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Protein

Pleckstrin homology domain-containing family M member 2

Gene

PLEKHM2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29131. PLEKHM2.

Subcellular locationi

  1. 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.

Polymorphism and mutation databases

BioMutaiPLEKHM2.
DMDMi160419243.

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

BgeeiQ8IWE5.
ExpressionAtlasiQ8IWE5. baseline and differential.
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 – 2123Combined sources
Beta strandi774 – 7807Combined sources
Beta strandi787 – 7893Combined sources
Beta strandi793 – 8008Combined sources
Beta strandi803 – 8119Combined sources
Beta strandi816 – 8205Combined sources
Beta strandi826 – 8316Combined sources
Beta strandi840 – 8456Combined sources
Beta strandi851 – 8544Combined sources
Helixi858 – 87215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000015175.
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

        10         20         30         40         50
MEPGEVKDRI LENISLSVKK LQSYFAACED EIPAIRNHDK VLQRLCEHLD
60 70 80 90 100
HALLYGLQDL SSGYWVLVVH FTRREAIKQI EVLQHVATNL GRSRAWLYLA
110 120 130 140 150
LNENSLESYL RLFQENLGLL HKYYVKNALV CSHDHLTLFL TLVSGLEFIR
160 170 180 190 200
FELDLDAPYL DLAPYMPDYY KPQYLLDFED RLPSSVHGSD SLSLNSFNSV
210 220 230 240 250
TSTNLEWDDS AIAPSSEDYD FGDVFPAVPS VPSTDWEDGD LTDTVSGPRS
260 270 280 290 300
TASDLTSSKA STRSPTQRQN PFNEEPAETV SSSDTTPVHT TSQEKEEAQA
310 320 330 340 350
LDPPDACTEL EVIRVTKKKK IGKKKKSRSD EEASPLHPAC SQKKCAKQGD
360 370 380 390 400
GDSRNGSPSL GRDSPDTMLA SPQEEGEGPS STTESSERSE PGLLIPEMKD
410 420 430 440 450
TSMERLGQPL SKVIDQLNGQ LDPSTWCSRA EPPDQSFRTG SPGDAPERPP
460 470 480 490 500
LCDFSEGLSA PMDFYRFTVE SPSTVTSGGG HHDPAGLGQP LHVPSSPEAA
510 520 530 540 550
GQEEEGGGGE GQTPRPLEDT TREAQELEAQ LSLVREGPVS EPEPGTQEVL
560 570 580 590 600
CQLKRDQPSP CLSSAEDSGV DEGQGSPSEM VHSSEFRVDN NHLLLLMIHV
610 620 630 640 650
FRENEEQLFK MIRMSTGHME GNLQLLYVLL TDCYVYLLRK GATEKPYLVE
660 670 680 690 700
EAVSYNELDY VSVGLDQQTV KLVCTNRRKQ FLLDTADVAL AEFFLASLKS
710 720 730 740 750
AMIKGCREPP YPSILTDATM EKLALAKFVA QESKCEASAV TVRFYGLVHW
760 770 780 790 800
EDPTDESLGP TPCHCSPPEG TITKEGMLHY KAGTSYLGKE HWKTCFVVLS
810 820 830 840 850
NGILYQYPDR TDVIPLLSVN MGGEQCGGCR RANTTDRPHA FQVILSDRPC
860 870 880 890 900
LELSAESEAE MAEWMQHLCQ AVSKGVIPQG VAPSPCIPCC LVLTDDRLFT
910 920 930 940 950
CHEDCQTSFF RSLGTAKLGD ISAVSTEPGK EYCVLEFSQD SQQLLPPWVI
960 970 980 990 1000
YLSCTSELDR LLSALNSGWK TIYQVDLPHT AIQEASNKKK FEDALSLIHS
1010
AWQRSDSLCR GRASRDPWC
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. Curated
The sequence BAA74865.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiPLEKHM2.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

DIPiDIP-46410N.
IntActiQ8IWE5. 1 interaction.

PTM databases

PhosphoSiteiQ8IWE5.

Polymorphism and mutation databases

BioMutaiPLEKHM2.
DMDMi160419243.

Proteomic databases

MaxQBiQ8IWE5.
PaxDbiQ8IWE5.
PRIDEiQ8IWE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23207.
GeneCardsiGC01P016008.
HGNCiHGNC:29131. PLEKHM2.
HPAiHPA032304.
MIMi609613. gene.
neXtProtiNX_Q8IWE5.
PharmGKBiPA134888781.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41387.
GeneTreeiENSGT00390000015175.
HOVERGENiHBG059073.
InParanoidiQ8IWE5.
KOiK15348.
OMAiGILYQYP.
OrthoDBiEOG7V765M.
PhylomeDBiQ8IWE5.
TreeFamiTF332641.

Miscellaneous databases

EvolutionaryTraceiQ8IWE5.
GeneWikiiPLEKHM2.
GenomeRNAii23207.
NextBioi44735.
PROiQ8IWE5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IWE5.
ExpressionAtlasiQ8IWE5. baseline and differential.
GenevestigatoriQ8IWE5.

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]
ProtoNetiSearch...

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: April 29, 2015
This is version 96 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.