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Q96JJ3

- ELMO2_HUMAN

UniProt

Q96JJ3 - ELMO2_HUMAN

Protein

Engulfment and cell motility protein 2

Gene

ELMO2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (16 May 2003)
      Previous versions | rss
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    Functioni

    Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. receptor tyrosine kinase binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell chemotaxis Source: UniProtKB
    3. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    4. innate immune response Source: Reactome
    5. phagocytosis Source: InterPro

    Keywords - Biological processi

    Apoptosis, Phagocytosis

    Enzyme and pathway databases

    ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Engulfment and cell motility protein 2
    Alternative name(s):
    Protein ced-12 homolog A
    Short name:
    hCed-12A
    Gene namesi
    Name:ELMO2
    Synonyms:CED12A, KIAA1834
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:17233. ELMO2.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytosol 1 Publication. Membrane 1 Publication

    GO - Cellular componenti

    1. cytoskeleton Source: InterPro
    2. cytosol Source: UniProtKB
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27755.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 720720Engulfment and cell motility protein 2PRO_0000153714Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481PhosphotyrosineBy similarity
    Modified residuei717 – 7171PhosphotyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96JJ3.
    PaxDbiQ96JJ3.
    PRIDEiQ96JJ3.

    PTM databases

    PhosphoSiteiQ96JJ3.

    Expressioni

    Tissue specificityi

    Widely expressed, with a higher expression in skeletal muscle, kidney and placenta.1 Publication

    Gene expression databases

    ArrayExpressiQ96JJ3.
    BgeeiQ96JJ3.
    GenevestigatoriQ96JJ3.

    Organism-specific databases

    HPAiHPA018811.

    Interactioni

    Subunit structurei

    Interacts with the SH3-domain of DOCK1 via its SH3-binding site. Probably part of a complex with DOCK1 and RAC1. Probably part of a complex with DOCK1 and CRK isoform CRK-II. Interacts with ARHGEF16, DOCK4 and EPHA2; mediates activation of RAC1 by EPHA2.2 Publications

    Protein-protein interaction databases

    BioGridi121987. 3 interactions.
    IntActiQ96JJ3. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96JJ3.
    SMRiQ96JJ3. Positions 523-717.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini311 – 485175ELMOPROSITE-ProRule annotationAdd
    BLAST
    Domaini553 – 674122PHAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi700 – 7078SH3-binding

    Sequence similaritiesi

    Contains 1 ELMO domain.PROSITE-ProRule annotation
    Contains 1 PH domain.Curated

    Keywords - Domaini

    SH3-binding

    Phylogenomic databases

    eggNOGiNOG295208.
    HOVERGENiHBG051463.
    InParanoidiQ96JJ3.
    OrthoDBiEOG7D85VW.
    PhylomeDBiQ96JJ3.
    TreeFamiTF312966.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR024574. DUF3361.
    IPR006816. Engulfment_cell_motility_ELMO.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF11841. DUF3361. 1 hit.
    PF04727. ELMO_CED12. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS51335. ELMO. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96JJ3-1) [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

    MPPPSDIVKV AIEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT    50
    LRYADGPQLY ITEQTRSDIK NGTILQLAIS PSRAARQLME RTQSSNMETR 100
    LDAMKELAKL SADVTFATEF INMDGIIVLT RLVESGTKLL SHYSEMLAFT 150
    LTAFLELMDH GIVSWDMVSI TFIKQIAGYV SQPMVDVSIL QRSLAILESM 200
    VLNSQSLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN ALFLKAPEDK 250
    RQDMANAFAQ KHLRSIILNH VIRGNRPIKT EMAHQLYVLQ VLTFNLLEER 300
    MMTKMDPNDQ AQRDIIFELR RIAFDAESDP SNAPGSGTEK RKAMYTKDYK 350
    MLGFTNHINP AMDFTQTPPG MLALDNMLYL AKVHQDTYIR IVLENSSRED 400
    KHECPFGRSA IELTKMLCEI LQVGELPNEG RNDYHPMFFT HDRAFEELFG 450
    ICIQLLNKTW KEMRATAEDF NKVMQVVREQ ITRALPSKPN SLDQFKSKLR 500
    SLSYSEILRL RQSERMSQDD FQSPPIVELR EKIQPEILEL IKQQRLNRLC 550
    EGSSFRKIGN RRRQERFWYC RLALNHKVLH YGDLDDNPQG EVTFESLQEK 600
    IPVADIKAIV TGKDCPHMKE KSALKQNKEV LELAFSILYD PDETLNFIAP 650
    NKYEYCIWID GLSALLGKDM SSELTKSDLD TLLSMEMKLR LLDLENIQIP 700
    EAPPPIPKEP SSYDFVYHYG 720
    Length:720
    Mass (Da):82,615
    Last modified:May 16, 2003 - v2
    Checksum:iA67377E3B26F2937
    GO
    Isoform 2 (identifier: Q96JJ3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-88: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:632
    Mass (Da):72,798
    Checksum:i066EE50A3A2B358A
    GO

    Sequence cautioni

    The sequence BAB13879.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB14210.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB14405.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB47463.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti208 – 2081Y → C in BAB71350. (PubMed:14702039)Curated
    Sequence conflicti299 – 2991E → G in BAB13879. (PubMed:14702039)Curated
    Sequence conflicti509 – 5091R → P in BAB13879. (PubMed:14702039)Curated
    Sequence conflicti586 – 5861D → N in BAB14210. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti695 – 6951E → D.
    Corresponds to variant rs34630674 [ dbSNP | Ensembl ].
    VAR_048928

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8888Missing in isoform 2. 1 PublicationVSP_055477Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF398886 Transcribed RNA. Translation: AAL14467.1.
    AF417861 mRNA. Translation: AAL38512.1.
    AB058737 mRNA. Translation: BAB47463.1. Different initiation.
    AK021718 mRNA. Translation: BAB13879.1. Different initiation.
    AK022731 mRNA. Translation: BAB14210.1. Different initiation.
    AK023103 mRNA. Translation: BAB14405.1. Different initiation.
    AK057032 mRNA. Translation: BAB71350.1.
    AL031686 Genomic DNA. No translation available.
    AL133227 Genomic DNA. Translation: CAI40561.1.
    CH471077 Genomic DNA. Translation: EAW75739.1.
    CH471077 Genomic DNA. Translation: EAW75743.1.
    CH471077 Genomic DNA. Translation: EAW75745.1.
    CH471077 Genomic DNA. Translation: EAW75746.1.
    BC000143 mRNA. Translation: AAH00143.2.
    CCDSiCCDS13398.1.
    RefSeqiNP_573403.1. NM_133171.3.
    NP_877496.1. NM_182764.1.
    XP_005260553.1. XM_005260496.1.
    XP_006723917.1. XM_006723854.1.
    UniGeneiHs.210469.

    Genome annotation databases

    EnsembliENST00000290246; ENSP00000290246; ENSG00000062598. [Q96JJ3-1]
    ENST00000372176; ENSP00000361249; ENSG00000062598. [Q96JJ3-3]
    ENST00000396391; ENSP00000379673; ENSG00000062598. [Q96JJ3-1]
    GeneIDi63916.
    KEGGihsa:63916.
    UCSCiuc002xrs.1. human.

    Polymorphism databases

    DMDMi30913107.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF398886 Transcribed RNA. Translation: AAL14467.1 .
    AF417861 mRNA. Translation: AAL38512.1 .
    AB058737 mRNA. Translation: BAB47463.1 . Different initiation.
    AK021718 mRNA. Translation: BAB13879.1 . Different initiation.
    AK022731 mRNA. Translation: BAB14210.1 . Different initiation.
    AK023103 mRNA. Translation: BAB14405.1 . Different initiation.
    AK057032 mRNA. Translation: BAB71350.1 .
    AL031686 Genomic DNA. No translation available.
    AL133227 Genomic DNA. Translation: CAI40561.1 .
    CH471077 Genomic DNA. Translation: EAW75739.1 .
    CH471077 Genomic DNA. Translation: EAW75743.1 .
    CH471077 Genomic DNA. Translation: EAW75745.1 .
    CH471077 Genomic DNA. Translation: EAW75746.1 .
    BC000143 mRNA. Translation: AAH00143.2 .
    CCDSi CCDS13398.1.
    RefSeqi NP_573403.1. NM_133171.3.
    NP_877496.1. NM_182764.1.
    XP_005260553.1. XM_005260496.1.
    XP_006723917.1. XM_006723854.1.
    UniGenei Hs.210469.

    3D structure databases

    ProteinModelPortali Q96JJ3.
    SMRi Q96JJ3. Positions 523-717.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121987. 3 interactions.
    IntActi Q96JJ3. 1 interaction.

    PTM databases

    PhosphoSitei Q96JJ3.

    Polymorphism databases

    DMDMi 30913107.

    Proteomic databases

    MaxQBi Q96JJ3.
    PaxDbi Q96JJ3.
    PRIDEi Q96JJ3.

    Protocols and materials databases

    DNASUi 63916.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290246 ; ENSP00000290246 ; ENSG00000062598 . [Q96JJ3-1 ]
    ENST00000372176 ; ENSP00000361249 ; ENSG00000062598 . [Q96JJ3-3 ]
    ENST00000396391 ; ENSP00000379673 ; ENSG00000062598 . [Q96JJ3-1 ]
    GeneIDi 63916.
    KEGGi hsa:63916.
    UCSCi uc002xrs.1. human.

    Organism-specific databases

    CTDi 63916.
    GeneCardsi GC20M044994.
    HGNCi HGNC:17233. ELMO2.
    HPAi HPA018811.
    MIMi 606421. gene.
    neXtProti NX_Q96JJ3.
    PharmGKBi PA27755.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295208.
    HOVERGENi HBG051463.
    InParanoidi Q96JJ3.
    OrthoDBi EOG7D85VW.
    PhylomeDBi Q96JJ3.
    TreeFami TF312966.

    Enzyme and pathway databases

    Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Miscellaneous databases

    GeneWikii ELMO2.
    GenomeRNAii 63916.
    NextBioi 65636.
    PROi Q96JJ3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96JJ3.
    Bgeei Q96JJ3.
    Genevestigatori Q96JJ3.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR024574. DUF3361.
    IPR006816. Engulfment_cell_motility_ELMO.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF11841. DUF3361. 1 hit.
    PF04727. ELMO_CED12. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS51335. ELMO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH DOCK1.
    2. "The C. elegans PH domain protein CED-12 regulates cytoskeletal reorganization via a Rho/Rac GTPase signaling pathway."
      Zhou Z., Caron E., Hartwieg E., Hall A., Horvitz H.R.
      Dev. Cell 1:477-489(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
      Tissue: Testis.
    3. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
      DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "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 1).
      Tissue: Embryo, Neuroepithelioma and Teratocarcinoma.
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 2).
      Tissue: Cervix.
    8. "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent mechanism."
      Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S., Negishi M., Katoh H.
      J. Cell Biol. 190:461-477(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARHGEF16; DOCK4 AND EPHA2, SUBCELLULAR LOCATION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiELMO2_HUMAN
    AccessioniPrimary (citable) accession number: Q96JJ3
    Secondary accession number(s): E1P5T3
    , Q5JVZ6, Q7Z5G9, Q96CJ2, Q96ME5, Q96PA9, Q9H938, Q9H9L5, Q9HAH0, Q9NQQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2003
    Last sequence update: May 16, 2003
    Last modified: October 1, 2014
    This is version 123 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 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3