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P10153

- RNAS2_HUMAN

UniProt

P10153 - RNAS2_HUMAN

Protein

Non-secretory ribonuclease

Gene

RNASE2

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

    This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities.2 Publications

    Catalytic activityi

    Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei42 – 421Proton acceptor
    Active sitei156 – 1561Proton donor

    GO - Molecular functioni

    1. nucleic acid binding Source: InterPro
    2. pancreatic ribonuclease activity Source: UniProtKB-EC
    3. ribonuclease activity Source: ProtInc

    GO - Biological processi

    1. chemotaxis Source: UniProtKB
    2. RNA catabolic process Source: ProtInc
    3. RNA phosphodiester bond hydrolysis Source: GOC

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    Chemotaxis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Non-secretory ribonuclease (EC:3.1.27.5)
    Alternative name(s):
    Eosinophil-derived neurotoxin
    RNase UpI-2
    Ribonuclease 2
    Short name:
    RNase 2
    Ribonuclease US
    Gene namesi
    Name:RNASE2
    Synonyms:EDN, RNS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:10045. RNASE2.

    Subcellular locationi

    Lysosome Curated. Cytoplasmic granule
    Note: Matrix of eosinophil's large specific granule.

    GO - Cellular componenti

    1. extracellular region Source: ProtInc
    2. extracellular vesicular exosome Source: UniProt
    3. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34413.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27275 PublicationsAdd
    BLAST
    Chaini28 – 161134Non-secretory ribonucleasePRO_0000030874Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi34 – 341C-linked (Man)CAR_000004
    Glycosylationi44 – 441N-linked (GlcNAc...)
    Disulfide bondi50 ↔ 110
    Modified residuei60 – 601Nitrated tyrosine1 Publication
    Disulfide bondi64 ↔ 123
    Disulfide bondi82 ↔ 138
    Glycosylationi86 – 861N-linked (GlcNAc...)
    Disulfide bondi89 ↔ 98
    Glycosylationi92 – 921N-linked (GlcNAc...)
    Glycosylationi111 – 1111N-linked (GlcNAc...)
    Glycosylationi119 – 1191N-linked (GlcNAc...)

    Post-translational modificationi

    A particular signal processing and glycosylation pattern may differentiate the UpI2 RNase, found specifically in pregnant women urine, from other nonsecretory RNases.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Nitration

    Proteomic databases

    PaxDbiP10153.
    PeptideAtlasiP10153.
    PRIDEiP10153.

    PTM databases

    PhosphoSiteiP10153.
    UniCarbKBiP10153.

    Expressioni

    Tissue specificityi

    Liver, lung, spleen, leukocytes and body fluids.

    Gene expression databases

    BgeeiP10153.
    CleanExiHS_RNASE2.
    GenevestigatoriP10153.

    Organism-specific databases

    HPAiHPA044983.

    Interactioni

    Subunit structurei

    Interacts with and forms a tight 1:1 complex with RNH1. Dimerization of two such complexes may occur.3 Publications

    Protein-protein interaction databases

    BioGridi111965. 1 interaction.
    STRINGi9606.ENSP00000303276.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi34 – 429
    Beta strandi46 – 494
    Helixi50 – 6112
    Beta strandi66 – 738
    Helixi75 – 828
    Beta strandi98 – 1003
    Beta strandi105 – 11410
    Helixi120 – 1223
    Beta strandi124 – 14017
    Turni143 – 1453
    Beta strandi151 – 16111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GQVX-ray0.98A28-161[»]
    1HI2X-ray1.60A28-161[»]
    1HI3X-ray1.80A28-161[»]
    1HI4X-ray1.80A28-161[»]
    1HI5X-ray1.80A28-161[»]
    1K2AX-ray1.00A26-160[»]
    2BEXX-ray1.99C/D28-161[»]
    2BZZX-ray0.98A28-161[»]
    2C01X-ray1.24X28-161[»]
    2C02X-ray2.00A28-161[»]
    2C05X-ray1.86A28-161[»]
    ProteinModelPortaliP10153.
    SMRiP10153. Positions 26-161.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10153.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni65 – 695Substrate binding

    Domaini

    The N-terminal region is necessary for mediating chemotactic activity.

    Sequence similaritiesi

    Belongs to the pancreatic ribonuclease family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG39501.
    HOGENOMiHOG000276882.
    HOVERGENiHBG008396.
    InParanoidiP10153.
    KOiK01168.
    OMAiRDPPQYP.
    OrthoDBiEOG7KDFCP.
    PhylomeDBiP10153.
    TreeFamiTF333393.

    Family and domain databases

    Gene3Di3.10.130.10. 1 hit.
    InterProiIPR001427. RNaseA.
    IPR023411. RNaseA_AS.
    IPR023412. RNaseA_domain.
    [Graphical view]
    PANTHERiPTHR11437. PTHR11437. 1 hit.
    PfamiPF00074. RnaseA. 1 hit.
    [Graphical view]
    PRINTSiPR00794. RIBONUCLEASE.
    ProDomiPD000535. RNaseA. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00092. RNAse_Pc. 1 hit.
    [Graphical view]
    SUPFAMiSSF54076. SSF54076. 1 hit.
    PROSITEiPS00127. RNASE_PANCREATIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10153-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVPKLFTSQI CLLLLLGLLA VEGSLHVKPP QFTWAQWFET QHINMTSQQC    50
    TNAMQVINNY QRRCKNQNTF LLTTFANVVN VCGNPNMTCP SNKTRKNCHH 100
    SGSQVPLIHC NLTTPSPQNI SNCRYAQTPA NMFYIVACDN RDQRRDPPQY 150
    PVVPVHLDRI I 161
    Length:161
    Mass (Da):18,354
    Last modified:January 1, 1990 - v2
    Checksum:i9406C4596CA69038
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371W → R AA sequence (PubMed:3926759)Curated
    Sequence conflicti39 – 402ET → QE AA sequence (PubMed:3926759)Curated
    Sequence conflicti46 – 461T → V AA sequence (PubMed:3926759)Curated
    Sequence conflicti47 – 471S → T AA sequence (PubMed:3182786)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti100 – 1001H → Q.
    Corresponds to variant rs8012891 [ dbSNP | Ensembl ].
    VAR_059820
    Natural varianti156 – 1561H → N Probably inactive. 1 Publication
    Corresponds to variant rs146887874 [ dbSNP | Ensembl ].
    VAR_013150

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30510 mRNA. Translation: AAC82505.1.
    M28129 mRNA. Translation: AAA50284.1.
    M24157 mRNA. Translation: AAA52337.1.
    X16546 Genomic DNA. Translation: CAA34546.1.
    AF294007 Genomic DNA. Translation: AAG31577.1.
    AF294008 Genomic DNA. Translation: AAG31578.1.
    AF294009 Genomic DNA. Translation: AAG31579.1.
    AF294010 Genomic DNA. Translation: AAG31580.1.
    AF294011 Genomic DNA. Translation: AAG31581.1.
    AF294012 Genomic DNA. Translation: AAG31582.1.
    AF294013 Genomic DNA. Translation: AAG31583.1.
    AF294014 Genomic DNA. Translation: AAG31584.1.
    AF294015 Genomic DNA. Translation: AAG31585.1.
    X55987 Genomic DNA. Translation: CAA39459.1.
    X55988 mRNA. Translation: CAA39460.1.
    BC093678 mRNA. Translation: AAH93678.1.
    BC093680 mRNA. Translation: AAH93680.1.
    BC096059 mRNA. Translation: AAH96059.1.
    CCDSiCCDS9561.1.
    PIRiA35328. A33922.
    RefSeqiNP_002925.1. NM_002934.2.
    UniGeneiHs.728.

    Genome annotation databases

    EnsembliENST00000304625; ENSP00000303276; ENSG00000169385.
    GeneIDi6036.
    KEGGihsa:6036.
    UCSCiuc001vyl.1. human.

    Polymorphism databases

    DMDMi133168.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30510 mRNA. Translation: AAC82505.1 .
    M28129 mRNA. Translation: AAA50284.1 .
    M24157 mRNA. Translation: AAA52337.1 .
    X16546 Genomic DNA. Translation: CAA34546.1 .
    AF294007 Genomic DNA. Translation: AAG31577.1 .
    AF294008 Genomic DNA. Translation: AAG31578.1 .
    AF294009 Genomic DNA. Translation: AAG31579.1 .
    AF294010 Genomic DNA. Translation: AAG31580.1 .
    AF294011 Genomic DNA. Translation: AAG31581.1 .
    AF294012 Genomic DNA. Translation: AAG31582.1 .
    AF294013 Genomic DNA. Translation: AAG31583.1 .
    AF294014 Genomic DNA. Translation: AAG31584.1 .
    AF294015 Genomic DNA. Translation: AAG31585.1 .
    X55987 Genomic DNA. Translation: CAA39459.1 .
    X55988 mRNA. Translation: CAA39460.1 .
    BC093678 mRNA. Translation: AAH93678.1 .
    BC093680 mRNA. Translation: AAH93680.1 .
    BC096059 mRNA. Translation: AAH96059.1 .
    CCDSi CCDS9561.1.
    PIRi A35328. A33922.
    RefSeqi NP_002925.1. NM_002934.2.
    UniGenei Hs.728.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GQV X-ray 0.98 A 28-161 [» ]
    1HI2 X-ray 1.60 A 28-161 [» ]
    1HI3 X-ray 1.80 A 28-161 [» ]
    1HI4 X-ray 1.80 A 28-161 [» ]
    1HI5 X-ray 1.80 A 28-161 [» ]
    1K2A X-ray 1.00 A 26-160 [» ]
    2BEX X-ray 1.99 C/D 28-161 [» ]
    2BZZ X-ray 0.98 A 28-161 [» ]
    2C01 X-ray 1.24 X 28-161 [» ]
    2C02 X-ray 2.00 A 28-161 [» ]
    2C05 X-ray 1.86 A 28-161 [» ]
    ProteinModelPortali P10153.
    SMRi P10153. Positions 26-161.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111965. 1 interaction.
    STRINGi 9606.ENSP00000303276.

    Chemistry

    BindingDBi P10153.
    ChEMBLi CHEMBL5120.

    PTM databases

    PhosphoSitei P10153.
    UniCarbKBi P10153.

    Polymorphism databases

    DMDMi 133168.

    Proteomic databases

    PaxDbi P10153.
    PeptideAtlasi P10153.
    PRIDEi P10153.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304625 ; ENSP00000303276 ; ENSG00000169385 .
    GeneIDi 6036.
    KEGGi hsa:6036.
    UCSCi uc001vyl.1. human.

    Organism-specific databases

    CTDi 6036.
    GeneCardsi GC14P021423.
    HGNCi HGNC:10045. RNASE2.
    HPAi HPA044983.
    MIMi 131410. gene.
    neXtProti NX_P10153.
    PharmGKBi PA34413.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39501.
    HOGENOMi HOG000276882.
    HOVERGENi HBG008396.
    InParanoidi P10153.
    KOi K01168.
    OMAi RDPPQYP.
    OrthoDBi EOG7KDFCP.
    PhylomeDBi P10153.
    TreeFami TF333393.

    Miscellaneous databases

    EvolutionaryTracei P10153.
    GeneWikii Eosinophil-derived_neurotoxin.
    GenomeRNAii 6036.
    NextBioi 23525.
    PROi P10153.
    SOURCEi Search...

    Gene expression databases

    Bgeei P10153.
    CleanExi HS_RNASE2.
    Genevestigatori P10153.

    Family and domain databases

    Gene3Di 3.10.130.10. 1 hit.
    InterProi IPR001427. RNaseA.
    IPR023411. RNaseA_AS.
    IPR023412. RNaseA_domain.
    [Graphical view ]
    PANTHERi PTHR11437. PTHR11437. 1 hit.
    Pfami PF00074. RnaseA. 1 hit.
    [Graphical view ]
    PRINTSi PR00794. RIBONUCLEASE.
    ProDomi PD000535. RNaseA. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00092. RNAse_Pc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54076. SSF54076. 1 hit.
    PROSITEi PS00127. RNASE_PANCREATIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of human eosinophil-derived neurotoxin cDNA: identity of deduced amino acid sequence with human nonsecretory ribonucleases."
      Hamann K.J., Barker R.L., Loegering D.A., Pease L.R., Gleich G.J.
      Gene 83:161-167(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases."
      Barker R.L., Loegering D.A., Ten R.M., Hamann K.J., Pease L.R., Gleich G.J.
      J. Immunol. 143:952-955(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family."
      Rosenberg H.F., Tenen D.G., Ackerman S.J.
      Proc. Natl. Acad. Sci. U.S.A. 86:4460-4464(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: evidence for intronless coding sequences in the ribonuclease gene superfamily."
      Hamann K.J., Ten R.M., Loegering D.A., Jenkins R.B., Heise M.T., Schad C.R., Pease L.R., Gleich G.J., Barker R.L.
      Genomics 7:535-546(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Sequence variation at two eosinophil-associated ribonuclease loci in humans."
      Zhang J., Rosenberg H.F.
      Genetics 156:1949-1958(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-156.
    6. Simonsen C.C., Kennedy J., Comstock L., Ashton N., McGrogan M.
      Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Colon and Leukemia.
    7. "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].
    8. Cited for: PROTEIN SEQUENCE OF 28-161.
    9. "Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease."
      Gleich G.J., Loegering D.A., Bell M.P., Checkel J.L., Ackerman S.J., McKean D.J.
      Proc. Natl. Acad. Sci. U.S.A. 83:3146-3150(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-82, FUNCTION.
    10. "Purification and properties of bovine kidney ribonucleases."
      Niwata Y., Ohgi K., Sanda A., Takizawa Y., Irie M.
      J. Biochem. 97:923-934(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-55.
    11. "Purification and characterization of a ribonuclease from human liver."
      Sorrentino S., Tucker G.K., Glitz D.G.
      J. Biol. Chem. 263:16125-16131(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-53.
      Tissue: Liver.
    12. "Characterization of a unique nonsecretory ribonuclease from urine of pregnant women."
      Sakakibara R., Hashida K., Kitahara T., Ishiguro M.
      J. Biochem. 111:325-330(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-43.
      Tissue: Urine.
    13. "Characterisation of UGP and its relationship with beta-core fragment."
      Kardana A., Bagshawe K.D., Coles B., Read D., Taylor M.
      Br. J. Cancer 67:686-692(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-45.
      Tissue: Urine.
    14. "New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us."
      Hofsteenge J., Mueller D.R., de Beer T., Loeffler A., Richter W.J., Vliegenthart J.F.G.
      Biochemistry 33:13524-13530(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT TRP-34.
    15. "The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose."
      de Beer T., Vliegenthart J.F.G., Loeffler A., Hofsteenge J.
      Biochemistry 34:11785-11789(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF C-GLYCOSYLATED GROUP.
    16. "Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp."
      Krieg J., Hartmann S., Vicentini A., Glasner W., Hess D., Hofsteenge J.
      Mol. Biol. Cell 9:301-309(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT TRP-34.
    17. "Mutational analysis of the complex of human RNase inhibitor and human eosinophil-derived neurotoxin (RNase 2)."
      Teufel D.P., Kao R.Y., Acharya K.R., Shapiro R.
      Biochemistry 42:1451-1459(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RNH1.
    18. "Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with chemotactic activities for dendritic cells."
      Yang D., Rosenberg H.F., Chen Q., Dyer K.D., Kurosaka K., Oppenheim J.J.
      Blood 102:3396-3403(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CHEMOTAXIS.
    19. Cited for: NITRATION AT TYR-60.
    20. "X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83-A resolution."
      Mosimann S.C., Newton D.L., Youle R.J., James M.N.G.
      J. Mol. Biol. 260:540-552(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
    21. "Mapping the ribonucleolytic active site of eosinophil-derived neurotoxin (EDN). High resolution crystal structures of EDN complexes with adenylic nucleotide inhibitors."
      Leonidas D.D., Boix E., Prill R., Suzuki M., Turton R., Minson K., Swaminathan G.J., Youle R.J., Acharya K.R.
      J. Biol. Chem. 276:15009-15017(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    22. "Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by placental ribonuclease inhibitor."
      Iyer S., Holloway D.E., Kumar K., Shapiro R., Acharya K.R.
      J. Mol. Biol. 347:637-655(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 28-161 IN COMPLEX WITH RNH1, SUBUNIT.
    23. "Crystal structures of eosinophil-derived neurotoxin (EDN) in complex with the inhibitors 5'-ATP, Ap3A, Ap4A, and Ap5A."
      Baker M.D., Holloway D.E., Swaminathan G.J., Acharya K.R.
      Biochemistry 45:416-426(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) OF 28-161 IN COMPLEX WITH ADP AND ATP.

    Entry informationi

    Entry nameiRNAS2_HUMAN
    AccessioniPrimary (citable) accession number: P10153
    Secondary accession number(s): Q52M39, Q9H2B7, Q9UCG7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 164 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

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

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3