil elastase."
    Wilde C.G., Snable J.L., Griffith J.E., Scott R.W.
    J. Biol. Chem. 265:2038-2041(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-47 AND 196-219.
  14. "Monoclonal antibodies specific for neutrophil proteinase 4. Production and use for isolation of the enzyme."
    Ohlsson K., Linder C., Rosengren M.
    Biol. Chem. Hoppe-Seyler 371:549-555(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-52.
  15. "The relation of 29 kD C-ANCA antigen to proteinase 3."
    Goldschmeding R., Dolman K.M., van den Ende M.E., van der Meer-Gerritsen C.H., Sonnenberg A., von dem Borne A.E.
    APMIS Suppl. 19:26-27(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-48.
  16. "Wegener's granulomatosis autoantigen is a novel neutrophil serine proteinase."
    Niles J.L., McCluskey R.T., Ahmad M.F., Arnaout M.A.
    Blood 74:1888-1893(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-47.
  17. Cited for: PROTEIN SEQUENCE OF 28-47.
  18. "Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis."
    Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.
    J. Immunol. Methods 180:25-33(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-47, CATALYTIC ACTIVITY.
    Tissue: Neutrophil.
  19. "Anti-neutrophil cytoplasm antibodies in Wegener's granulomatosis recognize an elastinolytic enzyme."
    Ludemann J., Utecht B., Gross W.L.
    J. Exp. Med. 171:357-362(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-43.
  20. "A novel form of dipeptidylpeptidase IV found in human serum. Isolation, characterization, and comparison with T lymphocyte membrane dipeptidylpeptidase IV (CD26)."
    Duke-Cohan J.S., Morimoto C., Rocker J.A., Schlossman S.F.
    J. Biol. Chem. 270:14107-14114(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 110-121, VARIANT ILE-119.
    Tissue: Serum.
  21. "Identity of Wegener's autoantigen (p29) with proteinase 3 and myeloblastin."
    Gupta S.K., Niles J.L., McCluskey R.T., Arnaout M.A.
    Blood 76:2162-2162(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTITY OF WEGENER'S AUTOANTIGEN WITH PROTEINASE 3.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies."
    Fujinaga M., Charnaia M.M., Halenbeck R., Koths K., James M.N.G.
    J. Mol. Biol. 261:267-278(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiPRTN3_HUMAN
AccessioniPrimary (citable) accession number: P24158
Secondary accession number(s): P15637
, P18078, Q4VB08, Q4VB09, Q6LBM7, Q6LBN2, Q9UD25, Q9UQD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: December 15, 1998
Last modified: September 3, 2014
This is version 160 of the entry and version 3 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi