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Protein

Non-specific lipid-transfer protein

Gene

Scp2

Organism
Mus musculus (Mouse)
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.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BRENDAi2.3.1.176. 3474.
ReactomeiR-MMU-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-MMU-2046106. alpha-linolenic acid (ALA) metabolism.
R-MMU-389887. Beta-oxidation of pristanoyl-CoA.

Chemistry

SwissLipidsiSLP:000000495.

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
Synonyms:Scp-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:98254. Scp2.

Subcellular locationi

  • Cytoplasm

  • Note: Cytoplasmic in the liver and also associated with mitochondria especially in steroidogenic tissues.
Isoform SCPx :
  • Peroxisome

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Non-specific lipid-transfer proteinPRO_0000034093Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31PhosphoserineBy similarity
Modified residuei7 – 71N6-acetyllysineCombined sources
Modified residuei8 – 81PhosphoserineBy similarity
Modified residuei40 – 401N6-succinyllysineCombined sources
Modified residuei132 – 1321N6-acetyllysine; alternateCombined sources
Modified residuei132 – 1321N6-succinyllysine; alternateCombined sources
Modified residuei168 – 1681N6-succinyllysineCombined sources
Modified residuei173 – 1731N6-acetyllysineCombined sources
Modified residuei177 – 1771N6-acetyllysineCombined sources
Modified residuei183 – 1831N6-acetyllysine; alternateCombined sources
Modified residuei183 – 1831N6-succinyllysine; alternateCombined sources
Modified residuei211 – 2111N6-succinyllysineCombined sources
Modified residuei282 – 2821N6-succinyllysineCombined sources
Modified residuei341 – 3411N6-acetyllysine; alternateCombined sources
Modified residuei341 – 3411N6-succinyllysine; alternateCombined sources
Modified residuei432 – 4321N6-acetyllysine; alternateCombined sources
Modified residuei432 – 4321N6-succinyllysine; alternateCombined sources
Modified residuei438 – 4381N6-acetyllysine; alternateCombined sources
Modified residuei438 – 4381N6-succinyllysine; alternateCombined sources
Modified residuei443 – 4431N6-acetyllysine; alternateCombined sources
Modified residuei443 – 4431N6-succinyllysine; alternateCombined sources
Modified residuei453 – 4531N6-acetyllysine; alternateCombined sources
Modified residuei453 – 4531N6-succinyllysine; alternateCombined sources
Modified residuei464 – 4641N6-succinyllysineCombined sources
Modified residuei470 – 4701N6-acetyllysine; alternateCombined sources
Modified residuei470 – 4701N6-succinyllysine; alternateCombined sources
Modified residuei479 – 4791N6-succinyllysineCombined sources
Modified residuei491 – 4911N6-acetyllysineCombined sources
Modified residuei492 – 4921N6-succinyllysineCombined sources
Modified residuei511 – 5111N6-succinyllysineCombined sources
Modified residuei516 – 5161PhosphoserineCombined sources
Modified residuei522 – 5221N6-succinyllysineCombined sources
Modified residuei534 – 5341N6-succinyllysineCombined sources
Modified residuei544 – 5441N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP32020.
MaxQBiP32020.
PaxDbiP32020.
PRIDEiP32020.
TopDownProteomicsiP32020-1. [P32020-1]

PTM databases

iPTMnetiP32020.
PhosphoSiteiP32020.

Expressioni

Tissue specificityi

Present at low levels in all tissues examined but expressed predominantly in the liver.

Gene expression databases

BgeeiP32020.
CleanExiMM_SCP2.
ExpressionAtlasiP32020. baseline and differential.
GenevisibleiP32020. MM.

Interactioni

Subunit structurei

Interacts with PEX5.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP32020. 6 interactions.
MINTiMINT-219254.
STRINGi10090.ENSMUSP00000030340.

Structurei

3D structure databases

ProteinModelPortaliP32020.
SMRiP32020. Positions 12-393, 425-547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini433 – 543111SCP2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi545 – 5473Microbody targeting signalSequence analysis

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.
InParanoidiP32020.
KOiK08764.
OMAiHMEVMIN.
OrthoDBiEOG78H3T0.
PhylomeDBiP32020.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform SCPx (identifier: P32020-1) [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
MPSVALKSPR LRRVFVVGVG MTKFMKPGGE NSRDYPDMAK EAGQKALEDA
60 70 80 90 100
QIPYSAVEQA CVGYVYGDST SGQRAIYHSL GLTGIPIINV NNNCSTGSTA
110 120 130 140 150
LFMAHQLIQG GLANCVLALG FEKMERGSIG TKFSDRTTPT DKHIEVLIDK
160 170 180 190 200
YGLSAHPITP QMFGYAGKEH MEKYGTKVEH FAKIGWKNHK HSVNNTYSQF
210 220 230 240 250
QDEYSLEEVM KSKPVFDFLT ILQCCPTSDG AAAAILSSEE FVQQYGLQSK
260 270 280 290 300
AVEIVAQEMM TDLPSTFEEK SIIKVVGYDM SKEAARRCYE KSGLTPNDVD
310 320 330 340 350
VIELHDCFSV NELITYEALG LCPEGQGGTL VDRGDNTYGG KWVINPSGGL
360 370 380 390 400
ISKGHPLGAT GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGLGGAVVV
410 420 430 440 450
TLYRMGFPEA ASSFRTHQVS AAPTSSAGDG FKANLVFKEI EKKLEEEGEQ
460 470 480 490 500
FVKKIGGIFA FKVKDGPGGK EATWVVDVKN GKGSVLPNSD KKADCTITMA
510 520 530 540
DSDLLALMTG KMNPQSAFFQ GKLKIAGNMG LAMKLQNLQL QPGKAKL
Length:547
Mass (Da):59,126
Last modified:June 16, 2003 - v3
Checksum:i37BA2E730D9CB105
GO
Isoform SCP2 (identifier: P32020-2) [UniParc]FASTAAdd to basket

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

Note: Mitochondrial precursor. Contains a mitochondrial transit peptide at positions 405-424 (Potential).Curated
Show »
Length:143
Mass (Da):15,237
Checksum:i6A466BBBFB9B9A00
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2321A → C in AAA40098 (PubMed:8428655).Curated
Sequence conflicti478 – 4781V → A in AAA40099 (PubMed:1709640).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 404404Missing in isoform SCP2. CuratedVSP_018895Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91458 mRNA. Translation: AAA40098.1.
AK002425 mRNA. Translation: BAB22092.2.
AK004860 mRNA. No translation available.
AL844206 Genomic DNA. Translation: CAM27075.1.
AL844206 Genomic DNA. Translation: CAM27076.1.
BC018384 mRNA. Translation: AAH18384.1.
BC034613 mRNA. Translation: AAH34613.1.
M62361 mRNA. Translation: AAA40099.1.
X91150 Genomic DNA. Translation: CAA62592.1.
CCDSiCCDS18446.1. [P32020-1]
PIRiA40015.
JU0157.
RefSeqiNP_035457.1. NM_011327.4. [P32020-1]
UniGeneiMm.379011.

Genome annotation databases

EnsembliENSMUST00000030340; ENSMUSP00000030340; ENSMUSG00000028603. [P32020-1]
ENSMUST00000106701; ENSMUSP00000102312; ENSMUSG00000028603. [P32020-2]
GeneIDi20280.
KEGGimmu:20280.
UCSCiuc008uas.2. mouse. [P32020-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91458 mRNA. Translation: AAA40098.1.
AK002425 mRNA. Translation: BAB22092.2.
AK004860 mRNA. No translation available.
AL844206 Genomic DNA. Translation: CAM27075.1.
AL844206 Genomic DNA. Translation: CAM27076.1.
BC018384 mRNA. Translation: AAH18384.1.
BC034613 mRNA. Translation: AAH34613.1.
M62361 mRNA. Translation: AAA40099.1.
X91150 Genomic DNA. Translation: CAA62592.1.
CCDSiCCDS18446.1. [P32020-1]
PIRiA40015.
JU0157.
RefSeqiNP_035457.1. NM_011327.4. [P32020-1]
UniGeneiMm.379011.

3D structure databases

ProteinModelPortaliP32020.
SMRiP32020. Positions 12-393, 425-547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP32020. 6 interactions.
MINTiMINT-219254.
STRINGi10090.ENSMUSP00000030340.

Chemistry

SwissLipidsiSLP:000000495.

PTM databases

iPTMnetiP32020.
PhosphoSiteiP32020.

Proteomic databases

EPDiP32020.
MaxQBiP32020.
PaxDbiP32020.
PRIDEiP32020.
TopDownProteomicsiP32020-1. [P32020-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030340; ENSMUSP00000030340; ENSMUSG00000028603. [P32020-1]
ENSMUST00000106701; ENSMUSP00000102312; ENSMUSG00000028603. [P32020-2]
GeneIDi20280.
KEGGimmu:20280.
UCSCiuc008uas.2. mouse. [P32020-1]

Organism-specific databases

CTDi6342.
MGIiMGI:98254. Scp2.

Phylogenomic databases

eggNOGiKOG1406. Eukaryota.
KOG4170. Eukaryota.
ENOG410XPRW. LUCA.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000221741.
HOVERGENiHBG006506.
InParanoidiP32020.
KOiK08764.
OMAiHMEVMIN.
OrthoDBiEOG78H3T0.
PhylomeDBiP32020.
TreeFamiTF300574.

Enzyme and pathway databases

BRENDAi2.3.1.176. 3474.
ReactomeiR-MMU-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-MMU-2046106. alpha-linolenic acid (ALA) metabolism.
R-MMU-389887. Beta-oxidation of pristanoyl-CoA.

Miscellaneous databases

NextBioi297975.
PROiP32020.
SOURCEiSearch...

Gene expression databases

BgeeiP32020.
CleanExiMM_SCP2.
ExpressionAtlasiP32020. baseline and differential.
GenevisibleiP32020. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression and sequences of mouse sterol-carrier protein-x-encoding cDNAs and a related pseudogene."
    Seedorf U., Raabe M., Assmann G.
    Gene 123:165-172(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney and Liver.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Tissue: Liver and Mammary gland.
  5. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 525-534, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  6. "cDNA sequence and bacterial expression of mouse liver sterol carrier protein-2."
    Moncecchi D.T., Pastuszyn A., Scallen T.J.
    J. Biol. Chem. 266:9885-9892(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 405-547, PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  7. "Structure and chromosomal assignment of the murine sterol carrier protein 2 gene (Scp2) and two related pseudogenes by in situ hybridization."
    Raabe M., Seedorf U., Hameister H., Ellinghaus P., Assmann G.
    Cytogenet. Cell Genet. 73:279-281(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
    Strain: 129/Sv.
    Tissue: Liver.
  8. "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
    Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
    Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-132; LYS-168; LYS-183; LYS-211; LYS-282; LYS-341; LYS-432; LYS-438; LYS-443; LYS-453; LYS-464; LYS-470; LYS-479; LYS-492; LYS-511; LYS-522; LYS-534 AND LYS-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-132; LYS-177; LYS-183; LYS-341; LYS-432; LYS-438; LYS-443; LYS-453; LYS-470 AND LYS-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNLTP_MOUSE
AccessioniPrimary (citable) accession number: P32020
Secondary accession number(s): A2APS2, A2APS3, Q9DBM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: June 16, 2003
Last modified: May 11, 2016
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.