SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O00562

- PITM1_HUMAN

UniProt

O00562 - PITM1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Membrane-associated phosphatidylinositol transfer protein 1
Gene
PITPNM1, DRES9, NIR2, PITPNM
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphatidylinositol transporter activity Source: ProtInc

GO - Biological processi

  1. brain development Source: ProtInc
  2. lipid metabolic process Source: ProtInc
  3. phospholipid transport Source: GOC
  4. phototransduction Source: ProtInc
  5. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PITPNM1
Synonyms:DRES9, NIR2, PITPNM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:9003. PITPNM1.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. Golgi cisterna membrane Source: UniProtKB-SubCell
  2. cleavage furrow Source: UniProtKB-SubCell
  3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  4. lipid particle Source: UniProtKB-SubCell
  5. membrane Source: ProtInc
  6. midbody Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Lipid droplet, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591T → A: Prevents association with lipid droplets. 1 Publication
Mutagenesisi59 – 591T → E: Causes association with lipid droplets. 1 Publication
Mutagenesisi287 – 2871T → 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. 1 Publication
Mutagenesisi300 – 3001S → A: No effect on phosphorylation. 1 Publication
Mutagenesisi326 – 3261S → A: No effect on phosphorylation. 1 Publication
Mutagenesisi349 – 3535EFFDA → ALLAG: Loss of interaction with VAPB. 1 Publication
Mutagenesisi382 – 3821S → A: Strongly reduced phosphorylation. 1 Publication
Mutagenesisi389 – 3891T → 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. 1 Publication
Mutagenesisi794 – 7941T → 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. 1 Publication
Mutagenesisi896 – 8961S → A: Reduced phosphorylation. 1 Publication
Mutagenesisi1223 – 12231T → 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. 1 Publication

Organism-specific databases

PharmGKBiPA33337.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12441244Membrane-associated phosphatidylinositol transfer protein 1
PRO_0000232738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591Phosphothreonine Inferred
Modified residuei287 – 2871Phosphothreonine; by CDK11 Publication
Modified residuei382 – 3821Phosphoserine; by CDK11 Publication
Modified residuei896 – 8961Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on multiple sites by CDK1 at the onset of mitosis. Phosphorylation facilitates dissociation from the Golgi complex and is required for interaction with PLK1.3 Publications
Phosphorylated on threonine residues upon treatment with oleic acid.3 Publications
Phosphorylated on tyrosine residues by PTK2B.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00562.
PaxDbiO00562.
PRIDEiO00562.

PTM databases

PhosphoSiteiO00562.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

ArrayExpressiO00562.
BgeeiO00562.
CleanExiHS_PITPNM1.
GenevestigatoriO00562.

Organism-specific databases

HPAiHPA060227.

Interactioni

Subunit structurei

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.4 Publications

Protein-protein interaction databases

BioGridi114965. 1 interaction.
IntActiO00562. 2 interactions.
STRINGi9606.ENSP00000348772.

Structurei

3D structure databases

ProteinModelPortaliO00562.
SMRiO00562. Positions 1-254.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini686 – 880195DDHD
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi310 – 31910Poly-Ser

Sequence similaritiesi

Contains 1 DDHD domain.

Phylogenomic databases

eggNOGiCOG5083.
HOGENOMiHOG000294231.
HOVERGENiHBG052733.
InParanoidiO00562.
OMAiMQNIARD.
OrthoDBiEOG7NW69J.
PhylomeDBiO00562.
TreeFamiTF312967.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
3.40.50.1000. 1 hit.
InterProiIPR004177. DDHD.
IPR023214. HAD-like_dom.
IPR013209. LNS2.
IPR001666. PI_transfer.
IPR023393. START-like_dom.
[Graphical view]
PANTHERiPTHR10658. PTHR10658. 1 hit.
PfamiPF02862. DDHD. 1 hit.
PF02121. IP_trans. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view]
PRINTSiPR00391. PITRANSFER.
SMARTiSM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
PROSITEiPS51043. DDHD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O00562-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MLIKEYHILL PMSLDEYQVA QLYMIQKKSR EESSGEGSGV EILANRPYTD     50
GPGGSGQYTH KVYHVGSHIP GWFRALLPKA ALQVEEESWN AYPYTRTRYT 100
CPFVEKFSIE IETYYLPDGG QQPNVFNLSG AERRQRILDT IDIVRDAVAP 150
GEYKAEEDPR LYHSVKTGRG PLSDDWARTA AQTGPLMCAY KLCKVEFRYW 200
GMQAKIEQFI HDVGLRRVML RAHRQAWCWQ DEWTELSMAD IRALEEETAR 250
MLAQRMAKCN TGSEGSEAQP PGKPSTEARS AASNTGTPDG PEAPPGPDAS 300
PDASFGKQWS SSSRSSYSSQ HGGAVSPQSL SEWRMQNIAR DSENSSEEEF 350
FDAHEGFSDS EEVFPKEMTK WNSNDFIDAF ASPVEAEGTP EPGAEAAKGI 400
EDGAQAPRDS EGLDGAGELG AEACAVHALF LILHSGNILD SGPGDANSKQ 450
ADVQTLSSAF EAVTRIHFPE ALGHVALRLV PCPPICAAAY ALVSNLSPYS 500
HDGDSLSRSQ DHIPLAALPL LATSSSRYQG AVATVIARTN QAYSAFLRSP 550
EGAGFCGQVA LIGDGVGGIL GFDALCHSAN AGTGSRGSSR RGSMNNELLS 600
PEFGPVRDPL ADGVEGLGRG SPEPSALPPQ RIPSDMASPE PEGSQNSLQA 650
APATTSSWEP RRASTAFCPP AASSEAPDGP SSTARLDFKV SGFFLFGSPL 700
GLVLALRKTV MPALEAAQMR PACEQIYNLF HAADPCASRL EPLLAPKFQA 750
IAPLTVPRYQ KFPLGDGSSL LLADTLQTHS SLFLEELEML VPSTPTSTSG 800
AFWKGSELAT DPPAQPAAPS TTSEVVKILE RWWGTKRIDY SLYCPEALTA 850
FPTVTLPHLF HASYWESADV VAFILRQVIE KERPQLAECE EPSIYSPAFP 900
REKWQRKRTQ VKIRNVTSNH RASDTVVCEG RPQVLSGRFM YGPLDVVTLT 950
GEKVDVYIMT QPLSGKWIHF GTEVTNSSGR LTFPVPPERA LGIGVYPVRM 1000
VVRGDHTYAE CCLTVVARGT EAVVFSIDGS FTASVSIMGS DPKVRAGAVD 1050
VVRHWQDSGY LIVYVTGRPD MQKHRVVAWL SQHNFPHGVV SFCDGLTHDP 1100
LRQKAMFLQS LVQEVELNIV AGYGSPKDVA VYAALGLSPS QTYIVGRAVR 1150
KLQAQCQFLS DGYVAHLGQL EAGSHSHASS GPPRAALGKS SYGVAAPVDF 1200
LRKQSQLLRS RGPSQAEREG PGTPPTTLAR GKARSISLKL DSEE 1244
Length:1,244
Mass (Da):134,848
Last modified:October 31, 2006 - v4
Checksum:iF4B66E98B085E9C0
GO
Isoform 2 (identifier: O00562-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,243
Mass (Da):134,777
Checksum:i6262539C57A79DA6
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei716 – 7161Missing in isoform 2.
VSP_021157

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti931 – 9311R → P in AAK01444. 1 Publication
Sequence conflicti1034 – 10341S → G in AAR06909. 1 Publication
Sequence conflicti1116 – 11161E → G in CAA67224. 1 Publication
Sequence conflicti1133 – 11331A → T in CAA67224. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31620.1. [O00562-1]
CCDS44659.1. [O00562-2]
RefSeqiNP_001124320.1. NM_001130848.1. [O00562-2]
NP_004901.2. NM_004910.2. [O00562-1]
UniGeneiHs.372295.

Genome annotation databases

EnsembliENST00000356404; ENSP00000348772; ENSG00000110697. [O00562-1]
ENST00000436757; ENSP00000398787; ENSG00000110697. [O00562-2]
ENST00000534749; ENSP00000437286; ENSG00000110697. [O00562-1]
GeneIDi9600.
KEGGihsa:9600.
UCSCiuc001olx.3. human. [O00562-1]
uc001olz.3. human. [O00562-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS31620.1. [O00562-1 ]
CCDS44659.1. [O00562-2 ]
RefSeqi NP_001124320.1. NM_001130848.1. [O00562-2 ]
NP_004901.2. NM_004910.2. [O00562-1 ]
UniGenei Hs.372295.

3D structure databases

ProteinModelPortali O00562.
SMRi O00562. Positions 1-254.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114965. 1 interaction.
IntActi O00562. 2 interactions.
STRINGi 9606.ENSP00000348772.

Chemistry

ChEMBLi CHEMBL1764937.

PTM databases

PhosphoSitei O00562.

Proteomic databases

MaxQBi O00562.
PaxDbi O00562.
PRIDEi O00562.

Protocols and materials databases

DNASUi 9600.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356404 ; ENSP00000348772 ; ENSG00000110697 . [O00562-1 ]
ENST00000436757 ; ENSP00000398787 ; ENSG00000110697 . [O00562-2 ]
ENST00000534749 ; ENSP00000437286 ; ENSG00000110697 . [O00562-1 ]
GeneIDi 9600.
KEGGi hsa:9600.
UCSCi uc001olx.3. human. [O00562-1 ]
uc001olz.3. human. [O00562-2 ]

Organism-specific databases

CTDi 9600.
GeneCardsi GC11M067260.
HGNCi HGNC:9003. PITPNM1.
HPAi HPA060227.
MIMi 608794. gene.
neXtProti NX_O00562.
PharmGKBi PA33337.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5083.
HOGENOMi HOG000294231.
HOVERGENi HBG052733.
InParanoidi O00562.
OMAi MQNIARD.
OrthoDBi EOG7NW69J.
PhylomeDBi O00562.
TreeFami TF312967.

Miscellaneous databases

ChiTaRSi PITPNM1. human.
GeneWikii PITPNM1.
GenomeRNAii 9600.
NextBioi 36015.
PROi O00562.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00562.
Bgeei O00562.
CleanExi HS_PITPNM1.
Genevestigatori O00562.

Family and domain databases

Gene3Di 3.30.530.20. 1 hit.
3.40.50.1000. 1 hit.
InterProi IPR004177. DDHD.
IPR023214. HAD-like_dom.
IPR013209. LNS2.
IPR001666. PI_transfer.
IPR023393. START-like_dom.
[Graphical view ]
PANTHERi PTHR10658. PTHR10658. 1 hit.
Pfami PF02862. DDHD. 1 hit.
PF02121. IP_trans. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view ]
PRINTSi PR00391. PITRANSFER.
SMARTi SM00775. LNS2. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
PROSITEi PS51043. DDHD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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. 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.

Entry informationi

Entry nameiPITM1_HUMAN
AccessioniPrimary (citable) accession number: O00562
Secondary accession number(s): A6NME4
, Q6T7X3, Q8TBN3, Q9BZ73
Entry historyi
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 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi