Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P22307 (NLTP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Non-specific lipid-transfer protein

Short name=NSL-TP
EC=2.3.1.176
Alternative name(s):
Propanoyl-CoA C-acyltransferase
SCP-chi
SCPX
Sterol carrier protein 2
Short name=SCP-2
Sterol carrier protein X
Short name=SCP-X
Gene names
Name:SCP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis. Ref.14 Ref.18

Catalytic activity

3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3-alpha,7-alpha,12-alpha-trihydroxy-24-oxo-5-beta-cholestanoyl-CoA.

Subunit structure

Interacts with PEX5.

Subcellular location

Cytoplasm. Mitochondrion. Note: Cytoplasmic in the liver and also associated with mitochondria especially in steroidogenic tissues. Ref.18

Isoform SCPx: Peroxisome. Note: Interaction with PEX5 is essential for peroxisomal import. Ref.18

Isoform SCP2: Mitochondrion Probable Ref.18.

Tissue specificity

Liver, fibroblasts, and placenta.

Induction

Up-regulated by 4-hydroxy-tamoxifen. Ref.12

Involvement in disease

Leukoencephalopathy, with dystonia and motor neuropathy (LDMN) [MIM:613724]: A syndrome characterized by leukoencephalopathy, dystonic head tremor, spasmodic torticollis and reduced tendon reflexes in lower extremities. Additional features include hyposmia, pathologic saccadic eye movements, a slight hypoacusis, accumulation of branched-chain pristanic acid in plasma, and the presence of abnormal bile alcohol glucuronides in urine.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

In the N-terminal section; belongs to the thiolase family.

Contains 1 SCP2 domain.

Sequence caution

The sequence AAA03558.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentCytoplasm
Mitochondrion
Peroxisome
   Coding sequence diversityAlternative initiation
Alternative promoter usage
Alternative splicing
Polymorphism
   LigandLipid-binding
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processalpha-linolenic acid metabolic process

Traceable author statement. Source: Reactome

bile acid biosynthetic process

Traceable author statement. Source: Reactome

bile acid metabolic process

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

fatty acid beta-oxidation using acyl-CoA oxidase

Traceable author statement. Source: Reactome

inositol trisphosphate biosynthetic process

Inferred from direct assay PubMed 12641450. Source: UniProtKB

lipid hydroperoxide transport

Inferred from direct assay PubMed 15449949. Source: UniProtKB

lipid transport

Inferred from electronic annotation. Source: UniProtKB-KW

peroxisome organization

Inferred from electronic annotation. Source: Ensembl

phospholipid transport

Inferred from direct assay PubMed 12641450. Source: UniProtKB

positive regulation of intracellular cholesterol transport

Inferred from direct assay PubMed 15449949. Source: UniProtKB

positive regulation of steroid metabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

progesterone biosynthetic process

Inferred from direct assay Ref.3. Source: UniProtKB

protein localization to plasma membrane

Inferred from direct assay PubMed 12641450. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid biosynthetic process

Inferred from direct assay Ref.3. Source: UniProtKB

unsaturated fatty acid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

peroxisomal matrix

Traceable author statement. Source: Reactome

peroxisome

Inferred from direct assay PubMed 1347505PubMed 21375735. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 19584060. Source: UniProtKB

   Molecular_functioncholesterol binding

Inferred from direct assay PubMed 18465878. Source: UniProtKB

fatty-acyl-CoA binding

Inferred from direct assay PubMed 18465878. Source: UniProtKB

long-chain fatty acyl-CoA binding

Inferred from direct assay PubMed 17418802. Source: UniProtKB

oleic acid binding

Inferred from direct assay PubMed 18465878. Source: UniProtKB

phosphatidylinositol transporter activity

Inferred from direct assay PubMed 12641450. Source: UniProtKB

propanoyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction PubMed 19584060. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365PubMed 21375735. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CAV1Q031353EBI-1050999,EBI-603614
Cav1P498173EBI-1050999,EBI-1161338From a different organism.

Alternative products

This entry describes 8 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform SCPx (identifier: P22307-1)

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 SCP2 (identifier: P22307-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-404: Missing.
Note: Contains a mitochondrial transit peptide at positions 1-20 (Potential).
Isoform 3 (identifier: P22307-3)

The sequence of this isoform differs from the canonical sequence as follows:
     67-110: Missing.
     362-547: LAQCAELCWQ...LQLQPGNAKL → GHSCS
Isoform 4 (identifier: P22307-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
Note: Produced by alternative splicing. No experimental confirmation available.
Isoform 5 (identifier: P22307-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-404: Missing.
     447-463: EGEQFVKKIGGIFAFKV → IRRLTAQSQWLTQTSWL
     464-547: Missing.
Isoform 6 (identifier: P22307-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-404: Missing.
     412-414: Missing.
Isoform 7 (identifier: P22307-7)

The sequence of this isoform differs from the canonical sequence as follows:
     67-110: Missing.
Note: Produced by alternative splicing.
Isoform 8 (identifier: P22307-8)

The sequence of this isoform differs from the canonical sequence as follows:
     43-66: Missing.
Note: Produced by alternative splicing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 547547Non-specific lipid-transfer protein
PRO_0000034091

Regions

Domain433 – 543111SCP2
Motif545 – 5473Microbody targeting signal Potential

Amino acid modifications

Modified residue1321N6-acetyllysine; alternate By similarity
Modified residue1321N6-succinyllysine; alternate By similarity
Modified residue1681N6-succinyllysine By similarity
Modified residue1731N6-acetyllysine By similarity
Modified residue1771N6-acetyllysine By similarity
Modified residue1831N6-acetyllysine; alternate Ref.15
Modified residue1831N6-succinyllysine; alternate By similarity
Modified residue2821N6-succinyllysine By similarity
Modified residue3411N6-acetyllysine; alternate By similarity
Modified residue3411N6-succinyllysine; alternate By similarity
Modified residue4321N6-acetyllysine; alternate By similarity
Modified residue4321N6-succinyllysine; alternate By similarity
Modified residue4381N6-acetyllysine; alternate Ref.15
Modified residue4381N6-succinyllysine; alternate By similarity
Modified residue4431N6-acetyllysine; alternate By similarity
Modified residue4431N6-succinyllysine; alternate By similarity
Modified residue4531N6-acetyllysine; alternate By similarity
Modified residue4531N6-succinyllysine; alternate By similarity
Modified residue4641N6-succinyllysine By similarity
Modified residue4701N6-acetyllysine; alternate Ref.15
Modified residue4701N6-succinyllysine; alternate By similarity
Modified residue4791N6-succinyllysine By similarity
Modified residue4911N6-acetyllysine By similarity
Modified residue4921N6-succinyllysine By similarity
Modified residue5111N6-succinyllysine By similarity
Modified residue5161Phosphoserine By similarity
Modified residue5221N6-succinyllysine By similarity
Modified residue5341N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 404404Missing in isoform SCP2, isoform 5 and isoform 6.
VSP_018977
Alternative sequence1 – 8181Missing in isoform 4.
VSP_045187
Alternative sequence43 – 6624Missing in isoform 8.
VSP_047267
Alternative sequence67 – 11044Missing in isoform 3 and isoform 7.
VSP_042686
Alternative sequence362 – 547186LAQCA…GNAKL → GHSCS in isoform 3.
VSP_042687
Alternative sequence412 – 4143Missing in isoform 6.
VSP_047268
Alternative sequence447 – 46317EGEQF…FAFKV → IRRLTAQSQWLTQTSWL in isoform 5.
VSP_047269
Alternative sequence464 – 54784Missing in isoform 5.
VSP_047270
Natural variant1551A → D in a breast cancer sample; somatic mutation. Ref.19
VAR_035706

Experimental info

Mutagenesis5281N → D: Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-530. Ref.14
Mutagenesis5281N → I: Strongly reduces sterol carrier and phosphatidylcholine transfer activity. Ref.14
Mutagenesis5301G → D: Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-528. Ref.14
Sequence conflict101T → A in AAB41286. Ref.1
Sequence conflict561A → V in AK308105. Ref.5
Sequence conflict1161V → A in AK308105. Ref.5
Sequence conflict3411K → Q in BAG57810. Ref.5
Sequence conflict3931G → D in AAB41286. Ref.1
Sequence conflict4721A → D in AAB24921. Ref.4
Sequence conflict4821K → Q in AAB24921. Ref.4
Sequence conflict5011D → A in AAB24921. Ref.4
Sequence conflict5221K → P in AAB24921. Ref.4

Secondary structure

........................ 547
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1997. Version 2.
Checksum: 29F7551465C7143A

FASTA54758,994
        10         20         30         40         50         60 
MSSSPWEPAT LRRVFVVGVG MTKFVKPGAE NSRDYPDLAE EAGKKALADA QIPYSAVDQA 

        70         80         90        100        110        120 
CVGYVFGDST CGQRAIYHSL GMTGIPIINV NNNCATGSTA LFMARQLIQG GVAECVLALG 

       130        140        150        160        170        180 
FEKMSKGSLG IKFSDRTIPT DKHVDLLINK YGLSAHPVAP QMFGYAGKEH MEKYGTKIEH 

       190        200        210        220        230        240 
FAKIGWKNHK HSVNNPYSQF QDEYSLDEVM ASKEVFDFLT ILQCCPTSDG AAAAILASEA 

       250        260        270        280        290        300 
FVQKYGLQSK AVEILAQEMM TDLPSSFEEK SIIKMVGFDM SKEAARKCYE KSGLTPNDID 

       310        320        330        340        350        360 
VIELHDCFST NELLTYEALG LCPEGQGATL VDRGDNTYGG KWVINPSGGL ISKGHPLGAT 

       370        380        390        400        410        420 
GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGIGGAVVV TLYKMGFPEA ASSFRTHQIE 

       430        440        450        460        470        480 
AVPTSSASDG FKANLVFKEI EKKLEEEGEQ FVKKIGGIFA FKVKDGPGGK EATWVVDVKN 

       490        500        510        520        530        540 
GKGSVLPNSD KKADCTITMA DSDFLALMTG KMNPQSAFFQ GKLKITGNMG LAMKLQNLQL 


QPGNAKL 

« Hide

Isoform SCP2 [UniParc].

Checksum: DE7FD93BB320BB30
Show »

FASTA14315,401
Isoform 3 [UniParc].

Checksum: FC4864F7E46C77F7
Show »

FASTA32234,975
Isoform 4 [UniParc].

Checksum: 47E3BAB70472FF31
Show »

FASTA46650,342
Isoform 5 [UniParc].

Checksum: 8C1F69316F4AF3A9
Show »

FASTA596,699
Isoform 6 [UniParc].

Checksum: B4FED0091257ACC1
Show »

FASTA14015,079
Isoform 7 [UniParc].

Checksum: 26B3C3FC9F326D3E
Show »

FASTA50354,415
Isoform 8 [UniParc].

Checksum: CC516256338B09FA
Show »

FASTA52356,497

References

« Hide 'large scale' references
[1]"The structure of the human sterol carrier protein X/sterol carrier protein 2 gene (SCP2)."
Ohba T., Rennert H., Pfeifer S.M., He Z., Yamamoto R., Holt J.A., Billheimer J.T., Strauss J.F. III
Genomics 24:370-374(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SCPX).
Tissue: Liver.
[2]"cDNAs encoding members of a family of proteins related to human sterol carrier protein 2 and assignment of the gene to human chromosome 1 p21-pter."
He Z., Yamamoto R., Furth E.E., Schantz L.J., Naylor S.L., George H., Billheimer J.T., Strauss J.F. III
DNA Cell Biol. 10:559-569(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCPX).
Tissue: Liver.
[3]"Cloning and expression of a cDNA encoding human sterol carrier protein 2."
Yamamoto R., Kallen C.B., Babalola G.O., Rennert H., Billheimer J.T., Strauss J.F. III
Proc. Natl. Acad. Sci. U.S.A. 88:463-467(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCP2).
Tissue: Liver.
[4]"Localization of human sterol carrier protein 2 gene and cDNA expression in COS-7 cell."
Yamamoto R.
Hokkaido Igaku Zasshi 67:839-848(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SCP2).
Tissue: Liver.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 8), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-218 (ISOFORM 7).
Tissue: Brain, Caudate nucleus and Tongue.
[6]Heil O., Ebert L., Hennig S., Henze S., Radelof U., Schneider D., Korn B.
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
[7]"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].
[8]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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 3 AND SCP2).
Tissue: Brain.
[10]The MGC Project Team
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[11]Bienvenut W.V.
Submitted (MAR-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 455-462; 512-522 AND 535-546, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[12]"Regulation of sterol carrier protein gene expression by the forkhead transcription factor FOXO3a."
Dansen T.B., Kops G.J., Denis S., Jelluma N., Wanders R.J., Bos J.L., Burgering B.M., Wirtz K.W.
J. Lipid Res. 45:81-88(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE PROMOTER USAGE, INDUCTION BY 4-HYDROXY-TAMOXIFEN.
[13]"Mutations in the gene encoding peroxisomal sterol carrier protein X (SCPx) cause leukencephalopathy with dystonia and motor neuropathy."
Ferdinandusse S., Kostopoulos P., Denis S., Rusch H., Overmars H., Dillmann U., Reith W., Haas D., Wanders R.J., Duran M., Marziniak M.
Am. J. Hum. Genet. 78:1046-1052(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LDMN.
[14]"Structure-activity studies of human sterol carrier protein 2."
Seedorf U., Scheek S., Engel T., Steif C., Hinz H.-J., Assmann G.
J. Biol. Chem. 269:2613-2618(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-528 AND GLY-530, FUNCTION.
[15]"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-183; LYS-438 AND LYS-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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].
[17]"NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2."
Szyperski T., Scheek S., Johansson J., Assmann G., Seedorf U., Wuethrich K.
FEBS Lett. 335:18-26(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF SCP2.
[18]"Recognition of a functional peroxisome type 1 target by the dynamic import receptor Pex5p."
Stanley W.A., Filipp F.V., Kursula P., Schueller N., Erdmann R., Schliebs W., Sattler M., Wilmanns M.
Mol. Cell 24:653-663(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 426-547 IN COMPLEX WITH PEX5, FUNCTION, SUBCELLULAR LOCATION.
[19]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-155.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U11313 expand/collapse EMBL AC list , U11297, U11299, U11300, U11301, U11302, U11303, U11304, U11305, U11306, U11307, U11308, U11309, U11310, U11311, U11312 Genomic DNA. Translation: AAB41286.1.
M75883 mRNA. Translation: AAA03557.1.
M75884 mRNA. Translation: AAA03558.1. Different initiation.
M55421 mRNA. Translation: AAA03559.1.
S52450 mRNA. Translation: AAB24921.1.
AK294631 mRNA. Translation: BAG57810.1.
AK295214 mRNA. Translation: BAG58208.1.
AK308105 mRNA. No translation available.
CR995014 mRNA. No translation available.
AL445183, AC099677 Genomic DNA. Translation: CAH72590.1.
CH471059 Genomic DNA. Translation: EAX06760.1.
CH471059 Genomic DNA. Translation: EAX06761.1.
BC005911 mRNA. Translation: AAH05911.1.
BC067108 mRNA. Translation: AAH67108.1.
CB997588 mRNA. No translation available.
CCDSCCDS30719.1. [P22307-5]
CCDS41338.1. [P22307-3]
CCDS44149.1. [P22307-2]
CCDS44150.1. [P22307-6]
CCDS53317.1. [P22307-7]
CCDS53318.1. [P22307-8]
CCDS53319.1. [P22307-4]
CCDS572.1. [P22307-1]
PIRB40407.
I38205.
RefSeqNP_001007099.1. NM_001007098.2. [P22307-3]
NP_001007100.1. NM_001007099.2. [P22307-2]
NP_001007101.1. NM_001007100.2. [P22307-6]
NP_001007251.1. NM_001007250.2. [P22307-5]
NP_001180528.1. NM_001193599.1. [P22307-8]
NP_001180546.1. NM_001193617.1. [P22307-4]
NP_002970.2. NM_002979.4. [P22307-1]
UniGeneHs.476365.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QNDNMR-A425-547[»]
2C0LX-ray2.30B426-547[»]
ProteinModelPortalP22307.
SMRP22307. Positions 12-393, 426-547.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112246. 29 interactions.
IntActP22307. 10 interactions.
MINTMINT-3009685.
STRING9606.ENSP00000360569.

Chemistry

ChEMBLCHEMBL5950.

PTM databases

PhosphoSiteP22307.

Polymorphism databases

DMDM2507456.

2D gel databases

REPRODUCTION-2DPAGEIPI00026105.

Proteomic databases

MaxQBP22307.
PaxDbP22307.
PRIDEP22307.

Protocols and materials databases

DNASU6342.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371509; ENSP00000360564; ENSG00000116171. [P22307-7]
ENST00000371513; ENSP00000360568; ENSG00000116171. [P22307-3]
ENST00000371514; ENSP00000360569; ENSG00000116171. [P22307-1]
ENST00000407246; ENSP00000384569; ENSG00000116171. [P22307-8]
ENST00000408941; ENSP00000386214; ENSG00000116171. [P22307-5]
ENST00000430330; ENSP00000406636; ENSG00000116171. [P22307-6]
ENST00000435345; ENSP00000396413; ENSG00000116171. [P22307-2]
ENST00000488965; ENSP00000435783; ENSG00000116171. [P22307-5]
ENST00000528311; ENSP00000434132; ENSG00000116171. [P22307-4]
GeneID6342.
KEGGhsa:6342.
UCSCuc001cuq.2. human. [P22307-3]
uc001cur.2. human. [P22307-1]
uc001cus.2. human. [P22307-2]

Organism-specific databases

CTD6342.
GeneCardsGC01P053392.
HGNCHGNC:10606. SCP2.
HPAHPA027101.
HPA027135.
HPA027317.
MIM184755. gene.
613724. phenotype.
neXtProtNX_P22307.
Orphanet163684. Leukoencephalopathy - dystonia - motor neuropathy.
PharmGKBPA35014.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHOG000221741.
HOVERGENHBG006506.
InParanoidP22307.
KOK08764.
OMAPQMFGNA.
OrthoDBEOG78H3T0.
PhylomeDBP22307.
TreeFamTF300574.

Enzyme and pathway databases

BioCycMetaCyc:HS03991-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP22307.
BgeeP22307.
CleanExHS_SCP2.
GenevestigatorP22307.

Family and domain databases

Gene3D3.30.1050.10. 1 hit.
3.40.47.10. 4 hits.
InterProIPR003033. SCP2_sterol-bd_dom.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamPF02036. SCP2. 1 hit.
PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMSSF53901. SSF53901. 2 hits.
SSF55718. SSF55718. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSCP2. human.
EvolutionaryTraceP22307.
GeneWikiSCP2.
GenomeRNAi6342.
NextBio24628.
PROP22307.
SOURCESearch...

Entry information

Entry nameNLTP_HUMAN
AccessionPrimary (citable) accession number: P22307
Secondary accession number(s): A6NM69 expand/collapse secondary AC list , B4DGJ9, B4DHP6, C9JC79, D3DQ37, E1B6W5, F2Z3J1, Q15432, Q16622, Q5VVZ1, Q6NXF4, Q99430
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 168 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