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Q8IWE5 (PKHM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PLEKHM2
Synonyms:KIAA0842, SKIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1019 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

Interacts with KIF5B. Interacts with the S.typhimurium sifA protein; required for S.typhimurium infection. Ref.6

Subcellular location

Cytoplasm Ref.6.

Sequence similarities

Contains 1 PH domain.

Contains 1 RUN domain.

Sequence caution

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

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

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi organization

Inferred from mutant phenotype Ref.6. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionkinesin binding

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10191019Pleckstrin homology domain-containing family M member 2
PRO_0000309455

Regions

Domain36 – 158123RUN
Domain771 – 873103PH
Region1 – 310310Interaction with KIF5B
Region762 – 885124Interaction with sifA
Compositional bias317 – 3204Poly-Lys
Compositional bias323 – 3264Poly-Lys
Compositional bias506 – 5116Poly-Gly
Compositional bias593 – 5964Poly-Leu

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9

Natural variations

Natural variant321I → T.
Corresponds to variant rs12091750 [ dbSNP | Ensembl ].
VAR_036950

Experimental info

Mutagenesis8281G → D: Loss of interaction with sifA. Ref.10
Mutagenesis8301R → D: Loss of interaction with sifA. Ref.10
Mutagenesis8311R → A: Alters interaction with sifA. Ref.10
Mutagenesis8691C → D: Loss of interaction with sifA. Ref.10
Sequence conflict600 – 6023VFR → ASG in AAH30545. Ref.4

Secondary structure

..................... 1019
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8IWE5 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: FFD857F4C11BC0DB

FASTA1,019112,780
        10         20         30         40         50         60 
MEPGEVKDRI LENISLSVKK LQSYFAACED EIPAIRNHDK VLQRLCEHLD HALLYGLQDL 

        70         80         90        100        110        120 
SSGYWVLVVH FTRREAIKQI EVLQHVATNL GRSRAWLYLA LNENSLESYL RLFQENLGLL 

       130        140        150        160        170        180 
HKYYVKNALV CSHDHLTLFL TLVSGLEFIR FELDLDAPYL DLAPYMPDYY KPQYLLDFED 

       190        200        210        220        230        240 
RLPSSVHGSD SLSLNSFNSV TSTNLEWDDS AIAPSSEDYD FGDVFPAVPS VPSTDWEDGD 

       250        260        270        280        290        300 
LTDTVSGPRS TASDLTSSKA STRSPTQRQN PFNEEPAETV SSSDTTPVHT TSQEKEEAQA 

       310        320        330        340        350        360 
LDPPDACTEL EVIRVTKKKK IGKKKKSRSD EEASPLHPAC SQKKCAKQGD GDSRNGSPSL 

       370        380        390        400        410        420 
GRDSPDTMLA SPQEEGEGPS STTESSERSE PGLLIPEMKD TSMERLGQPL SKVIDQLNGQ 

       430        440        450        460        470        480 
LDPSTWCSRA EPPDQSFRTG SPGDAPERPP LCDFSEGLSA PMDFYRFTVE SPSTVTSGGG 

       490        500        510        520        530        540 
HHDPAGLGQP LHVPSSPEAA GQEEEGGGGE GQTPRPLEDT TREAQELEAQ LSLVREGPVS 

       550        560        570        580        590        600 
EPEPGTQEVL CQLKRDQPSP CLSSAEDSGV DEGQGSPSEM VHSSEFRVDN NHLLLLMIHV 

       610        620        630        640        650        660 
FRENEEQLFK MIRMSTGHME GNLQLLYVLL TDCYVYLLRK GATEKPYLVE EAVSYNELDY 

       670        680        690        700        710        720 
VSVGLDQQTV KLVCTNRRKQ FLLDTADVAL AEFFLASLKS AMIKGCREPP YPSILTDATM 

       730        740        750        760        770        780 
EKLALAKFVA QESKCEASAV TVRFYGLVHW EDPTDESLGP TPCHCSPPEG TITKEGMLHY 

       790        800        810        820        830        840 
KAGTSYLGKE HWKTCFVVLS NGILYQYPDR TDVIPLLSVN MGGEQCGGCR RANTTDRPHA 

       850        860        870        880        890        900 
FQVILSDRPC LELSAESEAE MAEWMQHLCQ AVSKGVIPQG VAPSPCIPCC LVLTDDRLFT 

       910        920        930        940        950        960 
CHEDCQTSFF RSLGTAKLGD ISAVSTEPGK EYCVLEFSQD SQQLLPPWVI YLSCTSELDR 

       970        980        990       1000       1010 
LLSALNSGWK TIYQVDLPHT AIQEASNKKK FEDALSLIHS AWQRSDSLCR GRASRDPWC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT46361.
RefSeqNP_055979.2. NM_015164.2.
UniGeneHs.646775.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CXBX-ray2.60B773-884[»]
3HW2X-ray3.30B771-875[»]
3ZFWX-ray2.90X/Y203-212[»]
ProteinModelPortalQ8IWE5.
SMRQ8IWE5. Positions 771-875.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46410N.
IntActQ8IWE5. 1 interaction.

PTM databases

PhosphoSiteQ8IWE5.

Polymorphism databases

DMDM160419243.

Proteomic databases

PaxDbQ8IWE5.
PRIDEQ8IWE5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375799; ENSP00000364956; ENSG00000116786.
GeneID23207.
KEGGhsa:23207.
UCSCuc010obo.2. human.

Organism-specific databases

CTD23207.
GeneCardsGC01P016008.
HGNCHGNC:29131. PLEKHM2.
HPAHPA032304.
MIM609613. gene.
neXtProtNX_Q8IWE5.
PharmGKBPA134888781.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41387.
HOVERGENHBG059073.
InParanoidQ8IWE5.
KOK15348.
OMAGILYQYP.
OrthoDBEOG7V765M.
PhylomeDBQ8IWE5.
TreeFamTF332641.

Gene expression databases

ArrayExpressQ8IWE5.
BgeeQ8IWE5.
GenevestigatorQ8IWE5.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR004012. Run.
[Graphical view]
PfamPF00169. PH. 1 hit.
PF02759. RUN. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00593. RUN. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50826. RUN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLEKHM2. human.
EvolutionaryTraceQ8IWE5.
GeneWikiPLEKHM2.
GenomeRNAi23207.
NextBio44735.
PROQ8IWE5.
SOURCESearch...

Entry information

Entry namePKHM2_HUMAN
AccessionPrimary (citable) accession number: Q8IWE5
Secondary accession number(s): O94928 expand/collapse secondary AC list , Q5VT65, Q6NUH9, Q7L8G1, Q8IVT7, Q8N2T4, Q96AY0, Q9NTF7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM