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P48739 (PIPNB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. 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:
Phosphatidylinositol transfer protein beta isoform

Short name=PI-TP-beta
Short name=PtdIns transfer protein beta
Short name=PtdInsTP beta
Gene names
Name:PITPNB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.

Subcellular location

Cytoplasm By similarity. Golgi apparatus By similarity.

Tissue specificity

Widely expressed in various tissues including brain.

Post-translational modification

Constitutive phosphorylation of Ser-262 has no effect on phospholipid transfer activity but is required for Golgi targeting By similarity.

Sequence similarities

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P48739-1)

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: P48739-2)

The sequence of this isoform differs from the canonical sequence as follows:
     257-271: MRKRGSVRGTSAADV → LRNQGQVRGTSAASDE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 271270Phosphatidylinositol transfer protein beta isoform
PRO_0000191643

Amino acid modifications

Modified residue2151N6-acetyllysine Ref.5
Modified residue2621Phosphoserine By similarity

Natural variations

Alternative sequence257 – 27115MRKRG…SAADV → LRNQGQVRGTSAASDE in isoform 2.
VSP_012762

Sequences

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

Last modified January 23, 2007. Version 2.
Checksum: AC5333FBC0F6CA06

FASTA27131,540
        10         20         30         40         50         60 
MVLIKEFRVV LPCSVQEYQV GQLYSVAEAS KNETGGGEGI EVLKNEPYEK DGEKGQYTHK 

        70         80         90        100        110        120 
IYHLKSKVPA FVRMIAPEGS LVFHEKAWNA YPYCRTIVTN EYMKDDFFIK IETWHKPDLG 

       130        140        150        160        170        180 
TLENVHGLDP NTWKTVEIVH IDIADRSQVE PADYKADEDP ALFQSVKTKR GPLGPNWKKE 

       190        200        210        220        230        240 
LANSPDCPQM CAYKLVTIKF KWWGLQSKVE NFIQKQEKRI FTNFHRQLFC WIDKWIDLTM 

       250        260        270 
EDIRRMEDET QKELETMRKR GSVRGTSAAD V 

« Hide

Isoform 2 [UniParc].

Checksum: 05142EA9F80BA7CB
Show »

FASTA27231,638

References

« Hide 'large scale' references
[1]"Cloning and expression of human cDNA encoding phosphatidylinositol transfer protein beta."
Tanaka S., Yamashita S., Hosaka K.
Biochim. Biophys. Acta 1259:199-202(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORMS 1 AND 2).
Tissue: Lymph and Skin.
[5]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30037 mRNA. Translation: BAA06277.1.
CR456541 mRNA. Translation: CAG30427.1.
AL031591 Genomic DNA. Translation: CAB63033.1.
AL031591 Genomic DNA. Translation: CAQ68296.1.
BC018704 mRNA. Translation: AAH18704.1.
BC031427 mRNA. Translation: AAH31427.1.
RefSeqNP_001271206.1. NM_001284277.1.
NP_001271207.1. NM_001284278.1.
NP_036531.1. NM_012399.4.
UniGeneHs.705323.

3D structure databases

ProteinModelPortalP48739.
SMRP48739. Positions 2-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117261. 4 interactions.
IntActP48739. 1 interaction.
MINTMINT-5002601.
STRING9606.ENSP00000334738.

PTM databases

PhosphoSiteP48739.

Polymorphism databases

DMDM1346772.

Proteomic databases

PaxDbP48739.
PRIDEP48739.

Protocols and materials databases

DNASU23760.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320996; ENSP00000321266; ENSG00000180957. [P48739-2]
ENST00000335272; ENSP00000334738; ENSG00000180957. [P48739-1]
GeneID23760.
KEGGhsa:23760.
UCSCuc003adk.3. human. [P48739-1]
uc003adl.3. human. [P48739-2]

Organism-specific databases

CTD23760.
GeneCardsGC22M028202.
HGNCHGNC:9002. PITPNB.
HPAHPA000528.
MIM606876. gene.
neXtProtNX_P48739.
PharmGKBPA33336.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250489.
HOVERGENHBG058915.
OrthoDBEOG7PGDRB.
PhylomeDBP48739.
TreeFamTF313279.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP48739.
BgeeP48739.
CleanExHS_PITPNB.
GenevestigatorP48739.

Family and domain databases

Gene3D3.30.530.20. 1 hit.
InterProIPR001666. PI_transfer.
IPR023393. START-like_dom.
[Graphical view]
PANTHERPTHR10658. PTHR10658. 1 hit.
PfamPF02121. IP_trans. 1 hit.
[Graphical view]
PRINTSPR00391. PITRANSFER.
ProtoNetSearch...

Other

ChiTaRSPITPNB. human.
GeneWikiPITPNB.
GenomeRNAi23760.
NextBio46707.
PROP48739.
SOURCESearch...

Entry information

Entry namePIPNB_HUMAN
AccessionPrimary (citable) accession number: P48739
Secondary accession number(s): B3KYB8, Q8N5W1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 123 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

MIM cross-references

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

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM