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Q9H4L4

- SENP3_HUMAN

UniProt

Q9H4L4 - SENP3_HUMAN

Protein

Sentrin-specific protease 3

Gene

SENP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (12 Dec 2006)
      Previous versions | rss
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    Functioni

    Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates. Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability. Deconjugates SUMO2 and SUMO3 from CDCA8. Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300. Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1. Plays a role in the regulation of sumoylation status of ZNF148. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes.7 Publications

    Catalytic activityi

    Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.

    Enzyme regulationi

    On oxidative stress, SENP3 degradation is blocked by inhibition of its ubiquitination, which stabilizes it as it accumulates in the nucleoplasm.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei465 – 4651By similarity
    Active sitei482 – 4821By similarity
    Active sitei532 – 5321By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ubiquitin-specific protease activity Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    BRENDAi3.4.22.68. 2681.

    Protein family/group databases

    MEROPSiC48.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sentrin-specific protease 3 (EC:3.4.22.68)
    Alternative name(s):
    SUMO-1-specific protease 3
    Sentrin/SUMO-specific protease SENP3
    Gene namesi
    Name:SENP3
    Synonyms:SSP3, SUSP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:17862. SENP3.

    Subcellular locationi

    Cytoplasm By similarity. Nucleusnucleolus. Nucleusnucleoplasm
    Note: Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions By similarity. Redistributes between the nucleolus and the nucleoplasm in response to mild oxidative stress.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. MLL1 complex Source: UniProtKB
    3. nucleolus Source: LIFEdb

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi532 – 5321C → S: Loss of enzymatic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134933213.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 574574Sentrin-specific protease 3PRO_0000101721Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei169 – 1691Phosphoserine3 Publications
    Modified residuei181 – 1811Phosphoserine1 Publication
    Modified residuei212 – 2121Phosphoserine2 Publications
    Modified residuei232 – 2321Phosphoserine3 Publications
    Modified residuei353 – 3531Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H4L4.
    PaxDbiQ9H4L4.
    PRIDEiQ9H4L4.

    PTM databases

    PhosphoSiteiQ9H4L4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H4L4.
    BgeeiQ9H4L4.
    CleanExiHS_SENP3.
    GenevestigatoriQ9H4L4.

    Organism-specific databases

    HPAiHPA060290.

    Interactioni

    Subunit structurei

    Binds to SUMO1 and SUMO3 By similarity. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with EP300, NPM1 and CDCA8. Component of the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and ZNF148. Interacts with NOL9.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NPM1P067486EBI-2880236,EBI-78579
    PELP1Q8IZL85EBI-2880236,EBI-716449
    TEX10Q9NXF12EBI-2880236,EBI-2371062
    UBCP0CG482EBI-2880236,EBI-3390054
    WDR18Q9BV383EBI-2880236,EBI-727429

    Protein-protein interaction databases

    BioGridi117594. 42 interactions.
    DIPiDIP-47511N.
    IntActiQ9H4L4. 22 interactions.
    MINTiMINT-1200849.
    STRINGi9606.ENSP00000314029.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H4L4.
    SMRiQ9H4L4. Positions 385-572.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni386 – 543158ProteaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi125 – 1284Nuclear localization signalSequence Analysis
    Motifi153 – 1597Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi13 – 6856Pro-richAdd
    BLAST
    Compositional biasi76 – 9217Glu-richAdd
    BLAST
    Compositional biasi192 – 1954Poly-Pro

    Sequence similaritiesi

    Belongs to the peptidase C48 family.Curated

    Phylogenomic databases

    eggNOGiCOG5160.
    HOGENOMiHOG000154287.
    HOVERGENiHBG059450.
    InParanoidiQ9H4L4.
    KOiK08593.
    OMAiRLPPRWG.
    PhylomeDBiQ9H4L4.
    TreeFamiTF316289.

    Family and domain databases

    InterProiIPR003653. Peptidase_C48.
    [Graphical view]
    PfamiPF02902. Peptidase_C48. 1 hit.
    [Graphical view]
    PROSITEiPS50600. ULP_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9H4L4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKETIQGTGS WGPEPPGPGI PPAYSSPRRE RLRWPPPPKP RLKSGGGFGP    50
    DPGSGTTVPA RRLPVPRPSF DASASEEEEE EEEEEDEDEE EEVAAWRLPP 100
    RWSQLGTSQR PRPSRPTHRK TCSQRRRRAM RAFRMLLYSK STSLTFHWKL 150
    WGRHRGRRRG LAHPKNHLSP QQGGATPQVP SPCCRFDSPR GPPPPRLGLL 200
    GALMAEDGVR GSPPVPSGPP MEEDGLRWTP KSPLDPDSGL LSCTLPNGFG 250
    GQSGPEGERS LAPPDASILI SNVCSIGDHV AQELFQGSDL GMAEEAERPG 300
    EKAGQHSPLR EEHVTCVQSI LDEFLQTYGS LIPLSTDEVV EKLEDIFQQE 350
    FSTPSRKGLV LQLIQSYQRM PGNAMVRGFR VAYKRHVLTM DDLGTLYGQN 400
    WLNDQVMNMY GDLVMDTVPE KVHFFNSFFY DKLRTKGYDG VKRWTKNVDI 450
    FNKELLLIPI HLEVHWSLIS VDVRRRTITY FDSQRTLNRR CPKHIAKYLQ 500
    AEAVKKDRLD FHQGWKGYFK MNVARQNNDS DCGAFVLQYC KHLALSQPFS 550
    FTQQDMPKLR RQIYKELCHC KLTV 574
    Length:574
    Mass (Da):65,010
    Last modified:December 12, 2006 - v2
    Checksum:iE495137EE7500741
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 312ER → DG in AAG33252. (PubMed:10806345)Curated
    Sequence conflicti60 – 601A → T in AAG33252. (PubMed:10806345)Curated
    Sequence conflicti65 – 651V → A in AAG33252. (PubMed:10806345)Curated
    Sequence conflicti113 – 1142PS → AL in AAG33252. (PubMed:10806345)Curated
    Sequence conflicti117 – 1171T → S in AAG33252. (PubMed:10806345)Curated
    Sequence conflicti134 – 1341R → Q in AAG33252. (PubMed:10806345)Curated
    Sequence conflicti161 – 1611L → S in AAH48306. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti515 – 5151W → R.
    Corresponds to variant rs9972914 [ dbSNP | Ensembl ].
    VAR_051544

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY008763 mRNA. Translation: AAG33252.1.
    AF199459 mRNA. Translation: AAL25652.1.
    AL050283 mRNA. Translation: CAB43384.2.
    AL834294 mRNA. Translation: CAD38967.1.
    BC048306 mRNA. Translation: AAH48306.1.
    BC080658 mRNA. Translation: AAH80658.1.
    PIRiT08759.
    RefSeqiNP_056485.2. NM_015670.5.
    UniGeneiHs.513926.
    Hs.733104.

    Genome annotation databases

    EnsembliENST00000429205; ENSP00000403712; ENSG00000161956.
    GeneIDi26168.
    KEGGihsa:26168.
    UCSCiuc002ghm.3. human.

    Polymorphism databases

    DMDMi119370525.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY008763 mRNA. Translation: AAG33252.1 .
    AF199459 mRNA. Translation: AAL25652.1 .
    AL050283 mRNA. Translation: CAB43384.2 .
    AL834294 mRNA. Translation: CAD38967.1 .
    BC048306 mRNA. Translation: AAH48306.1 .
    BC080658 mRNA. Translation: AAH80658.1 .
    PIRi T08759.
    RefSeqi NP_056485.2. NM_015670.5.
    UniGenei Hs.513926.
    Hs.733104.

    3D structure databases

    ProteinModelPortali Q9H4L4.
    SMRi Q9H4L4. Positions 385-572.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117594. 42 interactions.
    DIPi DIP-47511N.
    IntActi Q9H4L4. 22 interactions.
    MINTi MINT-1200849.
    STRINGi 9606.ENSP00000314029.

    Protein family/group databases

    MEROPSi C48.003.

    PTM databases

    PhosphoSitei Q9H4L4.

    Polymorphism databases

    DMDMi 119370525.

    Proteomic databases

    MaxQBi Q9H4L4.
    PaxDbi Q9H4L4.
    PRIDEi Q9H4L4.

    Protocols and materials databases

    DNASUi 26168.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000429205 ; ENSP00000403712 ; ENSG00000161956 .
    GeneIDi 26168.
    KEGGi hsa:26168.
    UCSCi uc002ghm.3. human.

    Organism-specific databases

    CTDi 26168.
    GeneCardsi GC17P007467.
    H-InvDB HIX0013501.
    HGNCi HGNC:17862. SENP3.
    HPAi HPA060290.
    MIMi 612844. gene.
    neXtProti NX_Q9H4L4.
    PharmGKBi PA134933213.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5160.
    HOGENOMi HOG000154287.
    HOVERGENi HBG059450.
    InParanoidi Q9H4L4.
    KOi K08593.
    OMAi RLPPRWG.
    PhylomeDBi Q9H4L4.
    TreeFami TF316289.

    Enzyme and pathway databases

    BRENDAi 3.4.22.68. 2681.

    Miscellaneous databases

    ChiTaRSi SENP3. human.
    GeneWikii SENP3.
    GenomeRNAii 26168.
    NextBioi 48279.
    PROi Q9H4L4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H4L4.
    Bgeei Q9H4L4.
    CleanExi HS_SENP3.
    Genevestigatori Q9H4L4.

    Family and domain databases

    InterProi IPR003653. Peptidase_C48.
    [Graphical view ]
    Pfami PF02902. Peptidase_C48. 1 hit.
    [Graphical view ]
    PROSITEi PS50600. ULP_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Ubiquitin-like proteins: new wines in new bottles."
      Yeh E.T.H., Gong L., Kamitani T.
      Gene 248:1-14(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Choi S.J., Jeon Y.-J., Kim K.I., Nishimori S., Suzuki T., Uchida S., Shimbara N., Tanaka K., Chung C.H.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Melanoma and Uterus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
      Tissue: Lymph and Uterus.
    6. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
      Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
      Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
    7. "Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors."
      Gregoire S., Yang X.-J.
      Mol. Cell. Biol. 25:2273-2287(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3."
      Gong L., Yeh E.T.H.
      J. Biol. Chem. 281:15869-15877(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing."
      Haindl M., Harasim T., Eick D., Muller S.
      EMBO Rep. 9:273-279(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-532, INTERACTION WITH NPM1.
    11. "Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases."
      Yun C., Wang Y., Mukhopadhyay D., Backlund P., Kolli N., Yergey A., Wilkinson K.D., Dasso M.
      J. Cell Biol. 183:589-595(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH NPM1.
    12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND THR-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation."
      Huang C., Han Y., Wang Y., Sun X., Yan S., Yeh E.T.H., Chen Y., Cang H., Li H., Shi G., Cheng J., Tang X., Yi J.
      EMBO J. 28:2748-2762(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH EP300.
    16. "RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin."
      Klein U.R., Haindl M., Nigg E.A., Muller S.
      Mol. Biol. Cell 20:410-418(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDCA8.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
      Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
      Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX.

    Entry informationi

    Entry nameiSENP3_HUMAN
    AccessioniPrimary (citable) accession number: Q9H4L4
    Secondary accession number(s): Q66K15
    , Q86VS7, Q96PS4, Q9Y3W9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2002
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 116 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, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3