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Q8IWE5

- PKHM2_HUMAN

UniProt

Q8IWE5 - PKHM2_HUMAN

Protein

Pleckstrin homology domain-containing family M member 2

Gene

PLEKHM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    May play a role in the regulation of conventional kinesin activity. Required for maintenance of the Golgi apparatus organization. May play a role in membrane tubulation.1 Publication

    GO - Molecular functioni

    1. kinesin binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. Golgi organization Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pleckstrin homology domain-containing family M member 2
    Short name:
    PH domain-containing family M member 2
    Alternative name(s):
    Salmonella-induced filaments A and kinesin-interacting protein
    Short name:
    SifA and kinesin-interacting protein
    Gene namesi
    Name:PLEKHM2
    Synonyms:KIAA0842, SKIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:29131. PLEKHM2.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi828 – 8281G → D: Loss of interaction with sifA. 1 Publication
    Mutagenesisi830 – 8301R → D: Loss of interaction with sifA. 1 Publication
    Mutagenesisi831 – 8311R → A: Alters interaction with sifA. 1 Publication
    Mutagenesisi869 – 8691C → D: Loss of interaction with sifA. 1 Publication

    Organism-specific databases

    PharmGKBiPA134888781.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10191019Pleckstrin homology domain-containing family M member 2PRO_0000309455Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8IWE5.
    PaxDbiQ8IWE5.
    PRIDEiQ8IWE5.

    PTM databases

    PhosphoSiteiQ8IWE5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8IWE5.
    BgeeiQ8IWE5.
    GenevestigatoriQ8IWE5.

    Organism-specific databases

    HPAiHPA032304.

    Interactioni

    Subunit structurei

    Interacts with KIF5B. Interacts with the S.typhimurium sifA protein; required for S.typhimurium infection.2 Publications

    Protein-protein interaction databases

    DIPiDIP-46410N.
    IntActiQ8IWE5. 1 interaction.

    Structurei

    Secondary structure

    1
    1019
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni210 – 2123
    Beta strandi774 – 7807
    Beta strandi787 – 7893
    Beta strandi793 – 8008
    Beta strandi803 – 8119
    Beta strandi816 – 8205
    Beta strandi826 – 8316
    Beta strandi840 – 8456
    Beta strandi851 – 8544
    Helixi858 – 87215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CXBX-ray2.60B773-884[»]
    3HW2X-ray3.30B771-875[»]
    3ZFWX-ray2.90X/Y203-212[»]
    ProteinModelPortaliQ8IWE5.
    SMRiQ8IWE5. Positions 771-875.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IWE5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 158123RUNPROSITE-ProRule annotationAdd
    BLAST
    Domaini771 – 873103PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 310310Interaction with KIF5BAdd
    BLAST
    Regioni762 – 885124Interaction with sifAAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi317 – 3204Poly-Lys
    Compositional biasi323 – 3264Poly-Lys
    Compositional biasi506 – 5116Poly-Gly
    Compositional biasi593 – 5964Poly-Leu

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 RUN domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG41387.
    HOVERGENiHBG059073.
    InParanoidiQ8IWE5.
    KOiK15348.
    OMAiGILYQYP.
    OrthoDBiEOG7V765M.
    PhylomeDBiQ8IWE5.
    TreeFamiTF332641.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR004012. Run.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    PF02759. RUN. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00593. RUN. 1 hit.
    [Graphical view]
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS50826. RUN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8IWE5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPGEVKDRI LENISLSVKK LQSYFAACED EIPAIRNHDK VLQRLCEHLD     50
    HALLYGLQDL SSGYWVLVVH FTRREAIKQI EVLQHVATNL GRSRAWLYLA 100
    LNENSLESYL RLFQENLGLL HKYYVKNALV CSHDHLTLFL TLVSGLEFIR 150
    FELDLDAPYL DLAPYMPDYY KPQYLLDFED RLPSSVHGSD SLSLNSFNSV 200
    TSTNLEWDDS AIAPSSEDYD FGDVFPAVPS VPSTDWEDGD LTDTVSGPRS 250
    TASDLTSSKA STRSPTQRQN PFNEEPAETV SSSDTTPVHT TSQEKEEAQA 300
    LDPPDACTEL EVIRVTKKKK IGKKKKSRSD EEASPLHPAC SQKKCAKQGD 350
    GDSRNGSPSL GRDSPDTMLA SPQEEGEGPS STTESSERSE PGLLIPEMKD 400
    TSMERLGQPL SKVIDQLNGQ LDPSTWCSRA EPPDQSFRTG SPGDAPERPP 450
    LCDFSEGLSA PMDFYRFTVE SPSTVTSGGG HHDPAGLGQP LHVPSSPEAA 500
    GQEEEGGGGE GQTPRPLEDT TREAQELEAQ LSLVREGPVS EPEPGTQEVL 550
    CQLKRDQPSP CLSSAEDSGV DEGQGSPSEM VHSSEFRVDN NHLLLLMIHV 600
    FRENEEQLFK MIRMSTGHME GNLQLLYVLL TDCYVYLLRK GATEKPYLVE 650
    EAVSYNELDY VSVGLDQQTV KLVCTNRRKQ FLLDTADVAL AEFFLASLKS 700
    AMIKGCREPP YPSILTDATM EKLALAKFVA QESKCEASAV TVRFYGLVHW 750
    EDPTDESLGP TPCHCSPPEG TITKEGMLHY KAGTSYLGKE HWKTCFVVLS 800
    NGILYQYPDR TDVIPLLSVN MGGEQCGGCR RANTTDRPHA FQVILSDRPC 850
    LELSAESEAE MAEWMQHLCQ AVSKGVIPQG VAPSPCIPCC LVLTDDRLFT 900
    CHEDCQTSFF RSLGTAKLGD ISAVSTEPGK EYCVLEFSQD SQQLLPPWVI 950
    YLSCTSELDR LLSALNSGWK TIYQVDLPHT AIQEASNKKK FEDALSLIHS 1000
    AWQRSDSLCR GRASRDPWC 1019
    Length:1,019
    Mass (Da):112,780
    Last modified:November 13, 2007 - v2
    Checksum:iFFD857F4C11BC0DB
    GO

    Sequence cautioni

    The sequence AAH40441.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA74865.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti600 – 6023VFR → ASG in AAH30545. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321I → T.
    Corresponds to variant rs12091750 [ dbSNP | Ensembl ].
    VAR_036950

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020649 mRNA. Translation: BAA74865.1. Different initiation.
    AL450998, AL121992, AL606758 Genomic DNA. Translation: CAH70859.1.
    AL606758, AL121992, AL450998 Genomic DNA. Translation: CAH72017.1.
    AL121992, AL450998, AL606758 Genomic DNA. Translation: CAI22373.1.
    CH471167 Genomic DNA. Translation: EAW51745.1.
    BC008002 mRNA. Translation: AAH08002.1.
    BC016488 mRNA. Translation: AAH16488.1.
    BC030545 mRNA. Translation: AAH30545.1.
    BC040441 mRNA. Translation: AAH40441.1. Different initiation.
    BC042103 mRNA. Translation: AAH42103.1.
    AL137297 mRNA. Translation: CAB70684.1.
    CCDSiCCDS44063.1.
    PIRiT46361.
    RefSeqiNP_055979.2. NM_015164.2.
    UniGeneiHs.646775.

    Genome annotation databases

    EnsembliENST00000375799; ENSP00000364956; ENSG00000116786.
    GeneIDi23207.
    KEGGihsa:23207.
    UCSCiuc010obo.2. human.

    Polymorphism databases

    DMDMi160419243.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020649 mRNA. Translation: BAA74865.1 . Different initiation.
    AL450998 , AL121992 , AL606758 Genomic DNA. Translation: CAH70859.1 .
    AL606758 , AL121992 , AL450998 Genomic DNA. Translation: CAH72017.1 .
    AL121992 , AL450998 , AL606758 Genomic DNA. Translation: CAI22373.1 .
    CH471167 Genomic DNA. Translation: EAW51745.1 .
    BC008002 mRNA. Translation: AAH08002.1 .
    BC016488 mRNA. Translation: AAH16488.1 .
    BC030545 mRNA. Translation: AAH30545.1 .
    BC040441 mRNA. Translation: AAH40441.1 . Different initiation.
    BC042103 mRNA. Translation: AAH42103.1 .
    AL137297 mRNA. Translation: CAB70684.1 .
    CCDSi CCDS44063.1.
    PIRi T46361.
    RefSeqi NP_055979.2. NM_015164.2.
    UniGenei Hs.646775.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CXB X-ray 2.60 B 773-884 [» ]
    3HW2 X-ray 3.30 B 771-875 [» ]
    3ZFW X-ray 2.90 X/Y 203-212 [» ]
    ProteinModelPortali Q8IWE5.
    SMRi Q8IWE5. Positions 771-875.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-46410N.
    IntActi Q8IWE5. 1 interaction.

    PTM databases

    PhosphoSitei Q8IWE5.

    Polymorphism databases

    DMDMi 160419243.

    Proteomic databases

    MaxQBi Q8IWE5.
    PaxDbi Q8IWE5.
    PRIDEi Q8IWE5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375799 ; ENSP00000364956 ; ENSG00000116786 .
    GeneIDi 23207.
    KEGGi hsa:23207.
    UCSCi uc010obo.2. human.

    Organism-specific databases

    CTDi 23207.
    GeneCardsi GC01P016008.
    HGNCi HGNC:29131. PLEKHM2.
    HPAi HPA032304.
    MIMi 609613. gene.
    neXtProti NX_Q8IWE5.
    PharmGKBi PA134888781.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41387.
    HOVERGENi HBG059073.
    InParanoidi Q8IWE5.
    KOi K15348.
    OMAi GILYQYP.
    OrthoDBi EOG7V765M.
    PhylomeDBi Q8IWE5.
    TreeFami TF332641.

    Miscellaneous databases

    ChiTaRSi PLEKHM2. human.
    EvolutionaryTracei Q8IWE5.
    GeneWikii PLEKHM2.
    GenomeRNAii 23207.
    NextBioi 44735.
    PROi Q8IWE5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IWE5.
    Bgeei Q8IWE5.
    Genevestigatori Q8IWE5.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR004012. Run.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF02759. RUN. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00593. RUN. 1 hit.
    [Graphical view ]
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS50826. RUN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Bone, Cervix, Kidney, Ovary and Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 824-1019.
      Tissue: Testis.
    6. "The intracellular fate of Salmonella depends on the recruitment of kinesin."
      Boucrot E., Henry T., Borg J.-P., Gorvel J.-P., Meresse S.
      Science 308:1174-1178(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIF5B AND SALMONELLA TYPHIMURIUM SIFA PROTEIN.
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation."
      Ohlson M.B., Huang Z., Alto N.M., Blanc M.-P., Dixon J.E., Chai J., Miller S.I.
      Cell Host Microbe 4:434-446(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 773-884 IN COMPLEX WITH SALMONELLA TYPHIMURIUM SIFA PROTEIN, MUTAGENESIS OF GLY-828; ARG-830; ARG-831 AND CYS-869.

    Entry informationi

    Entry nameiPKHM2_HUMAN
    AccessioniPrimary (citable) accession number: Q8IWE5
    Secondary accession number(s): O94928
    , Q5VT65, Q6NUH9, Q7L8G1, Q8IVT7, Q8N2T4, Q96AY0, Q9NTF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 92 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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