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Q8IWE5

- PKHM2_HUMAN

UniProt

Q8IWE5 - PKHM2_HUMAN

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Protein
Pleckstrin homology domain-containing family M member 2
Gene
PLEKHM2, KIAA0842, SKIP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 2
PRO_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.1 Publication

Protein-protein interaction databases

DIPiDIP-46410N.
IntActiQ8IWE5. 1 interaction.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ8IWE5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 158123RUN
Add
BLAST
Domaini771 – 873103PH
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 310310Interaction with KIF5B
Add
BLAST
Regioni762 – 885124Interaction with sifA
Add
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.
Contains 1 RUN domain.

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.

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti600 – 6023VFR → ASG in AAH30545. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 91 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

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