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Protein

F-BAR domain only protein 2

Gene

Fcho2

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

Functioni

Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor.2 Publications

GO - Molecular functioni

  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • phosphatidylinositol binding Source: UniProtKB
  • phosphatidylserine binding Source: UniProtKB

GO - Biological processi

  • clathrin coat assembly Source: UniProtKB
  • clathrin-mediated endocytosis Source: UniProtKB
  • membrane invagination Source: UniProtKB
  • protein localization to plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
F-BAR domain only protein 2
Gene namesi
Name:Fcho2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:3505790. Fcho2.

Subcellular locationi

GO - Cellular componenti

  • clathrin-coated vesicle Source: UniProtKB
  • coated pit Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381F → E: Loss of function mutant which is unable to promote clathrin coated-pits formation. Cytosolic mutant; when associated with E-73. 1 Publication
Mutagenesisi73 – 731W → E: Loss of function mutant which is unable to promote clathrin coated-pits formation. Cytosolic mutant; when associated with E-38. 1 Publication
Mutagenesisi136 – 1361L → E: Loss of function mutant which is unable to promote clathrin coated-pits formation. Binds to membrane but is unable to induce membrane tubulation. Induces the formation of large and static clathrin-coated pits. 1 Publication
Mutagenesisi146 – 1461K → E: Loss of function mutant which is unable to promote clathrin coated-pits formation. Cytosolic mutant which is unable to bind and induce membrane tubulation; when associated with E-165. 1 Publication
Mutagenesisi165 – 1651K → E: Loss of function mutant which is unable to promote clathrin coated-pits formation. Cytosolic mutant which is unable to bind and induce membrane tubulation; when associated with E-146. 1 Publication
Mutagenesisi268 – 2681I → N: Loss of function mutant which is unable to promote clathrin coated-pits formation. Binds to membrane but is unable to induce membrane tubulation. Induces the formation of large and static clathrin-coated pits. 1 Publication
Mutagenesisi797 – 7971K → E: Loss of interaction with EPS15 and ITSN1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 809809F-BAR domain only protein 2PRO_0000266006Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi147 – 147Interchain (with C-273)By similarity
Disulfide bondi273 – 273Interchain (with C-147)By similarity
Modified residuei312 – 3121PhosphoserineCombined sources
Modified residuei385 – 3851PhosphothreonineBy similarity
Modified residuei387 – 3871PhosphoserineCombined sources
Modified residuei394 – 3941PhosphoserineCombined sources
Modified residuei402 – 4021PhosphoserineCombined sources
Modified residuei403 – 4031PhosphoserineCombined sources
Modified residuei487 – 4871PhosphoserineCombined sources
Modified residuei492 – 4921PhosphoserineCombined sources
Modified residuei495 – 4951PhosphoserineBy similarity
Modified residuei507 – 5071PhosphoserineCombined sources
Modified residuei509 – 5091PhosphoserineCombined sources
Modified residuei510 – 5101PhosphoserineCombined sources
Modified residuei532 – 5321PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated. Mainly undergoes monoubiquitination but also polyubiquitination.1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ3UQN2.
MaxQBiQ3UQN2.
PaxDbiQ3UQN2.
PeptideAtlasiQ3UQN2.
PRIDEiQ3UQN2.

PTM databases

iPTMnetiQ3UQN2.
PhosphoSiteiQ3UQN2.

Expressioni

Tissue specificityi

Ubiquitously expressed (at protein level).1 Publication

Gene expression databases

BgeeiQ3UQN2.
CleanExiMM_FCHO2.
ExpressionAtlasiQ3UQN2. baseline and differential.
GenevisibleiQ3UQN2. MM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked (By similarity). May form homotetramer. Interacts with AP2A1. Interacts with EPS15, EPS15R, ITSN1 and ITSN2; recruit those scaffolding proteins which in turn may interact with the adaptor protein complex AP-2 at the plasma membrane. Interacts with DAB2 (via DPF motifs); mediates LDL receptor/LDLR endocytosis.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A7BFV92EBI-6094986,EBI-6095043From a different organism.
EPS15P425663EBI-6094986,EBI-396684From a different organism.
ITSN1Q158113EBI-6094986,EBI-602041From a different organism.

Protein-protein interaction databases

BioGridi230041. 23 interactions.
DIPiDIP-29489N.
IntActiQ3UQN2. 17 interactions.
MINTiMINT-4113870.
STRINGi10090.ENSMUSP00000042959.

Structurei

3D structure databases

ProteinModelPortaliQ3UQN2.
SMRiQ3UQN2. Positions 3-274.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 250248F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini541 – 808268MHDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3 – 274272Mediates dimerization and binding to membranes enriched in Pi(4,5)-P2 and induces their tubulationAdd
BLAST
Regioni520 – 809290Mediates interaction with DAB2, EPS15, EPS15R and ITSN1By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili87 – 15670Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi444 – 4474Poly-Ser
Compositional biasi507 – 51812Poly-SerAdd
BLAST

Sequence similaritiesi

Belongs to the FCHO family.Curated
Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 MHD (mu homology) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2398. Eukaryota.
ENOG410Y7RY. LUCA.
GeneTreeiENSGT00510000046419.
HOGENOMiHOG000231544.
HOVERGENiHBG081524.
InParanoidiQ3UQN2.
KOiK20042.
OMAiSSTKDFW.
OrthoDBiEOG712TVK.
PhylomeDBiQ3UQN2.
TreeFamiTF328986.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028565. MHD.
IPR018808. Muniscin_C.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF10291. muHD. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
[Graphical view]
PROSITEiPS51741. F_BAR. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3UQN2-1) [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
MVMAHFVENF WGEKNNGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS
60 70 80 90 100
RSMTKLAKSA SNYSQLGTFA PMWDVFKTST EKLANCHLDL VRKLQELIKE
110 120 130 140 150
VQKYGEEQVK SHKKTKEEVA GTLEAVQAIQ NITQALQKSK ENYTAKCVEQ
160 170 180 190 200
ERLKKEGATQ REIEKAAVKS KKATDTYKLY VEKYALTKAD FEQKMTETAQ
210 220 230 240 250
KFQDIEETHL IHIKEIIGSL SNAVKEIHLQ IGQVHEEFIN NMANTTIESL
260 270 280 290 300
IQKFAESKGT GKERPGLIEF EECDPASAVE GIKPRKRKTF ALPGIIKKEK
310 320 330 340 350
DAESVECPDA DSLNIPDVDE EGFSIKPEAN QNDTKENHFY SSSDSDSEDE
360 370 380 390 400
EPKRYRIEIK PAHPNNLHHT MASLDELKVS IGNITLSPAV SRHSPVQMNR
410 420 430 440 450
NSSNEELTKS KPSSLPTEKG TNDLLAWDPL FGSSLESSSA PLTSSSSARP
460 470 480 490 500
TTPLSLGTLV PPPRPASRPK LASGKLSGIN EIPRPFSPPV TSNTSPPPTA
510 520 530 540 550
PLARAESSSS ISSSASLSAA NTPTVGVSRG PSPVSLGNQD TLPVAIALTE
560 570 580 590 600
SVNAYFKGAD PTKCIVKITG DVTISFPSGI IKVFTSNPSP AVLCFRVKNI
610 620 630 640 650
SRLEQILPNS QLVFSDPSQC DSNTKDFWMN MQAVTIYLKK LSEQNPAASY
660 670 680 690 700
YNVDVLKYQV SSNGIQSTPL NLATYWKCSA STTDLRVDYK YNPEAMVAPS
710 720 730 740 750
VLSNIQVVVP VDGGVTNMQS LPPAIWNAEQ MKAFWKLSGI SEKSDSGGSG
760 770 780 790 800
SLRAKFDLSE GPSKPTTLAV QFLSEGNTLS GVDIELVGTG YRLSLVKKRF

ATGRYLADC
Length:809
Mass (Da):88,734
Last modified:October 11, 2005 - v1
Checksum:i79FA8C2AFE6B606B
GO
Isoform 2 (identifier: Q3UQN2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     392-394: RHS → GFL
     395-809: Missing.

Note: No experimental confirmation available.
Show »
Length:394
Mass (Da):44,630
Checksum:i0E1FD6850DDE27F3
GO
Isoform 3 (identifier: Q3UQN2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     404-414: NEELTKSKPSS → SKFDIGIGYFM
     415-809: Missing.

Note: No experimental confirmation available.
Show »
Length:414
Mass (Da):46,967
Checksum:i3535081B39834995
GO

Sequence cautioni

The sequence AAH52456.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH53718.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC27226.1 differs from that shown. Reason: Frameshift at position 11. Curated
The sequence BAC27226.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131E → K in BAC27226 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei392 – 3943RHS → GFL in isoform 2. 1 PublicationVSP_021912
Alternative sequencei395 – 809415Missing in isoform 2. 1 PublicationVSP_021913Add
BLAST
Alternative sequencei404 – 41411NEELTKSKPSS → SKFDIGIGYFM in isoform 3. 1 PublicationVSP_021914Add
BLAST
Alternative sequencei415 – 809395Missing in isoform 3. 1 PublicationVSP_021915Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031041 mRNA. Translation: BAC27226.1. Different initiation.
AK142282 mRNA. Translation: BAE25007.1.
AK146566 mRNA. Translation: BAE27264.1.
BC052456 mRNA. Translation: AAH52456.1. Different initiation.
BC053718 mRNA. Translation: AAH53718.1. Different initiation.
CCDSiCCDS56897.1. [Q3UQN2-1]
RefSeqiNP_766179.2. NM_172591.3. [Q3UQN2-1]
UniGeneiMm.23928.

Genome annotation databases

EnsembliENSMUST00000040340; ENSMUSP00000042959; ENSMUSG00000041685. [Q3UQN2-1]
ENSMUST00000109403; ENSMUSP00000105030; ENSMUSG00000041685. [Q3UQN2-2]
GeneIDi218503.
KEGGimmu:218503.
UCSCiuc011zdl.2. mouse. [Q3UQN2-2]
uc033gnc.1. mouse. [Q3UQN2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031041 mRNA. Translation: BAC27226.1. Different initiation.
AK142282 mRNA. Translation: BAE25007.1.
AK146566 mRNA. Translation: BAE27264.1.
BC052456 mRNA. Translation: AAH52456.1. Different initiation.
BC053718 mRNA. Translation: AAH53718.1. Different initiation.
CCDSiCCDS56897.1. [Q3UQN2-1]
RefSeqiNP_766179.2. NM_172591.3. [Q3UQN2-1]
UniGeneiMm.23928.

3D structure databases

ProteinModelPortaliQ3UQN2.
SMRiQ3UQN2. Positions 3-274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230041. 23 interactions.
DIPiDIP-29489N.
IntActiQ3UQN2. 17 interactions.
MINTiMINT-4113870.
STRINGi10090.ENSMUSP00000042959.

PTM databases

iPTMnetiQ3UQN2.
PhosphoSiteiQ3UQN2.

Proteomic databases

EPDiQ3UQN2.
MaxQBiQ3UQN2.
PaxDbiQ3UQN2.
PeptideAtlasiQ3UQN2.
PRIDEiQ3UQN2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040340; ENSMUSP00000042959; ENSMUSG00000041685. [Q3UQN2-1]
ENSMUST00000109403; ENSMUSP00000105030; ENSMUSG00000041685. [Q3UQN2-2]
GeneIDi218503.
KEGGimmu:218503.
UCSCiuc011zdl.2. mouse. [Q3UQN2-2]
uc033gnc.1. mouse. [Q3UQN2-1]

Organism-specific databases

CTDi115548.
MGIiMGI:3505790. Fcho2.

Phylogenomic databases

eggNOGiKOG2398. Eukaryota.
ENOG410Y7RY. LUCA.
GeneTreeiENSGT00510000046419.
HOGENOMiHOG000231544.
HOVERGENiHBG081524.
InParanoidiQ3UQN2.
KOiK20042.
OMAiSSTKDFW.
OrthoDBiEOG712TVK.
PhylomeDBiQ3UQN2.
TreeFamiTF328986.

Miscellaneous databases

ChiTaRSiFcho2. mouse.
PROiQ3UQN2.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UQN2.
CleanExiMM_FCHO2.
ExpressionAtlasiQ3UQN2. baseline and differential.
GenevisibleiQ3UQN2. MM.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028565. MHD.
IPR018808. Muniscin_C.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF10291. muHD. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
[Graphical view]
PROSITEiPS51741. F_BAR. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1; 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Amnion, Heart and Thymus.
  2. "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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-402 AND SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-387; SER-403; SER-487; SER-492; SER-507; SER-509 AND SER-510, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "FCHo proteins are nucleators of clathrin-mediated endocytosis."
    Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R., McMahon H.T.
    Science 328:1281-1284(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EPS15; EPS15R; ITSN1 AND ITSN2, MUTAGENESIS OF PHE-38; TRP-73; LEU-136; LYS-146; LYS-165; ILE-268 AND LYS-797.
  6. "Characterization of the EFC/F-BAR domain protein, FCHO2."
    Uezu A., Umeda K., Tsujita K., Suetsugu S., Takenawa T., Nakanishi H.
    Genes Cells 16:868-878(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LIPID-BINDING, SUBCELLULAR LOCATION, HOMOOLIGOMERIZATION, INTERACTION WITH EPS15, UBIQUITINATION, TISSUE SPECIFICITY.
  7. "Hotspots organize clathrin-mediated endocytosis by efficient recruitment and retention of nucleating resources."
    Nunez D., Antonescu C., Mettlen M., Liu A., Schmid S.L., Loerke D., Danuser G.
    Traffic 12:1868-1878(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CCV NUCLEATION.
  8. "FCH domain only-2 organizes clathrin-coated structures and interacts with Disabled-2 for low-density lipoprotein receptor endocytosis."
    Mulkearns E.E., Cooper J.A.
    Mol. Biol. Cell 23:1330-1342(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2.

Entry informationi

Entry nameiFCHO2_MOUSE
AccessioniPrimary (citable) accession number: Q3UQN2
Secondary accession number(s): Q3UJ91, Q7TMS9, Q8C0I2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: October 11, 2005
Last modified: July 6, 2016
This is version 87 of the entry and version 1 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.