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Protein
Submitted name:

Non-specific lipid-transfer protein

Gene

SCP2

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Non-specific lipid-transfer proteinImported
Gene namesi
Name:SCP2Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10606. SCP2.

PTM / Processingi

Proteomic databases

EPDiE9PLD1.
PaxDbiE9PLD1.
PRIDEiE9PLD1.

Expressioni

Gene expression databases

BgeeiE9PLD1.
ExpressionAtlasiE9PLD1. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000360569.

Structurei

3D structure databases

ProteinModelPortaliE9PLD1.
SMRiE9PLD1. Positions 12-362.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 239226Thiolase_NInterPro annotationAdd
BLAST
Domaini283 – 36280Thiolase_CInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thiolase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG1406. Eukaryota.
KOG4170. Eukaryota.
ENOG410XPRW. LUCA.
GeneTreeiENSGT00530000062928.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E9PLD1-1 [UniParc]FASTAAdd to basket

« 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
ISKGHPLGAT GGHSCS
Length:366
Mass (Da):39,553
Last modified:April 5, 2011 - v1
Checksum:iFD7682E738F5337E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC099677 Genomic DNA. No translation available.
AL445183 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000478631; ENSP00000435194; ENSG00000116171.
UCSCiuc057gqg.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC099677 Genomic DNA. No translation available.
AL445183 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliE9PLD1.
SMRiE9PLD1. Positions 12-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000360569.

Proteomic databases

EPDiE9PLD1.
PaxDbiE9PLD1.
PRIDEiE9PLD1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000478631; ENSP00000435194; ENSG00000116171.
UCSCiuc057gqg.1. human.

Organism-specific databases

HGNCiHGNC:10606. SCP2.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1406. Eukaryota.
KOG4170. Eukaryota.
ENOG410XPRW. LUCA.
GeneTreeiENSGT00530000062928.

Miscellaneous databases

ChiTaRSiSCP2. human.
NextBioi35503182.

Gene expression databases

BgeeiE9PLD1.
ExpressionAtlasiE9PLD1. baseline and differential.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , 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., 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., 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., 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., McLaren S., Milne S., Mistry S., Moore M.J., 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., 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., Banerjee R., Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D., Porter K.M., Prigmore E.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  5. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiE9PLD1_HUMAN
AccessioniPrimary (citable) accession number: E9PLD1
Entry historyi
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: April 13, 2016
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.