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Protein

Non-specific lipid-transfer protein

Gene

SCP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis.2 Publications

Catalytic activityi

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.

GO - Molecular functioni

  • cholesterol binding Source: UniProtKB
  • fatty-acyl-CoA binding Source: UniProtKB
  • long-chain fatty acyl-CoA binding Source: UniProtKB
  • oleic acid binding Source: UniProtKB
  • phosphatidylinositol transporter activity Source: UniProtKB
  • propanoyl-CoA C-acyltransferase activity Source: UniProtKB-EC
  • propionyl-CoA C2-trimethyltridecanoyltransferase activity Source: Reactome
  • receptor binding Source: UniProtKB
  • sterol transporter activity Source: GO_Central

GO - Biological processi

  • alpha-linolenic acid metabolic process Source: Reactome
  • bile acid biosynthetic process Source: Reactome
  • fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
  • inositol trisphosphate biosynthetic process Source: UniProtKB
  • lipid hydroperoxide transport Source: UniProtKB
  • peroxisome organization Source: Ensembl
  • phospholipid transport Source: UniProtKB
  • positive regulation of intracellular cholesterol transport Source: UniProtKB
  • positive regulation of steroid metabolic process Source: UniProtKB
  • progesterone biosynthetic process Source: UniProtKB
  • protein localization to plasma membrane Source: UniProtKB
  • steroid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS03991-MONOMER.
ZFISH:HS03991-MONOMER.
BRENDAi2.3.1.176. 2681.
ReactomeiR-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-HSA-2046106. alpha-linolenic acid (ALA) metabolism.
R-HSA-389887. Beta-oxidation of pristanoyl-CoA.

Names & Taxonomyi

Protein namesi
Recommended name:
Non-specific lipid-transfer protein (EC:2.3.1.176)
Short name:
NSL-TP
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 namesi
Name:SCP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10606. SCP2.

Subcellular locationi

Isoform SCPx :
  • Peroxisome

  • Note: Interaction with PEX5 is essential for peroxisomal import.

GO - Cellular componenti

  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • mitochondrion Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • peroxisomal matrix Source: Reactome
  • peroxisome Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

Pathology & Biotechi

Involvement in diseasei

Leukoencephalopathy, with dystonia and motor neuropathy (LDMN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:613724

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi528N → D: Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-530. 1 Publication1
Mutagenesisi528N → I: Strongly reduces sterol carrier and phosphatidylcholine transfer activity. 1 Publication1
Mutagenesisi530G → D: Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-528. 1 Publication1

Organism-specific databases

DisGeNETi6342.
MalaCardsiSCP2.
MIMi613724. phenotype.
OpenTargetsiENSG00000116171.
Orphaneti163684. Leukoencephalopathy - dystonia - motor neuropathy.
PharmGKBiPA35014.

Chemistry databases

ChEMBLiCHEMBL5950.

Polymorphism and mutation databases

BioMutaiSCP2.
DMDMi2507456.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000340911 – 547Non-specific lipid-transfer proteinAdd BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3PhosphoserineBy similarity1
Modified residuei132N6-acetyllysine; alternateBy similarity1
Modified residuei132N6-succinyllysine; alternateBy similarity1
Modified residuei168N6-succinyllysineBy similarity1
Modified residuei173N6-acetyllysineBy similarity1
Modified residuei177N6-acetyllysineBy similarity1
Modified residuei183N6-acetyllysine; alternateCombined sources1
Modified residuei183N6-succinyllysine; alternateBy similarity1
Modified residuei282N6-succinyllysineBy similarity1
Modified residuei341N6-acetyllysine; alternateBy similarity1
Modified residuei341N6-succinyllysine; alternateBy similarity1
Modified residuei432N6-acetyllysine; alternateBy similarity1
Modified residuei432N6-succinyllysine; alternateBy similarity1
Modified residuei438N6-acetyllysine; alternateCombined sources1
Modified residuei438N6-succinyllysine; alternateBy similarity1
Modified residuei443N6-acetyllysine; alternateBy similarity1
Modified residuei443N6-succinyllysine; alternateBy similarity1
Modified residuei453N6-acetyllysine; alternateBy similarity1
Modified residuei453N6-succinyllysine; alternateBy similarity1
Modified residuei464N6-succinyllysineBy similarity1
Modified residuei470N6-acetyllysine; alternateCombined sources1
Modified residuei470N6-succinyllysine; alternateBy similarity1
Modified residuei479N6-succinyllysineBy similarity1
Modified residuei491N6-acetyllysineBy similarity1
Modified residuei492N6-succinyllysineBy similarity1
Modified residuei511N6-succinyllysineBy similarity1
Modified residuei516PhosphoserineBy similarity1
Modified residuei522N6-succinyllysineBy similarity1
Modified residuei534N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP22307.
MaxQBiP22307.
PaxDbiP22307.
PeptideAtlasiP22307.
PRIDEiP22307.
TopDownProteomicsiP22307-1. [P22307-1]
P22307-2. [P22307-2]
P22307-4. [P22307-4]

2D gel databases

REPRODUCTION-2DPAGEIPI00026105.

PTM databases

iPTMnetiP22307.
PhosphoSitePlusiP22307.
SwissPalmiP22307.

Expressioni

Tissue specificityi

Liver, fibroblasts, and placenta.

Inductioni

Up-regulated by 4-hydroxy-tamoxifen.1 Publication

Gene expression databases

BgeeiENSG00000116171.
CleanExiHS_SCP2.
ExpressionAtlasiP22307. baseline and differential.
GenevisibleiP22307. HS.

Organism-specific databases

HPAiHPA027101.
HPA027135.
HPA027317.

Interactioni

Subunit structurei

Interacts with PEX5.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CAV1Q031353EBI-1050999,EBI-603614
Cav1P498173EBI-1050999,EBI-1161338From a different organism.
TRIP13Q156454EBI-1050999,EBI-358993

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112246. 38 interactors.
IntActiP22307. 11 interactors.
MINTiMINT-3009685.
STRINGi9606.ENSP00000360569.

Chemistry databases

BindingDBiP22307.

Structurei

Secondary structure

1547
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni427 – 430Combined sources4
Helixi432 – 454Combined sources23
Beta strandi457 – 465Combined sources9
Helixi467 – 469Combined sources3
Beta strandi472 – 480Combined sources9
Beta strandi484 – 487Combined sources4
Beta strandi494 – 500Combined sources7
Helixi501 – 508Combined sources8
Turni509 – 511Combined sources3
Helixi514 – 519Combined sources6
Beta strandi524 – 527Combined sources4
Helixi529 – 533Combined sources5
Helixi534 – 538Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QNDNMR-A425-547[»]
2C0LX-ray2.30B426-547[»]
ProteinModelPortaliP22307.
SMRiP22307.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22307.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini433 – 543SCP2Add BLAST111

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi545 – 547Microbody targeting signalSequence analysis3

Sequence similaritiesi

In the N-terminal section; belongs to the thiolase family.Curated
Contains 1 SCP2 domain.Curated

Phylogenomic databases

eggNOGiKOG1406. Eukaryota.
KOG4170. Eukaryota.
ENOG410XPRW. LUCA.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000221741.
HOVERGENiHBG006506.
InParanoidiP22307.
KOiK08764.
OMAiHMEVMIN.
OrthoDBiEOG091G026S.
PhylomeDBiP22307.
TreeFamiTF300574.

Family and domain databases

Gene3Di3.30.1050.10. 1 hit.
3.40.47.10. 4 hits.
InterProiIPR003033. SCP2_sterol-bd_dom.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02036. SCP2. 1 hit.
PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
SSF55718. SSF55718. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform SCPx (identifier: P22307-1) [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

        10         20         30         40         50
MSSSPWEPAT LRRVFVVGVG MTKFVKPGAE NSRDYPDLAE EAGKKALADA
60 70 80 90 100
QIPYSAVDQA CVGYVFGDST CGQRAIYHSL GMTGIPIINV NNNCATGSTA
110 120 130 140 150
LFMARQLIQG GVAECVLALG FEKMSKGSLG IKFSDRTIPT DKHVDLLINK
160 170 180 190 200
YGLSAHPVAP QMFGYAGKEH MEKYGTKIEH FAKIGWKNHK HSVNNPYSQF
210 220 230 240 250
QDEYSLDEVM ASKEVFDFLT ILQCCPTSDG AAAAILASEA FVQKYGLQSK
260 270 280 290 300
AVEILAQEMM TDLPSSFEEK SIIKMVGFDM SKEAARKCYE KSGLTPNDID
310 320 330 340 350
VIELHDCFST NELLTYEALG LCPEGQGATL VDRGDNTYGG KWVINPSGGL
360 370 380 390 400
ISKGHPLGAT GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGIGGAVVV
410 420 430 440 450
TLYKMGFPEA ASSFRTHQIE AVPTSSASDG FKANLVFKEI EKKLEEEGEQ
460 470 480 490 500
FVKKIGGIFA FKVKDGPGGK EATWVVDVKN GKGSVLPNSD KKADCTITMA
510 520 530 540
DSDFLALMTG KMNPQSAFFQ GKLKITGNMG LAMKLQNLQL QPGNAKL
Length:547
Mass (Da):58,994
Last modified:November 1, 1997 - v2
Checksum:i29F7551465C7143A
GO
Isoform SCP2 (identifier: P22307-2) [UniParc]FASTAAdd to basket

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.Curated
Show »
Length:143
Mass (Da):15,401
Checksum:iDE7FD93BB320BB30
GO
Isoform 3 (identifier: P22307-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     67-110: Missing.
     362-547: LAQCAELCWQ...LQLQPGNAKL → GHSCS

Show »
Length:322
Mass (Da):34,975
Checksum:iFC4864F7E46C77F7
GO
Isoform 4 (identifier: P22307-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.

Note: Produced by alternative splicing. No experimental confirmation available.
Show »
Length:466
Mass (Da):50,342
Checksum:i47E3BAB70472FF31
GO
Isoform 5 (identifier: P22307-5) [UniParc]FASTAAdd to basket

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

Show »
Length:59
Mass (Da):6,699
Checksum:i8C1F69316F4AF3A9
GO
Isoform 6 (identifier: P22307-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-404: Missing.
     412-414: Missing.

Show »
Length:140
Mass (Da):15,079
Checksum:iB4FED0091257ACC1
GO
Isoform 7 (identifier: P22307-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     67-110: Missing.

Note: Produced by alternative splicing.
Show »
Length:503
Mass (Da):54,415
Checksum:i26B3C3FC9F326D3E
GO
Isoform 8 (identifier: P22307-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-66: Missing.

Note: Produced by alternative splicing.
Show »
Length:523
Mass (Da):56,497
Checksum:iCC516256338B09FA
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10T → A in AAB41286 (PubMed:7698762).Curated1
Sequence conflicti56A → V in AK308105 (PubMed:14702039).Curated1
Sequence conflicti116V → A in AK308105 (PubMed:14702039).Curated1
Sequence conflicti341K → Q in BAG57810 (PubMed:14702039).Curated1
Sequence conflicti393G → D in AAB41286 (PubMed:7698762).Curated1
Sequence conflicti472A → D in AAB24921 (PubMed:1483685).Curated1
Sequence conflicti482K → Q in AAB24921 (PubMed:1483685).Curated1
Sequence conflicti501D → A in AAB24921 (PubMed:1483685).Curated1
Sequence conflicti522K → P in AAB24921 (PubMed:1483685).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035706155A → D in a breast cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0189771 – 404Missing in isoform SCP2, isoform 5 and isoform 6. 5 PublicationsAdd BLAST404
Alternative sequenceiVSP_0451871 – 81Missing in isoform 4. 1 PublicationAdd BLAST81
Alternative sequenceiVSP_04726743 – 66Missing in isoform 8. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_04268667 – 110Missing in isoform 3 and isoform 7. 2 PublicationsAdd BLAST44
Alternative sequenceiVSP_042687362 – 547LAQCA…GNAKL → GHSCS in isoform 3. 1 PublicationAdd BLAST186
Alternative sequenceiVSP_047268412 – 414Missing in isoform 6. 1 Publication3
Alternative sequenceiVSP_047269447 – 463EGEQF…FAFKV → IRRLTAQSQWLTQTSWL in isoform 5. 1 PublicationAdd BLAST17
Alternative sequenceiVSP_047270464 – 547Missing in isoform 5. 1 PublicationAdd BLAST84

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11313
, 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.
CCDSiCCDS30719.1. [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]
PIRiB40407.
I38205.
RefSeqiNP_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]
XP_016857535.1. XM_017002046.1. [P22307-2]
UniGeneiHs.476365.

Genome annotation databases

EnsembliENST00000371509; 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]
GeneIDi6342.
KEGGihsa:6342.
UCSCiuc001cuq.3. human. [P22307-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11313
, 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.
CCDSiCCDS30719.1. [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]
PIRiB40407.
I38205.
RefSeqiNP_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]
XP_016857535.1. XM_017002046.1. [P22307-2]
UniGeneiHs.476365.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QNDNMR-A425-547[»]
2C0LX-ray2.30B426-547[»]
ProteinModelPortaliP22307.
SMRiP22307.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112246. 38 interactors.
IntActiP22307. 11 interactors.
MINTiMINT-3009685.
STRINGi9606.ENSP00000360569.

Chemistry databases

BindingDBiP22307.
ChEMBLiCHEMBL5950.

PTM databases

iPTMnetiP22307.
PhosphoSitePlusiP22307.
SwissPalmiP22307.

Polymorphism and mutation databases

BioMutaiSCP2.
DMDMi2507456.

2D gel databases

REPRODUCTION-2DPAGEIPI00026105.

Proteomic databases

EPDiP22307.
MaxQBiP22307.
PaxDbiP22307.
PeptideAtlasiP22307.
PRIDEiP22307.
TopDownProteomicsiP22307-1. [P22307-1]
P22307-2. [P22307-2]
P22307-4. [P22307-4]

Protocols and materials databases

DNASUi6342.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371509; 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]
GeneIDi6342.
KEGGihsa:6342.
UCSCiuc001cuq.3. human. [P22307-1]

Organism-specific databases

CTDi6342.
DisGeNETi6342.
GeneCardsiSCP2.
HGNCiHGNC:10606. SCP2.
HPAiHPA027101.
HPA027135.
HPA027317.
MalaCardsiSCP2.
MIMi184755. gene.
613724. phenotype.
neXtProtiNX_P22307.
OpenTargetsiENSG00000116171.
Orphaneti163684. Leukoencephalopathy - dystonia - motor neuropathy.
PharmGKBiPA35014.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1406. Eukaryota.
KOG4170. Eukaryota.
ENOG410XPRW. LUCA.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000221741.
HOVERGENiHBG006506.
InParanoidiP22307.
KOiK08764.
OMAiHMEVMIN.
OrthoDBiEOG091G026S.
PhylomeDBiP22307.
TreeFamiTF300574.

Enzyme and pathway databases

BioCyciMetaCyc:HS03991-MONOMER.
ZFISH:HS03991-MONOMER.
BRENDAi2.3.1.176. 2681.
ReactomeiR-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-HSA-2046106. alpha-linolenic acid (ALA) metabolism.
R-HSA-389887. Beta-oxidation of pristanoyl-CoA.

Miscellaneous databases

ChiTaRSiSCP2. human.
EvolutionaryTraceiP22307.
GeneWikiiSCP2.
GenomeRNAii6342.
PROiP22307.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116171.
CleanExiHS_SCP2.
ExpressionAtlasiP22307. baseline and differential.
GenevisibleiP22307. HS.

Family and domain databases

Gene3Di3.30.1050.10. 1 hit.
3.40.47.10. 4 hits.
InterProiIPR003033. SCP2_sterol-bd_dom.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02036. SCP2. 1 hit.
PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
SSF55718. SSF55718. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNLTP_HUMAN
AccessioniPrimary (citable) accession number: P22307
Secondary accession number(s): A6NM69
, B4DGJ9, B4DHP6, C9JC79, D3DQ37, E1B6W5, F2Z3J1, Q15432, Q16622, Q5VVZ1, Q6NXF4, Q99430
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 194 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, Direct protein sequencing, 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

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 one 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.