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O00562 (PITM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Membrane-associated phosphatidylinositol transfer protein 1
Alternative name(s):
Drosophila retinal degeneration B homolog
Phosphatidylinositol transfer protein, membrane-associated 1
Short name=PITPnm 1
Pyk2 N-terminal domain-interacting receptor 2
Short name=NIR-2
Gene names
Name:PITPNM1
Synonyms:DRES9, NIR2, PITPNM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1244 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates RHOA activity, and plays a role in cytoskeleton remodeling. Necessary for normal completion of cytokinesis. Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Binds phosphatidyl inositol phosphates (in vitro). May catalyze the transfer of phosphatidylinositol and phosphatidylcholine between membranes By similarity. Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi. Binds calcium ions. Ref.2 Ref.8 Ref.10 Ref.11

Subunit structure

Interacts with PIK4CA By similarity. Interacts with PTK2B via its C-terminus. Interacts with RHOA. Has higher affinity for the inactive, GDP-bound form of RHOA. The CDK1-phosphorylated form interacts with PLK1. Interacts with VAPB. Ref.2 Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm. Golgi apparatusGolgi stack membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Lipid droplet. Cleavage furrow. Midbody. Note: Peripheral membrane protein associated with Golgi stacks in interphase cells. A minor proportion is associated with the endoplasmic reticulum. Associated with lipid droplets. Dissociates from the Golgi early on in mitosis and localizes to the cleavage furrow and midbody during cytokinesis. Ref.7 Ref.9

Tissue specificity

Ubiquitous. Ref.2

Post-translational modification

Phosphorylated on multiple sites by CDK1 at the onset of mitosis. Phosphorylation facilitates dissociation from the Golgi complex and is required for interaction with PLK1. Ref.2 Ref.7 Ref.9

Phosphorylated on threonine residues upon treatment with oleic acid. Ref.2 Ref.7 Ref.9

Phosphorylated on tyrosine residues by PTK2B. Ref.2 Ref.7 Ref.9

Sequence similarities

Belongs to the PtdIns transfer protein family. PI transfer class IIA subfamily.

Contains 1 DDHD domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00562-1)

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.
Isoform 2 (identifier: O00562-2)

The sequence of this isoform differs from the canonical sequence as follows:
     716-716: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12441244Membrane-associated phosphatidylinositol transfer protein 1
PRO_0000232738

Regions

Domain686 – 880195DDHD
Compositional bias310 – 31910Poly-Ser

Amino acid modifications

Modified residue591Phosphothreonine Probable
Modified residue2871Phosphothreonine; by CDK1 Ref.9
Modified residue3821Phosphoserine; by CDK1 Ref.9
Modified residue8961Phosphoserine Ref.9

Natural variations

Alternative sequence7161Missing in isoform 2.
VSP_021157

Experimental info

Mutagenesis591T → A: Prevents association with lipid droplets. Ref.7
Mutagenesis591T → E: Causes association with lipid droplets. Ref.7
Mutagenesis2871T → A: Slightly reduced phosphorylation. Strongly reduced phosphorylation; when associated with A-794 or A-389. Loss of threonine phosphorylation; when associated with A-389; A-793 and A-1222. Ref.9
Mutagenesis3001S → A: No effect on phosphorylation. Ref.9
Mutagenesis3261S → A: No effect on phosphorylation. Ref.9
Mutagenesis349 – 3535EFFDA → ALLAG: Loss of interaction with VAPB. Ref.10
Mutagenesis3821S → A: Strongly reduced phosphorylation. Ref.9
Mutagenesis3891T → A: No detectable effect on phosphorylation; when associated with A-793 and A-1222. Strongly reduced phosphorylation; when associated with A-287. Loss of threonine phosphorylation; when associated with A-287; A-794 and A-1222. Ref.9
Mutagenesis7941T → A: No detectable effect on phosphorylation; when associated with A-389 and A-1222. Strongly reduced phosphorylation; when associated with A-287. Loss of threonine phosphorylation; when associated with A-287; A-389 and A-1222. Ref.9
Mutagenesis8961S → A: Reduced phosphorylation. Ref.9
Mutagenesis12231T → A: No detectable effect on phosphorylation; when associated with A-389 and A-793. Loss of threonine phosphorylation; when associated with A-287; A-389 and A-794. Ref.9
Sequence conflict9311R → P in AAK01444. Ref.2
Sequence conflict10341S → G in AAR06909. Ref.3
Sequence conflict11161E → G in CAA67224. Ref.1
Sequence conflict11331A → T in CAA67224. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 31, 2006. Version 4.
Checksum: F4B66E98B085E9C0

FASTA1,244134,848
        10         20         30         40         50         60 
MLIKEYHILL PMSLDEYQVA QLYMIQKKSR EESSGEGSGV EILANRPYTD GPGGSGQYTH 

        70         80         90        100        110        120 
KVYHVGSHIP GWFRALLPKA ALQVEEESWN AYPYTRTRYT CPFVEKFSIE IETYYLPDGG 

       130        140        150        160        170        180 
QQPNVFNLSG AERRQRILDT IDIVRDAVAP GEYKAEEDPR LYHSVKTGRG PLSDDWARTA 

       190        200        210        220        230        240 
AQTGPLMCAY KLCKVEFRYW GMQAKIEQFI HDVGLRRVML RAHRQAWCWQ DEWTELSMAD 

       250        260        270        280        290        300 
IRALEEETAR MLAQRMAKCN TGSEGSEAQP PGKPSTEARS AASNTGTPDG PEAPPGPDAS 

       310        320        330        340        350        360 
PDASFGKQWS SSSRSSYSSQ HGGAVSPQSL SEWRMQNIAR DSENSSEEEF FDAHEGFSDS 

       370        380        390        400        410        420 
EEVFPKEMTK WNSNDFIDAF ASPVEAEGTP EPGAEAAKGI EDGAQAPRDS EGLDGAGELG 

       430        440        450        460        470        480 
AEACAVHALF LILHSGNILD SGPGDANSKQ ADVQTLSSAF EAVTRIHFPE ALGHVALRLV 

       490        500        510        520        530        540 
PCPPICAAAY ALVSNLSPYS HDGDSLSRSQ DHIPLAALPL LATSSSRYQG AVATVIARTN 

       550        560        570        580        590        600 
QAYSAFLRSP EGAGFCGQVA LIGDGVGGIL GFDALCHSAN AGTGSRGSSR RGSMNNELLS 

       610        620        630        640        650        660 
PEFGPVRDPL ADGVEGLGRG SPEPSALPPQ RIPSDMASPE PEGSQNSLQA APATTSSWEP 

       670        680        690        700        710        720 
RRASTAFCPP AASSEAPDGP SSTARLDFKV SGFFLFGSPL GLVLALRKTV MPALEAAQMR 

       730        740        750        760        770        780 
PACEQIYNLF HAADPCASRL EPLLAPKFQA IAPLTVPRYQ KFPLGDGSSL LLADTLQTHS 

       790        800        810        820        830        840 
SLFLEELEML VPSTPTSTSG AFWKGSELAT DPPAQPAAPS TTSEVVKILE RWWGTKRIDY 

       850        860        870        880        890        900 
SLYCPEALTA FPTVTLPHLF HASYWESADV VAFILRQVIE KERPQLAECE EPSIYSPAFP 

       910        920        930        940        950        960 
REKWQRKRTQ VKIRNVTSNH RASDTVVCEG RPQVLSGRFM YGPLDVVTLT GEKVDVYIMT 

       970        980        990       1000       1010       1020 
QPLSGKWIHF GTEVTNSSGR LTFPVPPERA LGIGVYPVRM VVRGDHTYAE CCLTVVARGT 

      1030       1040       1050       1060       1070       1080 
EAVVFSIDGS FTASVSIMGS DPKVRAGAVD VVRHWQDSGY LIVYVTGRPD MQKHRVVAWL 

      1090       1100       1110       1120       1130       1140 
SQHNFPHGVV SFCDGLTHDP LRQKAMFLQS LVQEVELNIV AGYGSPKDVA VYAALGLSPS 

      1150       1160       1170       1180       1190       1200 
QTYIVGRAVR KLQAQCQFLS DGYVAHLGQL EAGSHSHASS GPPRAALGKS SYGVAAPVDF 

      1210       1220       1230       1240 
LRKQSQLLRS RGPSQAEREG PGTPPTTLAR GKARSISLKL DSEE 

« Hide

Isoform 2 [UniParc].

Checksum: 6262539C57A79DA6
Show »

FASTA1,243134,777

References

« Hide 'large scale' references
[1]"A mammalian homologue of the Drosophila retinal degeneration B gene: implications for the evolution of phototransduction mechanisms."
Rubboli F., Bulfone A., Bogni S., Marchitiello A., Zollo M., Borsani G., Ballabio A., Banfi S.
Genes Funct. 1:205-213(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein."
Lev S., Hernandez J., Martinez R., Chen A., Plowman G., Schlessinger J.
Mol. Cell. Biol. 19:2278-2288(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CALCIUM-BINDING, INTERACTION WITH PTK2B, PHOSPHORYLATION, TISSUE SPECIFICITY.
Tissue: Brain.
[3]"Chromosomal localization, genomic organization and evolution of the genes encoding human phosphatidylinositol transfer protein membrane-associated (PITPNM) 1, 2 and 3."
Ocaka L., Spalluto C., Wilson D.I., Hunt D.M., Halford S.
Cytogenet. Genome Res. 108:293-302(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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: Duodenum.
[7]"Targeting of Nir2 to lipid droplets is regulated by a specific threonine residue within its PI-transfer domain."
Litvak V., Shaul Y.D., Shulewitz M., Amarilio R., Carmon S., Lev S.
Curr. Biol. 12:1513-1518(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF THR-59, PHOSPHORYLATION AT THR-59.
[8]"Nir2, a novel regulator of cell morphogenesis."
Tian D., Litvak V., Toledo-Rodriguez M., Carmon S., Lev S.
Mol. Cell. Biol. 22:2650-2662(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RHOA.
[9]"Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion."
Litvak V., Argov R., Dahan N., Ramachandran S., Amarilio R., Shainskaya A., Lev S.
Mol. Cell 14:319-330(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-287; SER-382 AND SER-896, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF THR-287; SER-300; SER-326; SER-382; THR-389; THR-794; SER-896 AND THR-1223, INTERACTION WITH CDK1 AND PLK1, SUBCELLULAR LOCATION.
[10]"Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction."
Amarilio R., Ramachandran S., Sabanay H., Lev S.
J. Biol. Chem. 280:5934-5944(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VAPB, MUTAGENESIS OF 349-GLU--ALA-353.
[11]"Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function."
Litvak V., Dahan N., Ramachandran S., Sabanay H., Lev S.
Nat. Cell Biol. 7:225-234(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98654 mRNA. Translation: CAA67224.1.
AF334584 mRNA. Translation: AAK01444.1.
AY429102 mRNA. Translation: AAR06909.1.
AP001184 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74638.1.
BC022230 mRNA. Translation: AAH22230.1.
CCDSCCDS31620.1. [O00562-1]
CCDS44659.1. [O00562-2]
RefSeqNP_001124320.1. NM_001130848.1. [O00562-2]
NP_004901.2. NM_004910.2. [O00562-1]
UniGeneHs.372295.

3D structure databases

ProteinModelPortalO00562.
SMRO00562. Positions 1-254.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114965. 1 interaction.
IntActO00562. 2 interactions.
STRING9606.ENSP00000348772.

Chemistry

ChEMBLCHEMBL1764937.

PTM databases

PhosphoSiteO00562.

Proteomic databases

MaxQBO00562.
PaxDbO00562.
PRIDEO00562.

Protocols and materials databases

DNASU9600.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356404; ENSP00000348772; ENSG00000110697. [O00562-1]
ENST00000436757; ENSP00000398787; ENSG00000110697. [O00562-2]
ENST00000534749; ENSP00000437286; ENSG00000110697. [O00562-1]
GeneID9600.
KEGGhsa:9600.
UCSCuc001olx.3. human. [O00562-1]
uc001olz.3. human. [O00562-2]

Organism-specific databases

CTD9600.
GeneCardsGC11M067260.
HGNCHGNC:9003. PITPNM1.
HPAHPA060227.
MIM608794. gene.
neXtProtNX_O00562.
PharmGKBPA33337.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5083.
HOGENOMHOG000294231.
HOVERGENHBG052733.
InParanoidO00562.
OMAMQNIARD.
OrthoDBEOG7NW69J.
PhylomeDBO00562.
TreeFamTF312967.

Gene expression databases

ArrayExpressO00562.
BgeeO00562.
CleanExHS_PITPNM1.
GenevestigatorO00562.

Family and domain databases

Gene3D3.30.530.20. 1 hit.
3.40.50.1000. 1 hit.
InterProIPR004177. DDHD.
IPR023214. HAD-like_dom.
IPR013209. LNS2.
IPR001666. PI_transfer.
IPR023393. START-like_dom.
[Graphical view]
PANTHERPTHR10658. PTHR10658. 1 hit.
PfamPF02862. DDHD. 1 hit.
PF02121. IP_trans. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view]
PRINTSPR00391. PITRANSFER.
SMARTSM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
PROSITEPS51043. DDHD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPITPNM1. human.
GeneWikiPITPNM1.
GenomeRNAi9600.
NextBio36015.
PROO00562.
SOURCESearch...

Entry information

Entry namePITM1_HUMAN
AccessionPrimary (citable) accession number: O00562
Secondary accession number(s): A6NME4 expand/collapse secondary AC list , Q6T7X3, Q8TBN3, Q9BZ73
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: October 31, 2006
Last modified: July 9, 2014
This is version 109 of the entry and version 4 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

MIM cross-references

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

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM