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O14638

- ENPP3_HUMAN

UniProt

O14638 - ENPP3_HUMAN

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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

Gene

ENPP3

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

Functioni

Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD.By similarity

Catalytic activityi

Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
A dinucleotide + H2O = 2 mononucleotides.

Cofactori

Binds 2 divalent metal cations per subunit.Curated

Enzyme regulationi

At low concentrations of ATP, a phosphorylated active site intermediate is formed which inhibits further ATP hydrolysis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi167 – 1671Zinc 1; catalyticBy similarity
Active sitei205 – 2051AMP-threonine intermediateBy similarity
Metal bindingi205 – 2051Zinc 1; catalyticBy similarity
Binding sitei226 – 2261SubstrateBy similarity
Binding sitei320 – 3201SubstrateBy similarity
Metal bindingi325 – 3251Zinc 2; catalyticBy similarity
Metal bindingi329 – 3291Zinc 2; via tele nitrogen; catalyticBy similarity
Metal bindingi372 – 3721Zinc 1; catalyticBy similarity
Metal bindingi373 – 3731Zinc 1; via tele nitrogen; catalyticBy similarity
Metal bindingi483 – 4831Zinc 2; via tele nitrogen; catalyticBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. NADH pyrophosphatase activity Source: UniProtKB-EC
  3. nucleic acid binding Source: InterPro
  4. nucleoside-triphosphate diphosphatase activity Source: BHF-UCL
  5. nucleotide diphosphatase activity Source: ProtInc
  6. phosphodiesterase I activity Source: ProtInc
  7. polysaccharide binding Source: InterPro
  8. scavenger receptor activity Source: InterPro

GO - Biological processi

  1. immune response Source: InterPro
  2. nucleic acid phosphodiester bond hydrolysis Source: GOC
  3. nucleoside triphosphate catabolic process Source: BHF-UCL
  4. phosphate-containing compound metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Short name:
E-NPP 3
Alternative name(s):
Phosphodiesterase I beta
Short name:
PD-Ibeta
Phosphodiesterase I/nucleotide pyrophosphatase 3
CD_antigen: CD203c
Including the following 2 domains:
Alkaline phosphodiesterase I (EC:3.1.4.1)
Nucleotide pyrophosphatase (EC:3.6.1.9)
Short name:
NPPase
Gene namesi
Name:ENPP3
Synonyms:PDNP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:3358. ENPP3.

Subcellular locationi

Membrane Curated; Single-pass type II membrane protein Curated. Secreted 2 Publications
Note: Located to the apical surface in intestinal and kidney epithelial cells. Located to the cell surface of basophils, and to the apical plasma membrane of bile duct cells. Secreted in serum, and in lumen of epithelial cells.

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. integral component of plasma membrane Source: ProtInc
  3. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27793.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 875875Ectonucleotide pyrophosphatase/phosphodiesterase family member 3PRO_0000188570Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 71PROSITE-ProRule annotation
Disulfide bondi58 ↔ 89PROSITE-ProRule annotation
Disulfide bondi69 ↔ 82PROSITE-ProRule annotation
Disulfide bondi75 ↔ 81PROSITE-ProRule annotation
Disulfide bondi98 ↔ 115PROSITE-ProRule annotation
Disulfide bondi103 ↔ 133PROSITE-ProRule annotation
Disulfide bondi113 ↔ 126PROSITE-ProRule annotation
Disulfide bondi119 ↔ 125PROSITE-ProRule annotation
Disulfide bondi144 ↔ 190PROSITE-ProRule annotation
Disulfide bondi152 ↔ 364PROSITE-ProRule annotation
Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi380 ↔ 478PROSITE-ProRule annotation
Glycosylationi426 – 4261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi429 ↔ 818PROSITE-ProRule annotation
Glycosylationi533 – 5331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi575 ↔ 679PROSITE-ProRule annotation
Disulfide bondi577 ↔ 664PROSITE-ProRule annotation
Glycosylationi582 – 5821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi594 – 5941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi687 – 6871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi699 – 6991N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi787 ↔ 797PROSITE-ProRule annotation
Glycosylationi789 – 7891N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylation is necessary for correct trafficking to the apical surface, but is not the apical targeting signal.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO14638.
PaxDbiO14638.
PRIDEiO14638.

PTM databases

PhosphoSiteiO14638.

Expressioni

Tissue specificityi

Expressed in bile ducts, prostate, uterus and colon. Exclusively expressed on basophils, mast cells and their progenitors.2 Publications

Inductioni

Up-regulated by stimulation by allergen or by cross-linking with IgE. The IgE-mediated activation is enhanced by tetradecanoyl phorbol acetate (TPA), a stimulator of the PKC pathway, and inhibited by the P13 kinase inhibitors, LY294002 and wortmannin. Up-regulated in invasive bile duct cancers.1 Publication

Gene expression databases

BgeeiO14638.
CleanExiHS_ENPP3.
ExpressionAtlasiO14638. baseline and differential.
GenevestigatoriO14638.

Organism-specific databases

HPAiHPA043772.

Interactioni

Protein-protein interaction databases

BioGridi111195. 2 interactions.
IntActiO14638. 1 interaction.
MINTiMINT-6610326.
STRINGi9606.ENSP00000350265.

Structurei

3D structure databases

ProteinModelPortaliO14638.
SMRiO14638. Positions 52-872.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini31 – 875845ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3019Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 9344SMB 1PROSITE-ProRule annotationAdd
BLAST
Domaini94 – 13845SMB 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni140 – 510371PhosphodiesteraseAdd
BLAST
Regioni605 – 875271NucleaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi78 – 803Cell attachment siteSequence Analysis

Sequence similaritiesi

Contains 2 SMB (somatomedin-B) domains.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1524.
GeneTreeiENSGT00760000119157.
HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiO14638.
KOiK01513.
OMAiTSDSQYD.
OrthoDBiEOG7XM2X4.
PhylomeDBiO14638.
TreeFamiTF330032.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PfamiPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14638-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESTLTLATE QPVKKNTLKK YKIACIVLLA LLVIMSLGLG LGLGLRKLEK
60 70 80 90 100
QGSCRKKCFD ASFRGLENCR CDVACKDRGD CCWDFEDTCV ESTRIWMCNK
110 120 130 140 150
FRCGETRLEA SLCSCSDDCL QRKDCCADYK SVCQGETSWL EENCDTAQQS
160 170 180 190 200
QCPEGFDLPP VILFSMDGFR AEYLYTWDTL MPNINKLKTC GIHSKYMRAM
210 220 230 240 250
YPTKTFPNHY TIVTGLYPES HGIIDNNMYD VNLNKNFSLS SKEQNNPAWW
260 270 280 290 300
HGQPMWLTAM YQGLKAATYF WPGSEVAING SFPSIYMPYN GSVPFEERIS
310 320 330 340 350
TLLKWLDLPK AERPRFYTMY FEEPDSSGHA GGPVSARVIK ALQVVDHAFG
360 370 380 390 400
MLMEGLKQRN LHNCVNIILL ADHGMDQTYC NKMEYMTDYF PRINFFYMYE
410 420 430 440 450
GPAPRIRAHN IPHDFFSFNS EEIVRNLSCR KPDQHFKPYL TPDLPKRLHY
460 470 480 490 500
AKNVRIDKVH LFVDQQWLAV RSKSNTNCGG GNHGYNNEFR SMEAIFLAHG
510 520 530 540 550
PSFKEKTEVE PFENIEVYNL MCDLLRIQPA PNNGTHGSLN HLLKVPFYEP
560 570 580 590 600
SHAEEVSKFS VCGFANPLPT ESLDCFCPHL QNSTQLEQVN QMLNLTQEEI
610 620 630 640 650
TATVKVNLPF GRPRVLQKNV DHCLLYHREY VSGFGKAMRM PMWSSYTVPQ
660 670 680 690 700
LGDTSPLPPT VPDCLRADVR VPPSESQKCS FYLADKNITH GFLYPPASNR
710 720 730 740 750
TSDSQYDALI TSNLVPMYEE FRKMWDYFHS VLLIKHATER NGVNVVSGPI
760 770 780 790 800
FDYNYDGHFD APDEITKHLA NTDVPIPTHY FVVLTSCKNK SHTPENCPGW
810 820 830 840 850
LDVLPFIIPH RPTNVESCPE GKPEALWVEE RFTAHIARVR DVELLTGLDF
860 870
YQDKVQPVSE ILQLKTYLPT FETTI
Length:875
Mass (Da):100,124
Last modified:September 23, 2008 - v2
Checksum:i629D2E33B4C45196
GO

Sequence cautioni

The sequence AAD05192.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221R → K in AAC51813. (PubMed:9344668)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti620 – 6201V → M.
Corresponds to variant rs9321309 [ dbSNP | Ensembl ].
VAR_018516
Natural varianti744 – 7441N → H.
Corresponds to variant rs36094194 [ dbSNP | Ensembl ].
VAR_046538
Natural varianti786 – 7861S → N.
Corresponds to variant rs17601580 [ dbSNP | Ensembl ].
VAR_031253

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF005632 mRNA. Translation: AAC51813.1.
EF560735 mRNA. Translation: ABQ59045.1.
AC005587 Genomic DNA. Translation: AAD05192.1. Sequence problems.
AL121575, AC005587, AL355150 Genomic DNA. Translation: CAI23322.1.
AL355150, AC005587, AL121575 Genomic DNA. Translation: CAI40481.1.
CH471051 Genomic DNA. Translation: EAW48045.1.
CCDSiCCDS5148.1.
RefSeqiNP_005012.2. NM_005021.3.
UniGeneiHs.486489.

Genome annotation databases

EnsembliENST00000357639; ENSP00000350265; ENSG00000154269.
ENST00000414305; ENSP00000406261; ENSG00000154269.
GeneIDi5169.
KEGGihsa:5169.
UCSCiuc003qcu.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF005632 mRNA. Translation: AAC51813.1 .
EF560735 mRNA. Translation: ABQ59045.1 .
AC005587 Genomic DNA. Translation: AAD05192.1 . Sequence problems.
AL121575 , AC005587 , AL355150 Genomic DNA. Translation: CAI23322.1 .
AL355150 , AC005587 , AL121575 Genomic DNA. Translation: CAI40481.1 .
CH471051 Genomic DNA. Translation: EAW48045.1 .
CCDSi CCDS5148.1.
RefSeqi NP_005012.2. NM_005021.3.
UniGenei Hs.486489.

3D structure databases

ProteinModelPortali O14638.
SMRi O14638. Positions 52-872.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111195. 2 interactions.
IntActi O14638. 1 interaction.
MINTi MINT-6610326.
STRINGi 9606.ENSP00000350265.

Chemistry

ChEMBLi CHEMBL5580.

PTM databases

PhosphoSitei O14638.

Proteomic databases

MaxQBi O14638.
PaxDbi O14638.
PRIDEi O14638.

Protocols and materials databases

DNASUi 5169.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357639 ; ENSP00000350265 ; ENSG00000154269 .
ENST00000414305 ; ENSP00000406261 ; ENSG00000154269 .
GeneIDi 5169.
KEGGi hsa:5169.
UCSCi uc003qcu.4. human.

Organism-specific databases

CTDi 5169.
GeneCardsi GC06P131949.
HGNCi HGNC:3358. ENPP3.
HPAi HPA043772.
MIMi 602182. gene.
neXtProti NX_O14638.
PharmGKBi PA27793.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1524.
GeneTreei ENSGT00760000119157.
HOGENOMi HOG000037439.
HOVERGENi HBG051484.
InParanoidi O14638.
KOi K01513.
OMAi TSDSQYD.
OrthoDBi EOG7XM2X4.
PhylomeDBi O14638.
TreeFami TF330032.

Miscellaneous databases

GeneWikii ENPP3.
GenomeRNAii 5169.
NextBioi 20000.
PROi O14638.
SOURCEi Search...

Gene expression databases

Bgeei O14638.
CleanExi HS_ENPP3.
ExpressionAtlasi O14638. baseline and differential.
Genevestigatori O14638.

Family and domain databases

Gene3Di 3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR001212. Somatomedin_B_dom.
[Graphical view ]
PANTHERi PTHR10151. PTHR10151. 1 hit.
Pfami PF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view ]
SMARTi SM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 1 hit.
PROSITEi PS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes."
    Piao J.-H., Goding J.W., Nakamura H., Sano K.
    Genomics 45:412-415(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Prostate.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Endometrium.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3."
    Buehring H.J., Seiffert M., Giesert C., Marxer A., Kanz L., Valent P., Sano K.
    Blood 97:3303-3305(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 393-405, IDENTIFICATION AS CD203C, SUBCELLULAR LOCATION.
  6. "Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases."
    Yano Y., Hayashi Y., Sano K., Nagano H., Nakaji M., Seo Y., Ninomiya T., Yoon S., Yokozaki H., Kasuga M.
    Cancer Lett. 207:139-147(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "The basophil-specific ectoenzyme E-NPP3 (CD203c) as a marker for cell activation and allergy diagnosis."
    Buehring H.J., Streble A., Valent P.
    Int. Arch. Allergy Immunol. 133:317-329(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, POSSIBLE APPLICATION IN ALLERGY DIAGNOSIS.

Entry informationi

Entry nameiENPP3_HUMAN
AccessioniPrimary (citable) accession number: O14638
Secondary accession number(s): Q5JTL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 23, 2008
Last modified: October 29, 2014
This is version 131 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, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3