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Protein

Phospholipid-transporting ATPase IC

Gene

Atp8b1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May play a role in asymmetric distribution of phospholipids in the canicular membrane. Plays a role in bile salt homeostasis. In cooperation with ABCB4 may be involved in establishing integrity of the canalicular membrane thus protecting hepatocytes from bile salts. Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity. Required for the preservation of cochlear hair cells in the inner ear. Required for the preservation of cochlear hair cells in the inner ear. According PubMed:20852622 is proposed to act as cardiolipin transporter during inflammatory injury; the function is questioned by PubMed:21475228.5 Publications

Catalytic activityi

ATP + H2O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei454 – 45414-aspartylphosphate intermediateBy similarity
Metal bindingi893 – 8931MagnesiumBy similarity
Metal bindingi897 – 8971MagnesiumBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cardiolipin binding Source: UniProtKB
  • lipid transporter activity Source: MGI
  • magnesium ion binding Source: InterPro
  • phospholipid-translocating ATPase activity Source: UniProtKB-EC

GO - Biological processi

  • bile acid metabolic process Source: MGI
  • drug transmembrane transport Source: MGI
  • inner ear receptor cell development Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: MGI
  • phospholipid translocation Source: MGI
  • regulation of microvillus assembly Source: MGI
  • sensory perception of sound Source: UniProtKB
  • vestibulocochlear nerve formation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hearing, Lipid transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.3.1. 3474.
ReactomeiR-MMU-936837. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid-transporting ATPase IC (EC:3.6.3.1)
Alternative name(s):
ATPase class I type 8B member 1
P4-ATPase flippase complex alpha subunit ATP8B1
Gene namesi
Name:Atp8b1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1859665. Atp8b1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 121121CytoplasmicSequence analysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence analysisAdd
BLAST
Topological domaini143 – 1442Exoplasmic loopSequence analysis
Transmembranei145 – 16521HelicalSequence analysisAdd
BLAST
Topological domaini166 – 339174CytoplasmicSequence analysisAdd
BLAST
Transmembranei340 – 36021HelicalSequence analysisAdd
BLAST
Topological domaini361 – 38525Exoplasmic loopSequence analysisAdd
BLAST
Transmembranei386 – 40621HelicalSequence analysisAdd
BLAST
Topological domaini407 – 952546CytoplasmicSequence analysisAdd
BLAST
Transmembranei953 – 97321HelicalSequence analysisAdd
BLAST
Topological domaini974 – 9829Exoplasmic loopSequence analysis
Transmembranei983 – 100321HelicalSequence analysisAdd
BLAST
Topological domaini1004 – 103229CytoplasmicSequence analysisAdd
BLAST
Transmembranei1033 – 105321HelicalSequence analysisAdd
BLAST
Topological domaini1054 – 107118Exoplasmic loopSequence analysisAdd
BLAST
Transmembranei1072 – 109221HelicalSequence analysisAdd
BLAST
Topological domaini1093 – 10942CytoplasmicSequence analysis
Transmembranei1095 – 111521HelicalSequence analysisAdd
BLAST
Topological domaini1116 – 114227Exoplasmic loopSequence analysisAdd
BLAST
Transmembranei1143 – 116321HelicalSequence analysisAdd
BLAST
Topological domaini1164 – 125188CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • brush border membrane Source: Ensembl
  • endoplasmic reticulum Source: MGI
  • Golgi apparatus Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MGI
  • stereocilium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice have unimpaired bile secretion, and no liver damage, but show mild abnormalities including depressed weight at weaning and elevated serum bile salt levels. Do not suffer from jaundice or diarrhea and have normal serum bilirubin levels and normal liver enzyme activities, except for mildly elevated serum AST (aspartate aminotransferase) activity. Display unimpaired transhepatic bile salt transport and are resistant to bile salt-induced cholestasis. Upon bile salt feeding, demonstrate serum bile salt accumulation, hepatic injury and expansion of the systemic bile salt pool and this failure of bile salt homeostasis occurrs in the absence of any defect in hepatic bile secretion.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi308 – 3081G → V: Markly decreased expression, hearing loss associated with degeneration of cochlear hair cells and spiral ganglion cells. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12511251Phospholipid-transporting ATPase ICPRO_0000370862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1223 – 12231PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ148W0.
MaxQBiQ148W0.
PaxDbiQ148W0.
PRIDEiQ148W0.

PTM databases

iPTMnetiQ148W0.
PhosphoSiteiQ148W0.

Expressioni

Tissue specificityi

Hepatocytes, bile duct, intestinal epithelial cells (cholangiocytes and ileocytes), and pancreatic acinar cells.1 Publication

Gene expression databases

BgeeiQ148W0.
GenevisibleiQ148W0. MM.

Interactioni

Subunit structurei

Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. The probable flippase ATP8B1:TMEM30A complex can form an intermediate phosphoenzyme in vitro. Also interacts with beta subunit TMEM30B (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025482.

Structurei

3D structure databases

ProteinModelPortaliQ148W0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KDRM. Eukaryota.
ENOG410XPYK. LUCA.
GeneTreeiENSGT00770000120474.
HOGENOMiHOG000202528.
InParanoidiQ148W0.
KOiK01530.
OMAiQRTNSKN.
OrthoDBiEOG7RRF68.
PhylomeDBiQ148W0.
TreeFamiTF300654.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR030346. ATP8B1.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 2 hits.
PTHR24092:SF48. PTHR24092:SF48. 2 hits.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q148W0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTERDSETT FDEESQPNDE VVPYSDDETE DELEDQGSTV EPEQNRVNRE
60 70 80 90 100
AEKKRETFRK DCTWQVKAND RKFHEQPHFM NTKFFCIKES KYASNAIKTY
110 120 130 140 150
KYNGFTFLPM NLFEQFKRAA NFYFLILLIL QAIPQISTLA WYTTLVPLLL
160 170 180 190 200
VLGITAIKDL VDDVARHKMD KEINNRTCEV IKDGRFKIIK WKDIQVGDVI
210 220 230 240 250
RLKKNDFIPA DILLLSSSEP NSLCYVETAE LDGETNLKFK MALEITDQYL
260 270 280 290 300
QIEDNLATFD GFIECEEPNN RLDKFTGTLF WKNQSFPLDA DKILLRGCVI
310 320 330 340 350
RNTDVCHGLV IFAGADTKIM KNSGKTRFKR TKIDYLMNYM VYTIFIVLIL
360 370 380 390 400
VSAGLAIGHA YWEAQVGNYS WYLYDGENAT PSYRGFLNFW GYIIVLNTMV
410 420 430 440 450
PISLYVSVEV IRLGQSHFIN WDLQMYYAEK DTPAKARTTT LNEQLGQIHY
460 470 480 490 500
IFSDKTGTLT QNIMTFKKCC INGTIYGDHR DASQHSHSKI ELVDFSWNTF
510 520 530 540 550
ADGKLAFYDH YLIEQIQSGK EPEVRQFFFL LSICHTVMVD RIDGQINYQA
560 570 580 590 600
ASPDEGALVN AARNFGFAFL ARTQNTITVS ELGSERTYNV LAILDFNSDR
610 620 630 640 650
KRMSIIVRTP EGSIRLYCKG ADTVIYERLH RMNPTKQETQ DALDIFASET
660 670 680 690 700
LRTLCLCYKE IEEKEFTEWN NKFMAASVAS SNRDEALDKV YEEIEKDLIL
710 720 730 740 750
LGATAIEDKL QDGVPETISK LAKADIKIWV LTGDKKETAE NIGFACELLT
760 770 780 790 800
EDTTICYGED INSLLHTRME NQRNRGGVSA KFAPPVYEPF FPPGENRALI
810 820 830 840 850
ITGSWLNEIL LEKKTKRSKI LKLKFPRTEE ERRMRSQSRR RLEEKKEQRQ
860 870 880 890 900
KNFVDLACEC SAVICCRVTP KQKAMVVDLV KRYKKAITLA IGDGANDVNM
910 920 930 940 950
IKTAHIGVGI SGQEGMQAVM SSDYSFAQFR YLQRLLLVHG RWSYIRMCKF
960 970 980 990 1000
LRYFFYKNFA FTLVHFWYSF FNGYSAQTAY EDWFITLYNV LYSSLPVLLM
1010 1020 1030 1040 1050
GLLDQDVSDK LSLRFPGLYV VGQRDLLFNY KRFFVSLLHG VLTSMVLFFI
1060 1070 1080 1090 1100
PLGAYLQTVG QDGEAPSDYQ SFAVTVASAL VITVNFQIGL DTSYWTFVNA
1110 1120 1130 1140 1150
FSIFGSIALY FGIMFDFHSA GIHVLFPSAF QFTGTASNAL RQPYIWLTII
1160 1170 1180 1190 1200
LTVAVCLLPV VAIRFLSMTI WPSESDKIQK HRKRLKAEEQ WKRRQSVFRR
1210 1220 1230 1240 1250
GVSSRRSAYA FSHQRGYADL ISSGRSIRKK RSPLDAIIAD GTAEYRRTVE

S
Length:1,251
Mass (Da):143,798
Last modified:May 5, 2009 - v2
Checksum:i394920189075875D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041G → A in AAR90342 (PubMed:14976163).Curated
Sequence conflicti108 – 1081L → I in AAR90342 (PubMed:14976163).Curated
Sequence conflicti155 – 1551T → M in BAE34046 (PubMed:16141072).Curated
Sequence conflicti174 – 1741N → S in AAR90342 (PubMed:14976163).Curated
Sequence conflicti176 – 1761R → M in AAR90342 (PubMed:14976163).Curated
Sequence conflicti531 – 5311L → P in BAE34046 (PubMed:16141072).Curated
Sequence conflicti575 – 5751N → Y in BAE34046 (PubMed:16141072).Curated
Sequence conflicti667 – 6671T → A in AAI17947 (PubMed:15489334).Curated
Sequence conflicti671 – 6711N → K in AAI17947 (PubMed:15489334).Curated
Sequence conflicti893 – 8931D → E in BAE34046 (PubMed:16141072).Curated
Sequence conflicti1226 – 12261S → C in BAE34046 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY506548 mRNA. Translation: AAR90342.1.
AK157316 mRNA. Translation: BAE34046.1.
BC117946 mRNA. Translation: AAI17947.1.
CCDSiCCDS29304.1.
RefSeqiNP_001001488.2. NM_001001488.3.
UniGeneiMm.270043.
Mm.456199.

Genome annotation databases

EnsembliENSMUST00000025482; ENSMUSP00000025482; ENSMUSG00000039529.
GeneIDi54670.
KEGGimmu:54670.
UCSCiuc008fem.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY506548 mRNA. Translation: AAR90342.1.
AK157316 mRNA. Translation: BAE34046.1.
BC117946 mRNA. Translation: AAI17947.1.
CCDSiCCDS29304.1.
RefSeqiNP_001001488.2. NM_001001488.3.
UniGeneiMm.270043.
Mm.456199.

3D structure databases

ProteinModelPortaliQ148W0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025482.

PTM databases

iPTMnetiQ148W0.
PhosphoSiteiQ148W0.

Proteomic databases

EPDiQ148W0.
MaxQBiQ148W0.
PaxDbiQ148W0.
PRIDEiQ148W0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025482; ENSMUSP00000025482; ENSMUSG00000039529.
GeneIDi54670.
KEGGimmu:54670.
UCSCiuc008fem.1. mouse.

Organism-specific databases

CTDi5205.
MGIiMGI:1859665. Atp8b1.

Phylogenomic databases

eggNOGiENOG410KDRM. Eukaryota.
ENOG410XPYK. LUCA.
GeneTreeiENSGT00770000120474.
HOGENOMiHOG000202528.
InParanoidiQ148W0.
KOiK01530.
OMAiQRTNSKN.
OrthoDBiEOG7RRF68.
PhylomeDBiQ148W0.
TreeFamiTF300654.

Enzyme and pathway databases

BRENDAi3.6.3.1. 3474.
ReactomeiR-MMU-936837. Ion transport by P-type ATPases.

Miscellaneous databases

NextBioi311520.
PROiQ148W0.
SOURCEiSearch...

Gene expression databases

BgeeiQ148W0.
GenevisibleiQ148W0. MM.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR030346. ATP8B1.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 2 hits.
PTHR24092:SF48. PTHR24092:SF48. 2 hits.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A mouse genetic model for familial cholestasis caused by ATP8B1 mutations reveals perturbed bile salt homeostasis but no impairment in bile secretion."
    Pawlikowska L., Groen A., Eppens E.F., Kunne C., Ottenhoff R., Looije N., Knisely A.S., Killeen N.P., Bull L.N., Elferink R.P.J.O., Freimer N.B.
    Hum. Mol. Genet. 13:881-892(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    Strain: 129.
  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: NOD.
  3. "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].
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: FUNCTION, MUTAGENESIS OF GLY-308.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver and Pancreas.
  7. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Complementary functions of the flippase ATP8B1 and the floppase ABCB4 in maintaining canalicular membrane integrity."
    Groen A., Romero M.R., Kunne C., Hoosdally S.J., Dixon P.H., Wooding C., Williamson C., Seppen J., Van den Oever K., Mok K.S., Paulusma C.C., Linton K.J., Oude Elferink R.P.
    Gastroenterology 141:1927-1937(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: FUNCTION.

Entry informationi

Entry nameiAT8B1_MOUSE
AccessioniPrimary (citable) accession number: Q148W0
Secondary accession number(s): Q3U010, Q6R964
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: May 11, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.