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Q9H2H8

- PPIL3_HUMAN

UniProt

Q9H2H8 - PPIL3_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase-like 3

Gene

PPIL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).

    GO - Molecular functioni

    1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. mRNA splicing, via spliceosome Source: UniProtKB
    2. protein folding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Enzyme and pathway databases

    BRENDAi5.2.1.8. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase-like 3 (EC:5.2.1.8)
    Short name:
    PPIase
    Alternative name(s):
    Cyclophilin J
    Short name:
    CyPJ
    Cyclophilin-like protein PPIL3
    Rotamase PPIL3
    Gene namesi
    Name:PPIL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9262. PPIL3.

    Subcellular locationi

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB

    Keywords - Cellular componenti

    Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33589.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 161160Peptidyl-prolyl cis-trans isomerase-like 3PRO_0000064166Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9H2H8.
    PaxDbiQ9H2H8.
    PRIDEiQ9H2H8.

    PTM databases

    PhosphoSiteiQ9H2H8.

    Expressioni

    Tissue specificityi

    Ubiquitous. Detected at low levels.1 Publication

    Gene expression databases

    ArrayExpressiQ9H2H8.
    BgeeiQ9H2H8.
    CleanExiHS_PPIL3.
    GenevestigatoriQ9H2H8.

    Organism-specific databases

    HPAiHPA040765.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    VP3Q991523EBI-751051,EBI-1776808From a different organism.

    Protein-protein interaction databases

    BioGridi119820. 19 interactions.
    IntActiQ9H2H8. 3 interactions.
    MINTiMINT-3063495.
    STRINGi9606.ENSP00000286175.

    Structurei

    Secondary structure

    1
    161
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76
    Beta strandi10 – 167
    Turni18 – 203
    Helixi22 – 3312
    Turni34 – 396
    Beta strandi44 – 463
    Turni47 – 493
    Beta strandi50 – 534
    Beta strandi58 – 614
    Beta strandi86 – 894
    Beta strandi92 – 954
    Beta strandi101 – 1066
    Helixi109 – 1113
    Turni112 – 1143
    Beta strandi117 – 1237
    Helixi125 – 1328
    Turni138 – 1403
    Beta strandi143 – 1453
    Beta strandi148 – 1558

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XYHX-ray2.60A1-161[»]
    2OJUX-ray2.40A/B1-161[»]
    2OK3X-ray2.00A1-161[»]
    ProteinModelPortaliQ9H2H8.
    SMRiQ9H2H8. Positions 1-160.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H2H8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 154153PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0652.
    HOGENOMiHOG000065981.
    HOVERGENiHBG001065.
    KOiK12734.
    OMAiCEMESRC.
    OrthoDBiEOG769ZKZ.
    PhylomeDBiQ9H2H8.
    TreeFamiTF352224.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view]
    PfamiPF00160. Pro_isomerase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSiPR00153. CSAPPISMRASE.
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H2H8-1) [UniParc]FASTAAdd to Basket

    Also known as: PPIL3b

    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

    MSVTLHTDVG DIKIEVFCER TPKTCENFLA LCASNYYNGC IFHRNIKGFM    50
    VQTGDPTGTG RGGNSIWGKK FEDEYSEYLK HNVRGVVSMA NNGPNTNGSQ 100
    FFITYGKQPH LDMKYTVFGK VIDGLETLDE LEKLPVNEKT YRPLNDVHIK 150
    DITIHANPFA Q 161
    Length:161
    Mass (Da):18,155
    Last modified:March 1, 2001 - v1
    Checksum:i5FE190D7858B07D4
    GO
    Isoform 2 (identifier: Q9H2H8-2) [UniParc]FASTAAdd to Basket

    Also known as: PPIL3a

    The sequence of this isoform differs from the canonical sequence as follows:
         27-58: NFLALCASNYYNGCIFHRNIKGFMVQTGDPTG → MESRCVPQAGVQWRDLGSLQPPPPGFKQVFCLSLPR

    Show »
    Length:165
    Mass (Da):18,627
    Checksum:iA533E5F757C18934
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 622RG → KR in AAO64723. 1 PublicationCurated
    Sequence conflicti65 – 651S → V in AAO64723. 1 PublicationCurated
    Sequence conflicti78 – 781Y → I in AAO64723. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti146 – 1461D → E.1 Publication
    Corresponds to variant rs7562391 [ dbSNP | Ensembl ].
    VAR_023417

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei27 – 5832NFLAL…GDPTG → MESRCVPQAGVQWRDLGSLQ PPPPGFKQVFCLSLPR in isoform 2. 2 PublicationsVSP_015468Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF251049 mRNA. Translation: AAK34939.1.
    AF271652 mRNA. Translation: AAG44766.1.
    AF146799 mRNA. Translation: AAO64723.1.
    AK027315 mRNA. Translation: BAB55036.1.
    AC005037 Genomic DNA. Translation: AAY14723.1.
    BC007693 mRNA. Translation: AAH07693.1.
    CCDSiCCDS2332.1. [Q9H2H8-2]
    CCDS2333.1. [Q9H2H8-1]
    RefSeqiNP_115861.1. NM_032472.3. [Q9H2H8-2]
    NP_570981.1. NM_130906.2. [Q9H2H8-1]
    XP_005246708.1. XM_005246651.2. [Q9H2H8-2]
    XP_005246709.1. XM_005246652.2. [Q9H2H8-1]
    UniGeneiHs.121076.

    Genome annotation databases

    EnsembliENST00000286175; ENSP00000286175; ENSG00000240344. [Q9H2H8-2]
    ENST00000392283; ENSP00000376107; ENSG00000240344. [Q9H2H8-1]
    ENST00000409449; ENSP00000387012; ENSG00000240344. [Q9H2H8-2]
    GeneIDi53938.
    KEGGihsa:53938.
    UCSCiuc002uwh.3. human. [Q9H2H8-1]
    uc002uwi.3. human. [Q9H2H8-2]

    Polymorphism databases

    DMDMi73921766.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF251049 mRNA. Translation: AAK34939.1 .
    AF271652 mRNA. Translation: AAG44766.1 .
    AF146799 mRNA. Translation: AAO64723.1 .
    AK027315 mRNA. Translation: BAB55036.1 .
    AC005037 Genomic DNA. Translation: AAY14723.1 .
    BC007693 mRNA. Translation: AAH07693.1 .
    CCDSi CCDS2332.1. [Q9H2H8-2 ]
    CCDS2333.1. [Q9H2H8-1 ]
    RefSeqi NP_115861.1. NM_032472.3. [Q9H2H8-2 ]
    NP_570981.1. NM_130906.2. [Q9H2H8-1 ]
    XP_005246708.1. XM_005246651.2. [Q9H2H8-2 ]
    XP_005246709.1. XM_005246652.2. [Q9H2H8-1 ]
    UniGenei Hs.121076.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XYH X-ray 2.60 A 1-161 [» ]
    2OJU X-ray 2.40 A/B 1-161 [» ]
    2OK3 X-ray 2.00 A 1-161 [» ]
    ProteinModelPortali Q9H2H8.
    SMRi Q9H2H8. Positions 1-160.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119820. 19 interactions.
    IntActi Q9H2H8. 3 interactions.
    MINTi MINT-3063495.
    STRINGi 9606.ENSP00000286175.

    PTM databases

    PhosphoSitei Q9H2H8.

    Polymorphism databases

    DMDMi 73921766.

    Proteomic databases

    MaxQBi Q9H2H8.
    PaxDbi Q9H2H8.
    PRIDEi Q9H2H8.

    Protocols and materials databases

    DNASUi 53938.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286175 ; ENSP00000286175 ; ENSG00000240344 . [Q9H2H8-2 ]
    ENST00000392283 ; ENSP00000376107 ; ENSG00000240344 . [Q9H2H8-1 ]
    ENST00000409449 ; ENSP00000387012 ; ENSG00000240344 . [Q9H2H8-2 ]
    GeneIDi 53938.
    KEGGi hsa:53938.
    UCSCi uc002uwh.3. human. [Q9H2H8-1 ]
    uc002uwi.3. human. [Q9H2H8-2 ]

    Organism-specific databases

    CTDi 53938.
    GeneCardsi GC02M201737.
    HGNCi HGNC:9262. PPIL3.
    HPAi HPA040765.
    MIMi 615811. gene.
    neXtProti NX_Q9H2H8.
    PharmGKBi PA33589.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0652.
    HOGENOMi HOG000065981.
    HOVERGENi HBG001065.
    KOi K12734.
    OMAi CEMESRC.
    OrthoDBi EOG769ZKZ.
    PhylomeDBi Q9H2H8.
    TreeFami TF352224.

    Enzyme and pathway databases

    BRENDAi 5.2.1.8. 2681.

    Miscellaneous databases

    ChiTaRSi PPIL3. human.
    EvolutionaryTracei Q9H2H8.
    GeneWikii PPIL3.
    GenomeRNAii 53938.
    NextBioi 56240.
    PROi Q9H2H8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H2H8.
    Bgeei Q9H2H8.
    CleanExi HS_PPIL3.
    Genevestigatori Q9H2H8.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a novel peptidylprolyl isomerase (cyclophilin)-like gene (PPIL3) from human fetal brain."
      Zhou Z., Ying K., Dai J., Tang R., Wang W., Huang Y., Zhao W., Xie Y., Mao Y.
      Cytogenet. Cell Genet. 92:231-236(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    2. Ding J.B., Yu L., Zhao S.Y.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Embryo.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1), VARIANT GLU-146.
      Tissue: Placenta.
    6. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    7. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family."
      Huang L.-L., Zhao X.-M., Huang C.-Q., Yu L., Xia Z.-X.
      Acta Crystallogr. D 61:316-321(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

    Entry informationi

    Entry nameiPPIL3_HUMAN
    AccessioniPrimary (citable) accession number: Q9H2H8
    Secondary accession number(s): Q86WF9, Q96IA9, Q9BXZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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