Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytosolic 5'-nucleotidase 3A

Gene

NT5C3A

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

Functioni

Nucleotidase which shows specific activity towards cytidine monophosphate (CMP) and 7-methylguanosine monophosphate (m7GMP) (PubMed:24603684). CMP seems to be the preferred substrate (PubMed:15968458).2 Publications

Catalytic activityi

N(7)-methyl-GMP + H2O = N(7)-methyl-guanosine + phosphate.1 Publication
CMP + H2O = cytidine + phosphate.1 Publication
A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.1 Publication

Kineticsi

  1. KM=15 µM for m7GMP (at 37 degrees Celsius)1 Publication
  2. KM=66 µM for CMP1 Publication
  3. KM=80 µM for CMP (at 37 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei88Nucleophile1 Publication1
    Metal bindingi88Magnesium1 Publication1
    Active sitei90Proton donor1 Publication1
    Metal bindingi90Magnesium; via carbonyl oxygen1 Publication1
    Binding sitei135CMPBy similarity1
    Binding sitei135N(7)-methyl-GMPBy similarity1
    Binding sitei156N(7)-methyl-GMPBy similarity1
    Binding sitei252SubstrateBy similarity1
    Metal bindingi277Magnesium1 Publication1

    GO - Molecular functioni

    • 2'-phosphotransferase activity Source: UniProtKB
    • 5'-nucleotidase activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Transferase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciZFISH:HS04585-MONOMER.
    BRENDAi3.1.3.91. 2681.
    ReactomeiR-HSA-73621. Pyrimidine catabolism.
    SABIO-RKQ9H0P0.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosolic 5'-nucleotidase 3A2 Publications (EC:3.1.3.52 Publications)
    Alternative name(s):
    7-methylguanosine phosphate-specific 5'-nucleotidase1 Publication (EC:3.1.3.911 Publication)
    Short name:
    7-methylguanosine nucleotidase
    Cytosolic 5'-nucleotidase 3
    Cytosolic 5'-nucleotidase III
    Short name:
    cN-III
    Pyrimidine 5'-nucleotidase 1
    Short name:
    P5'N-1
    Short name:
    P5N-1
    Short name:
    PN-I
    Uridine 5'-monophosphate hydrolase 1
    p36
    Gene namesi
    Name:NT5C3A
    Synonyms:NT5C3, P5N1, UMPH1
    ORF Names:HSPC233
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:17820. NT5C3A.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: Reactome
    • endoplasmic reticulum Source: UniProtKB
    • mitochondrion Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    P5N deficiency (P5ND)8 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAutosomal recessive condition causing hemolytic anemia characterized by marked basophilic stippling and the accumulation of high concentrations of pyrimidine nucleotides within the erythrocyte. It is implicated in the anemia of lead poisoning and is possibly associated with learning difficulties.
    See also OMIM:266120
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07316095R → G in P5ND. 1 Publication1
    Natural variantiVAR_073161113C → R in P5ND; reduced catalytic activity especially towards UMP. 1 Publication1
    Natural variantiVAR_023511137D → V in P5ND; reduced catalytic activity. 2 PublicationsCorresponds to variant rs104894025dbSNPEnsembl.1
    Natural variantiVAR_023512181L → P in P5ND; reduced catalytic activity in vitro; reduced protein stability in vivo, probably through increased proteasomal degradation. 3 Publications1
    Natural variantiVAR_073162207G → R in P5ND; reduced catalytic activity especially towards UMP. 2 Publications1
    Natural variantiVAR_023513229N → S in P5ND; almost complete loss of catalytic activity. 3 PublicationsCorresponds to variant rs104894028dbSNPEnsembl.1
    Natural variantiVAR_023514280G → R in P5ND; greatly reduced catalytic activity. 3 PublicationsCorresponds to variant rs104894029dbSNPEnsembl.1
    Natural variantiVAR_073163297I → T in P5ND. 2 Publications1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi88D → N: Loss of nucleotidase and phosphotransferase activity. 1 Publication1
    Mutagenesisi89F → A: Almost complete loss of nucleotidase and phosphotransferase activity. 1 Publication1
    Mutagenesisi90D → N: Loss of nucleotidase and phosphotransferase activity. 1 Publication1
    Mutagenesisi135E → D: No effect on nucleotidase activity. Almost complete loss of phosphotransferase activity. 1 Publication1
    Mutagenesisi232D → N: No effect on nucleotidase and phosphotransferase activity. 1 Publication1
    Mutagenesisi233F → A: Almost complete loss of nucleotidase and phosphotransferase activity. 1 Publication1
    Mutagenesisi234D → N: No effect on nucleotidase and phosphotransferase activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi51251.
    MalaCardsiNT5C3A.
    MIMi266120. phenotype.
    OpenTargetsiENSG00000122643.
    Orphaneti35120. Hemolytic anemia due to pyrimidine 5' nucleotidase deficiency.
    PharmGKBiPA31802.

    Polymorphism and mutation databases

    BioMutaiNT5C3A.
    DMDMi117949804.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000643871 – 336Cytosolic 5'-nucleotidase 3AAdd BLAST336

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei278PhosphoserineBy similarity1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    EPDiQ9H0P0.
    PaxDbiQ9H0P0.
    PeptideAtlasiQ9H0P0.
    PRIDEiQ9H0P0.

    PTM databases

    DEPODiQ9H0P0.
    iPTMnetiQ9H0P0.
    PhosphoSitePlusiQ9H0P0.

    Expressioni

    Tissue specificityi

    Isoforms 1, 3 and 4 are expressed in reticulocytes. Isoform 4 is hardly detectable in bone marrow and fetal liver.2 Publications

    Inductioni

    Isoform 2 is induced by interferon alpha in Raji cells in association with lupus inclusions.1 Publication

    Gene expression databases

    BgeeiENSG00000122643.
    ExpressionAtlasiQ9H0P0. baseline and differential.
    GenevisibleiQ9H0P0. HS.

    Organism-specific databases

    HPAiHPA010630.
    HPA029058.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi119408. 21 interactors.
    IntActiQ9H0P0. 9 interactors.
    MINTiMINT-3065844.
    STRINGi9606.ENSP00000242210.

    Structurei

    Secondary structure

    1336
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi65 – 78Combined sources14
    Helixi80 – 82Combined sources3
    Beta strandi83 – 87Combined sources5
    Turni90 – 92Combined sources3
    Beta strandi96 – 98Combined sources3
    Helixi106 – 111Combined sources6
    Helixi118 – 135Combined sources18
    Beta strandi138 – 140Combined sources3
    Helixi142 – 163Combined sources22
    Helixi167 – 169Combined sources3
    Helixi170 – 175Combined sources6
    Helixi185 – 194Combined sources10
    Beta strandi199 – 206Combined sources8
    Helixi207 – 216Combined sources10
    Beta strandi224 – 229Combined sources6
    Beta strandi231 – 233Combined sources3
    Beta strandi237 – 242Combined sources6
    Helixi252 – 258Combined sources7
    Helixi260 – 264Combined sources5
    Turni265 – 268Combined sources4
    Beta strandi271 – 279Combined sources9
    Helixi280 – 283Combined sources4
    Turni284 – 287Combined sources4
    Beta strandi292 – 300Combined sources9
    Helixi304 – 312Combined sources9
    Beta strandi315 – 320Combined sources6
    Helixi326 – 335Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2CN1X-ray2.67A64-336[»]
    2JGAX-ray3.01A64-336[»]
    2VKQX-ray2.50A64-336[»]
    ProteinModelPortaliQ9H0P0.
    SMRiQ9H0P0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H0P0.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni203 – 204Substrate binding1 Publication2

    Sequence similaritiesi

    Belongs to the pyrimidine 5'-nucleotidase family.Curated

    Phylogenomic databases

    eggNOGiKOG3128. Eukaryota.
    ENOG410ZQJ8. LUCA.
    GeneTreeiENSGT00390000012959.
    HOVERGENiHBG059750.
    KOiK01081.
    OMAiAGVYHSN.
    OrthoDBiEOG091G0BCN.
    PhylomeDBiQ9H0P0.
    TreeFamiTF314663.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006434. Pyrimidine_nucleotidase_eu.
    [Graphical view]
    PfamiPF05822. UMPH-1. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01544. HAD-SF-IE. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 2 (identifier: Q9H0P0-4) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MRAPSMDRAA VARVGAVASA SVCALVAGVV LAQYIFTLKR KTGRKTKIIE
    60 70 80 90 100
    MMPEFQKSSV RIKNPTRVEE IICGLIKGGA AKLQIITDFD MTLSRFSYKG
    110 120 130 140 150
    KRCPTCHNII DNCKLVTDEC RKKLLQLKEK YYAIEVDPVL TVEEKYPYMV
    160 170 180 190 200
    EWYTKSHGLL VQQALPKAKL KEIVAESDVM LKEGYENFFD KLQQHSIPVF
    210 220 230 240 250
    IFSAGIGDVL EEVIRQAGVY HPNVKVVSNF MDFDETGVLK GFKGELIHVF
    260 270 280 290 300
    NKHDGALRNT EYFNQLKDNS NIILLGDSQG DLRMADGVAN VEHILKIGYL
    310 320 330
    NDRVDELLEK YMDSYDIVLV QDESLEVANS ILQKIL
    Length:336
    Mass (Da):37,948
    Last modified:November 14, 2006 - v3
    Checksum:iC5D75CCF1BB61021
    GO
    Isoform 1 (identifier: Q9H0P0-1) [UniParc]FASTAAdd to basket
    Also known as: P5N-I

    The sequence of this isoform differs from the canonical sequence as follows:
         1-50: MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIE → MTNQESAVHVK

    Show »
    Length:297
    Mass (Da):33,915
    Checksum:iFB91A66DD2273598
    GO
    Isoform 3 (identifier: Q9H0P0-2) [UniParc]FASTAAdd to basket
    Also known as: p36

    The sequence of this isoform differs from the canonical sequence as follows:
         1-50: Missing.

    Show »
    Length:286
    Mass (Da):32,690
    Checksum:i29313E2790194ED9
    GO
    Isoform 4 (identifier: Q9H0P0-3) [UniParc]FASTAAdd to basket
    Also known as: P5N-R

    The sequence of this isoform differs from the canonical sequence as follows:
         1-51: Missing.

    Show »
    Length:285
    Mass (Da):32,559
    Checksum:iCB3B6812C90A5578
    GO

    Sequence cautioni

    The sequence AAF36153 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAG33630 differs from that shown. Reason: Frameshift at several positions.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti95R → K AA sequence (PubMed:8557639).Curated1
    Sequence conflicti144E → Q AA sequence (PubMed:8557639).Curated1
    Sequence conflicti329N → R AA sequence (PubMed:8557639).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07316095R → G in P5ND. 1 Publication1
    Natural variantiVAR_073161113C → R in P5ND; reduced catalytic activity especially towards UMP. 1 Publication1
    Natural variantiVAR_023511137D → V in P5ND; reduced catalytic activity. 2 PublicationsCorresponds to variant rs104894025dbSNPEnsembl.1
    Natural variantiVAR_023512181L → P in P5ND; reduced catalytic activity in vitro; reduced protein stability in vivo, probably through increased proteasomal degradation. 3 Publications1
    Natural variantiVAR_073162207G → R in P5ND; reduced catalytic activity especially towards UMP. 2 Publications1
    Natural variantiVAR_023513229N → S in P5ND; almost complete loss of catalytic activity. 3 PublicationsCorresponds to variant rs104894028dbSNPEnsembl.1
    Natural variantiVAR_023514280G → R in P5ND; greatly reduced catalytic activity. 3 PublicationsCorresponds to variant rs104894029dbSNPEnsembl.1
    Natural variantiVAR_073163297I → T in P5ND. 2 Publications1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0156241 – 51Missing in isoform 4. 1 PublicationAdd BLAST51
    Alternative sequenceiVSP_0215651 – 50MRAPS…TKIIE → MTNQESAVHVK in isoform 1. 2 PublicationsAdd BLAST50
    Alternative sequenceiVSP_0156231 – 50Missing in isoform 3. 2 PublicationsAdd BLAST50

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF312735 mRNA. Translation: AAG33630.1. Sequence problems.
    AL136716 mRNA. Translation: CAB66650.1.
    AK290118 mRNA. Translation: BAF82807.1.
    AK314109 mRNA. Translation: BAG36802.1.
    CR533518 mRNA. Translation: CAG38549.1.
    AC074338 Genomic DNA. No translation available.
    AC083863 Genomic DNA. No translation available.
    CH471073 Genomic DNA. Translation: EAW94007.1.
    CH471073 Genomic DNA. Translation: EAW94008.1.
    BC013292 mRNA. Translation: AAH13292.2.
    BC015856 mRNA. Translation: AAH15856.2.
    BC066914 mRNA. Translation: AAH66914.1.
    BC071652 mRNA. Translation: AAH71652.2.
    AF151067 mRNA. Translation: AAF36153.1. Different initiation.
    CCDSiCCDS34616.1. [Q9H0P0-4]
    CCDS34617.1. [Q9H0P0-1]
    CCDS55101.1. [Q9H0P0-3]
    RefSeqiNP_001002009.1. NM_001002009.2. [Q9H0P0-1]
    NP_001002010.1. NM_001002010.2. [Q9H0P0-4]
    NP_001159590.1. NM_001166118.2. [Q9H0P0-3]
    NP_057573.2. NM_016489.12. [Q9H0P0-1]
    XP_011513711.1. XM_011515409.2. [Q9H0P0-3]
    UniGeneiHs.487933.

    Genome annotation databases

    EnsembliENST00000242210; ENSP00000242210; ENSG00000122643. [Q9H0P0-4]
    ENST00000381626; ENSP00000371039; ENSG00000122643. [Q9H0P0-3]
    ENST00000396152; ENSP00000379456; ENSG00000122643. [Q9H0P0-1]
    ENST00000405342; ENSP00000385261; ENSG00000122643. [Q9H0P0-1]
    ENST00000409467; ENSP00000387166; ENSG00000122643. [Q9H0P0-3]
    ENST00000620705; ENSP00000484415; ENSG00000122643. [Q9H0P0-4]
    GeneIDi51251.
    KEGGihsa:51251.
    UCSCiuc003tdi.5. human. [Q9H0P0-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF312735 mRNA. Translation: AAG33630.1. Sequence problems.
    AL136716 mRNA. Translation: CAB66650.1.
    AK290118 mRNA. Translation: BAF82807.1.
    AK314109 mRNA. Translation: BAG36802.1.
    CR533518 mRNA. Translation: CAG38549.1.
    AC074338 Genomic DNA. No translation available.
    AC083863 Genomic DNA. No translation available.
    CH471073 Genomic DNA. Translation: EAW94007.1.
    CH471073 Genomic DNA. Translation: EAW94008.1.
    BC013292 mRNA. Translation: AAH13292.2.
    BC015856 mRNA. Translation: AAH15856.2.
    BC066914 mRNA. Translation: AAH66914.1.
    BC071652 mRNA. Translation: AAH71652.2.
    AF151067 mRNA. Translation: AAF36153.1. Different initiation.
    CCDSiCCDS34616.1. [Q9H0P0-4]
    CCDS34617.1. [Q9H0P0-1]
    CCDS55101.1. [Q9H0P0-3]
    RefSeqiNP_001002009.1. NM_001002009.2. [Q9H0P0-1]
    NP_001002010.1. NM_001002010.2. [Q9H0P0-4]
    NP_001159590.1. NM_001166118.2. [Q9H0P0-3]
    NP_057573.2. NM_016489.12. [Q9H0P0-1]
    XP_011513711.1. XM_011515409.2. [Q9H0P0-3]
    UniGeneiHs.487933.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2CN1X-ray2.67A64-336[»]
    2JGAX-ray3.01A64-336[»]
    2VKQX-ray2.50A64-336[»]
    ProteinModelPortaliQ9H0P0.
    SMRiQ9H0P0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119408. 21 interactors.
    IntActiQ9H0P0. 9 interactors.
    MINTiMINT-3065844.
    STRINGi9606.ENSP00000242210.

    PTM databases

    DEPODiQ9H0P0.
    iPTMnetiQ9H0P0.
    PhosphoSitePlusiQ9H0P0.

    Polymorphism and mutation databases

    BioMutaiNT5C3A.
    DMDMi117949804.

    Proteomic databases

    EPDiQ9H0P0.
    PaxDbiQ9H0P0.
    PeptideAtlasiQ9H0P0.
    PRIDEiQ9H0P0.

    Protocols and materials databases

    DNASUi51251.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000242210; ENSP00000242210; ENSG00000122643. [Q9H0P0-4]
    ENST00000381626; ENSP00000371039; ENSG00000122643. [Q9H0P0-3]
    ENST00000396152; ENSP00000379456; ENSG00000122643. [Q9H0P0-1]
    ENST00000405342; ENSP00000385261; ENSG00000122643. [Q9H0P0-1]
    ENST00000409467; ENSP00000387166; ENSG00000122643. [Q9H0P0-3]
    ENST00000620705; ENSP00000484415; ENSG00000122643. [Q9H0P0-4]
    GeneIDi51251.
    KEGGihsa:51251.
    UCSCiuc003tdi.5. human. [Q9H0P0-4]

    Organism-specific databases

    CTDi51251.
    DisGeNETi51251.
    GeneCardsiNT5C3A.
    HGNCiHGNC:17820. NT5C3A.
    HPAiHPA010630.
    HPA029058.
    MalaCardsiNT5C3A.
    MIMi266120. phenotype.
    606224. gene.
    neXtProtiNX_Q9H0P0.
    OpenTargetsiENSG00000122643.
    Orphaneti35120. Hemolytic anemia due to pyrimidine 5' nucleotidase deficiency.
    PharmGKBiPA31802.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3128. Eukaryota.
    ENOG410ZQJ8. LUCA.
    GeneTreeiENSGT00390000012959.
    HOVERGENiHBG059750.
    KOiK01081.
    OMAiAGVYHSN.
    OrthoDBiEOG091G0BCN.
    PhylomeDBiQ9H0P0.
    TreeFamiTF314663.

    Enzyme and pathway databases

    BioCyciZFISH:HS04585-MONOMER.
    BRENDAi3.1.3.91. 2681.
    ReactomeiR-HSA-73621. Pyrimidine catabolism.
    SABIO-RKQ9H0P0.

    Miscellaneous databases

    EvolutionaryTraceiQ9H0P0.
    GeneWikiiNT5C3.
    GenomeRNAii51251.
    PROiQ9H0P0.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000122643.
    ExpressionAtlasiQ9H0P0. baseline and differential.
    GenevisibleiQ9H0P0. HS.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006434. Pyrimidine_nucleotidase_eu.
    [Graphical view]
    PfamiPF05822. UMPH-1. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01544. HAD-SF-IE. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry namei5NT3A_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0P0
    Secondary accession number(s): A8K253
    , B2RAA5, B8ZZC4, Q6IPZ1, Q6NXS6, Q7L3G6, Q9P0P5, Q9UC42, Q9UC43, Q9UC44, Q9UC45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2005
    Last sequence update: November 14, 2006
    Last modified: November 30, 2016
    This is version 149 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 7
      Human chromosome 7: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.