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Q504Q3

- PAN2_HUMAN

UniProt

Q504Q3 - PAN2_HUMAN

Protein

PAB-dependent poly(A)-specific ribonuclease subunit PAN2

Gene

PAN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA when the poly(A) stretch is bound by poly(A)-binding protein (PABP), which is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1.2 PublicationsUniRule annotation

    Catalytic activityi

    Exonucleolytic cleavage of poly(A) to 5'-AMP.1 PublicationUniRule annotation

    Enzyme regulationi

    Positively regulated by the regulatory subunit PAN3.UniRule annotation

    GO - Molecular functioni

    1. 3'-5'-exoribonuclease activity Source: UniProtKB
    2. nucleic acid binding Source: InterPro
    3. poly(A)-specific ribonuclease activity Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA metabolic process Source: Reactome
    3. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    4. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
    5. RNA metabolic process Source: Reactome
    6. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    mRNA processing

    Enzyme and pathway databases

    ReactomeiREACT_20514. Deadenylation of mRNA.

    Protein family/group databases

    MEROPSiC19.978.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PAB-dependent poly(A)-specific ribonuclease subunit PAN2UniRule annotation (EC:3.1.13.4UniRule annotation)
    Short name:
    hPan2
    Alternative name(s):
    Inactive ubiquitin carboxyl-terminal hydrolase 52UniRule annotation
    PAB1P-dependent poly(A)-nucleaseUniRule annotation
    PAN deadenylation complex catalytic subunit 2UniRule annotation
    Gene namesi
    Name:PAN2UniRule annotation
    Synonyms:KIAA0710, USP52
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:20074. PAN2.

    Subcellular locationi

    CytoplasmP-body. Nucleus
    Note: Shuttles between nucleus and cytoplasm.

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB-SubCell
    4. PAN complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1087 – 10871D → A: Loss of exonuclease activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA162398664.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12021202PAB-dependent poly(A)-specific ribonuclease subunit PAN2PRO_0000280521Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei791 – 7911Phosphoserine1 Publication
    Modified residuei1189 – 11891Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ504Q3.
    PaxDbiQ504Q3.
    PRIDEiQ504Q3.

    PTM databases

    PhosphoSiteiQ504Q3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ504Q3.
    BgeeiQ504Q3.
    CleanExiHS_PAN2.
    GenevestigatoriQ504Q3.

    Interactioni

    Subunit structurei

    Interacts with the regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) deadenylation complex.2 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PAN3Q58A456EBI-1058976,EBI-2513054

    Protein-protein interaction databases

    BioGridi115252. 341 interactions.
    DIPiDIP-50708N.
    IntActiQ504Q3. 16 interactions.
    STRINGi9606.ENSP00000368809.

    Structurei

    3D structure databases

    ProteinModelPortaliQ504Q3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati153 – 19341WD 1Add
    BLAST
    Repeati195 – 23137WD 2Add
    BLAST
    Repeati244 – 28037WD 3Add
    BLAST
    Repeati328 – 36740WD 4Add
    BLAST
    Domaini517 – 924408USPUniRule annotationAdd
    BLAST
    Domaini975 – 1147173ExonucleaseUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family. PAN2 subfamily.UniRule annotation
    Contains 1 exonuclease domain.UniRule annotation
    Contains 1 USP domain.UniRule annotation
    Contains 4 WD repeats.UniRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG0847.
    HOGENOMiHOG000230585.
    HOVERGENiHBG089847.
    InParanoidiQ504Q3.
    KOiK12571.
    OMAiMEADWDE.
    OrthoDBiEOG7JHM4K.
    PhylomeDBiQ504Q3.
    TreeFamiTF105657.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    3.30.420.10. 1 hit.
    HAMAPiMF_03182. PAN2.
    InterProiIPR006055. Exonuclease.
    IPR013520. Exonuclease_RNaseT/DNA_pol3.
    IPR028881. PAN2.
    IPR012337. RNaseH-like_dom.
    IPR028889. UCH/PAN2.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00929. RNase_T. 1 hit.
    PF13423. UCH_1. 1 hit.
    [Graphical view]
    SMARTiSM00479. EXOIII. 1 hit.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    SSF53098. SSF53098. 1 hit.
    PROSITEiPS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q504Q3-1) [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

    MNFEGLDPGL AEYAPAMHSA LDPVLDAHLN PSLLQNVELD PEGVALEALP     50
    VQESVHIMEG VYSELHSVVA EVGVPVSVSH FDLHEEMLWV GSHGGHATSF 100
    FGPALERYSS FQVNGSDDIR QIQSLENGIL FLTKNNLKYM ARGGLIIFDY 150
    LLDENEDMHS LLLTDSSTLL VGGLQNHIIE IDLNTVQETQ KYAVETPGVT 200
    IMRQTNRFFF CGHTSGKVSL RDLRTFKVEH EFDAFSGSLS DFDVHGNLLA 250
    ACGFSSRLTG LACDRFLKVY DLRMMRAITP LQVHVDPAFL RFIPTYTSRL 300
    AIISQSGQCQ FCEPTGLANP ADIFHVNPVG PLLMTFDVSA SKQALAFGDS 350
    EGCVHLWTDS PEPSFNPYSR ETEFALPCLV DSLPPLDWSQ DLLPLSLIPV 400
    PLTTDTLLSD WPAANSAPAP RRAPPVDAEI LRTMKKVGFI GYAPNPRTRL 450
    RNQIPYRLKE SDSEFDSFSQ VTESPVGREE EPHLHMVSKK YRKVTIKYSK 500
    LGLEDFDFKH YNKTLFAGLE PHIPNAYCNC MIQVLYFLEP VRCLIQNHLC 550
    QKEFCLACEL GFLFHMLDLS RGDPCQGNNF LRAFRTIPEA SALGLILADS 600
    DEASGKGNLA RLIQRWNRFI LTQLHQDMQE LEIPQAYRGA GGSSFCSSGD 650
    SVIGQLFSCE MENCSLCRCG SETVRASSTL LFTLSYPDGS KSDKTGKNYD 700
    FAQVLKRSIC LDQNTQAWCD TCEKYQPTIQ TRNIRHLPDI LVINCEVNSS 750
    KEADFWRMQA EVAFKMAVKK HGGEISKNKE FALADWKELG SPEGVLVCPS 800
    IEELKNVWLP FSIRMKMTKN KGLDVCNWTD GDEMQWGPAR AEEEHGVYVY 850
    DLMATVVHIL DSRTGGSLVA HIKVGETYHQ RKEGVTHQQW YLFNDFLIEP 900
    IDKHEAVQFD MNWKVPAILY YVKRNLNSRY NLNIKNPIEA SVLLAEASLA 950
    RKQRKTHTTF IPLMLNEMPQ IGDLVGLDAE FVTLNEEEAE LRSDGTKSTI 1000
    KPSQMSVARI TCVRGQGPNE GIPFIDDYIS TQEQVVDYLT QYSGIKPGDL 1050
    DAKISSKHLT TLKSTYLKLR FLIDIGVKFV GHGLQKDFRV INLMVPKDQV 1100
    LDTVYLFHMP RKRMISLRFL AWYFLDLKIQ GETHDSIEDA RTALQLYRKY 1150
    LELSKNGTEP ESFHKVLKGL YEKGRKMDWK VPEPEGQTSP KNAAVFSSVL 1200
    AL 1202
    Length:1,202
    Mass (Da):135,368
    Last modified:May 18, 2010 - v3
    Checksum:i579194C102FCA019
    GO
    Isoform 2 (identifier: Q504Q3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         689-692: Missing.

    Show »
    Length:1,198
    Mass (Da):135,008
    Checksum:i9F0D327BE78EC7D7
    GO
    Isoform 3 (identifier: Q504Q3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         643-643: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,201
    Mass (Da):135,281
    Checksum:iE185DC887D382DC1
    GO

    Sequence cautioni

    The sequence BAA31685.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91G → E in AAH94885. (PubMed:15489334)Curated
    Sequence conflicti1091 – 10911I → V in AAH94885. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321S → N.1 Publication
    Corresponds to variant rs11558139 [ dbSNP | Ensembl ].
    VAR_031162
    Natural varianti179 – 1791I → L.3 Publications
    Corresponds to variant rs1918496 [ dbSNP | Ensembl ].
    VAR_031163
    Natural varianti1201 – 12011A → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036359

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei643 – 6431Missing in isoform 3. 1 PublicationVSP_023748
    Alternative sequencei689 – 6924Missing in isoform 2. 2 PublicationsVSP_023749

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB107585 mRNA. Translation: BAD02263.1.
    AB014610 mRNA. Translation: BAA31685.2. Different initiation.
    BC024043 mRNA. Translation: AAH24043.1.
    BC094885 mRNA. Translation: AAH94885.1.
    CCDSiCCDS44922.1. [Q504Q3-1]
    CCDS53802.1. [Q504Q3-3]
    CCDS8915.1. [Q504Q3-2]
    RefSeqiNP_001120932.1. NM_001127460.2.
    NP_001159751.1. NM_001166279.1.
    NP_055686.3. NM_014871.4.
    UniGeneiHs.273397.

    Genome annotation databases

    EnsembliENST00000257931; ENSP00000257931; ENSG00000135473. [Q504Q3-3]
    ENST00000425394; ENSP00000401721; ENSG00000135473. [Q504Q3-1]
    ENST00000440411; ENSP00000388231; ENSG00000135473. [Q504Q3-2]
    ENST00000548043; ENSP00000449861; ENSG00000135473. [Q504Q3-1]
    GeneIDi9924.
    KEGGihsa:9924.
    UCSCiuc001skx.3. human. [Q504Q3-1]
    uc001sky.3. human. [Q504Q3-2]
    uc001skz.3. human. [Q504Q3-3]

    Polymorphism databases

    DMDMi296439280.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB107585 mRNA. Translation: BAD02263.1 .
    AB014610 mRNA. Translation: BAA31685.2 . Different initiation.
    BC024043 mRNA. Translation: AAH24043.1 .
    BC094885 mRNA. Translation: AAH94885.1 .
    CCDSi CCDS44922.1. [Q504Q3-1 ]
    CCDS53802.1. [Q504Q3-3 ]
    CCDS8915.1. [Q504Q3-2 ]
    RefSeqi NP_001120932.1. NM_001127460.2.
    NP_001159751.1. NM_001166279.1.
    NP_055686.3. NM_014871.4.
    UniGenei Hs.273397.

    3D structure databases

    ProteinModelPortali Q504Q3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115252. 341 interactions.
    DIPi DIP-50708N.
    IntActi Q504Q3. 16 interactions.
    STRINGi 9606.ENSP00000368809.

    Protein family/group databases

    MEROPSi C19.978.

    PTM databases

    PhosphoSitei Q504Q3.

    Polymorphism databases

    DMDMi 296439280.

    Proteomic databases

    MaxQBi Q504Q3.
    PaxDbi Q504Q3.
    PRIDEi Q504Q3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257931 ; ENSP00000257931 ; ENSG00000135473 . [Q504Q3-3 ]
    ENST00000425394 ; ENSP00000401721 ; ENSG00000135473 . [Q504Q3-1 ]
    ENST00000440411 ; ENSP00000388231 ; ENSG00000135473 . [Q504Q3-2 ]
    ENST00000548043 ; ENSP00000449861 ; ENSG00000135473 . [Q504Q3-1 ]
    GeneIDi 9924.
    KEGGi hsa:9924.
    UCSCi uc001skx.3. human. [Q504Q3-1 ]
    uc001sky.3. human. [Q504Q3-2 ]
    uc001skz.3. human. [Q504Q3-3 ]

    Organism-specific databases

    CTDi 9924.
    GeneCardsi GC12M056710.
    HGNCi HGNC:20074. PAN2.
    neXtProti NX_Q504Q3.
    PharmGKBi PA162398664.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0847.
    HOGENOMi HOG000230585.
    HOVERGENi HBG089847.
    InParanoidi Q504Q3.
    KOi K12571.
    OMAi MEADWDE.
    OrthoDBi EOG7JHM4K.
    PhylomeDBi Q504Q3.
    TreeFami TF105657.

    Enzyme and pathway databases

    Reactomei REACT_20514. Deadenylation of mRNA.

    Miscellaneous databases

    GeneWikii USP52.
    GenomeRNAii 9924.
    NextBioi 37442.
    PROi Q504Q3.

    Gene expression databases

    ArrayExpressi Q504Q3.
    Bgeei Q504Q3.
    CleanExi HS_PAN2.
    Genevestigatori Q504Q3.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    3.30.420.10. 1 hit.
    HAMAPi MF_03182. PAN2.
    InterProi IPR006055. Exonuclease.
    IPR013520. Exonuclease_RNaseT/DNA_pol3.
    IPR028881. PAN2.
    IPR012337. RNaseH-like_dom.
    IPR028889. UCH/PAN2.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00929. RNase_T. 1 hit.
    PF13423. UCH_1. 1 hit.
    [Graphical view ]
    SMARTi SM00479. EXOIII. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    SSF53098. SSF53098. 1 hit.
    PROSITEi PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein."
      Uchida N., Hoshino S., Katada T.
      J. Biol. Chem. 279:1383-1391(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH PAN3 AND POLYADENYLATE-BINDING PROTEIN, MUTAGENESIS OF ASP-1087, VARIANT LEU-179.
      Tissue: Cervix carcinoma.
    2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT LEU-179.
      Tissue: Brain.
    3. Ohara O., Suyama M., Nagase T., Ishikawa K.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    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] (ISOFORMS 1 AND 2), VARIANTS ASN-32 AND LEU-179.
      Tissue: Eye and Testis.
    5. "Cloning and enzymatic analysis of 22 novel human ubiquitin-specific proteases."
      Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S., Lopez-Otin C.
      Biochem. Biophys. Res. Commun. 314:54-62(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF UBIQUITIN CARBOXYL TERMINAL HYDROLASE ACTIVITY.
    6. "Concerted action of poly(A) nucleases and decapping enzyme in mammalian mRNA turnover."
      Yamashita A., Chang T.-C., Yamashita Y., Zhu W., Zhong Z., Chen C.-Y.A., Shyu A.-B.
      Nat. Struct. Mol. Biol. 12:1054-1063(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells."
      Zheng D., Ezzeddine N., Chen C.Y., Zhu W., He X., Shyu A.B.
      J. Cell Biol. 182:89-101(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Structure of the PAN3 pseudokinase reveals the basis for interactions with the PAN2 deadenylase and the GW182 proteins."
      Christie M., Boland A., Huntzinger E., Weichenrieder O., Izaurralde E.
      Mol. Cell 51:360-373(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAN3.
    13. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-1201.

    Entry informationi

    Entry nameiPAN2_HUMAN
    AccessioniPrimary (citable) accession number: Q504Q3
    Secondary accession number(s): O75189, Q76E12, Q8IVE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 102 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3