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Protein

WASH complex subunit FAM21

Gene

Fam21

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes inhibits WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization and is involved in the fission of tubules that serve as transport intermediates during endosome sorting. Mediates the recruitment of the WASH core complex to endosome membranes via binding to phospholipids and VPS35 of the retromer CSC. Mediates the recruitment of the F-actin-capping protein dimer to the WASH core complex probably promoting localized F-actin polymerization needed for vesicle scission. Via its C-terminus binds various phospholipids, most strongly phosphatidylinositol 4-phosphate (PtdIns-4P), phosphatidylinositol 5-phosphate (PtdIns-5P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Required for the association of DNAJC13, SDCCAG3, ANKRD50 with retromer CSC subunit VPS35. Required for the endosomal recruitment of CCC complex subunits COMMD1, CCDC93 and C16orf62 homolog (By similarity).By similarity

GO - Molecular functioni

  1. phosphatidylinositol-3,4,5-trisphosphate binding Source: MGI
  2. phosphatidylinositol-3,4-bisphosphate binding Source: MGI
  3. phosphatidylinositol-3,5-bisphosphate binding Source: MGI
  4. phosphatidylinositol-3-phosphate binding Source: MGI
  5. phosphatidylinositol-4,5-bisphosphate binding Source: MGI
  6. phosphatidylinositol-4-phosphate binding Source: MGI
  7. phosphatidylinositol-5-phosphate binding Source: MGI

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
  2. retrograde transport, endosome to Golgi Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
WASH complex subunit FAM21
Gene namesi
Name:Fam21
Synonyms:D6Wsu116e, Kiaa0592
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:106463. Fam21.

Subcellular locationi

Early endosome membrane By similarity. Cell membrane By similarity

GO - Cellular componenti

  1. early endosome Source: UniProtKB
  2. early endosome membrane Source: UniProtKB-SubCell
  3. endosome Source: MGI
  4. plasma membrane Source: UniProtKB-SubCell
  5. WASH complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13341334WASH complex subunit FAM21PRO_0000317433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei157 – 1571Phosphoserine1 Publication
Modified residuei159 – 1591Phosphoserine1 Publication
Modified residuei284 – 2841Phosphoserine1 Publication
Modified residuei388 – 3881Phosphoserine1 Publication
Modified residuei533 – 5331Phosphoserine1 Publication
Modified residuei613 – 6131Phosphoserine1 Publication
Modified residuei614 – 6141Phosphoserine2 Publications
Modified residuei723 – 7231Phosphoserine1 Publication
Modified residuei747 – 7471Phosphoserine3 Publications
Modified residuei1169 – 11691Phosphoserine1 Publication
Modified residuei1172 – 11721Phosphoserine1 Publication
Modified residuei1173 – 11731Phosphoserine1 Publication
Modified residuei1333 – 13331Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6PGL7.
PaxDbiQ6PGL7.
PRIDEiQ6PGL7.

PTM databases

PhosphoSiteiQ6PGL7.

Expressioni

Gene expression databases

BgeeiQ6PGL7.
ExpressionAtlasiQ6PGL7. baseline and differential.
GenevestigatoriQ6PGL7.

Interactioni

Subunit structurei

Component of the WASH core complex also described as WASH regulatory complex SHRC composed of WASH1, FAM21, KIAA1033/ SWIP, KIAA0196/strumpellin and CCDC53; in the complex interacts (via N-terminus) directly with WASH1. The WASH core complex associates with the F-actin-capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or substoichiometric manner which was initially described as WASH complex. Interacts with VPS35; mediates the association with the retromer CSC complex. Interacts with FKBP15. Interacts with CCDC93, CCDC22, C16orf62 homolog; indicative for an association of the WASH core complex with the CCC complex (By similarity).By similarity

Protein-protein interaction databases

IntActiQ6PGL7. 3 interactions.
MINTiMINT-1864605.

Structurei

3D structure databases

ProteinModelPortaliQ6PGL7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 219219Sufficient for interaction with KIAA1033/SWIP, KIAA0196/strumpellin and CCDC53; required for interaction with WASH1By similarityAdd
BLAST
Regioni347 – 594248Sufficient for interaction with CCDC93By similarityAdd
BLAST
Regioni348 – 1334987Interaction with VPS35By similarityAdd
BLAST
Regioni932 – 1334403Interaction with phospholipidsBy similarityAdd
BLAST
Regioni1024 – 104219Required for interaction with F-actin-capping protein subunit alpha (CAPZA1 or CAPZA2 or CAPZA3)By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi358 – 36811LFa 1By similarityAdd
BLAST
Motifi441 – 45717LFa 2By similarityAdd
BLAST
Motifi476 – 48510LFa 3By similarity
Motifi531 – 54212LFa 4By similarityAdd
BLAST
Motifi566 – 57712LFa 5By similarityAdd
BLAST
Motifi658 – 67013LFa 6By similarityAdd
BLAST
Motifi686 – 69813LFa 7By similarityAdd
BLAST
Motifi835 – 8439LFa 8By similarity
Motifi852 – 8587LFa 9By similarity
Motifi874 – 88411LFa 10By similarityAdd
BLAST
Motifi1124 – 11318LFa 11By similarity
Motifi1164 – 117815LFa 12By similarityAdd
BLAST
Motifi1194 – 12029LFa 13By similarity
Motifi1227 – 12337LFa 14By similarity
Motifi1255 – 12639LFa 15By similarity
Motifi1283 – 129210LFa 16By similarity
Motifi1323 – 13319LFa 17By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi221 – 2288Poly-Glu
Compositional biasi443 – 45311Poly-AspAdd
BLAST
Compositional biasi661 – 6655Poly-Asp
Compositional biasi780 – 7834Poly-Ser

Domaini

The LFa (leucine-phenylalanine-acidic) motif bind directly to VPS35 of retromer CSC; adjacent motifs can act cooperatively to bind multiple CSCs, although there is significant variability in the affinities of different motifs for retromer.By similarity

Sequence similaritiesi

Belongs to the FAM21 family.Curated

Phylogenomic databases

eggNOGiNOG76301.
GeneTreeiENSGT00510000047694.
HOGENOMiHOG000112469.
HOVERGENiHBG055529.
InParanoidiQ6PGL7.
KOiK18462.
OMAiHSDNDQN.
OrthoDBiEOG7GBFWP.
PhylomeDBiQ6PGL7.
TreeFamiTF329309.

Family and domain databases

InterProiIPR027308. FAM21.
IPR029341. FAM21/CAPZIP.
[Graphical view]
PANTHERiPTHR21669:SF4. PTHR21669:SF4. 1 hit.
PfamiPF15255. CAP-ZIP_m. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q6PGL7-1) [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
MNRTSPDSER PPASEPVWER PWSVEEIRRS SQNWSLAADA GLLQFLQEFS
60 70 80 90 100
QQTISRTHEI KKQVDGLIQE TKATHCRLHN VFNDFLMLSN TQFIENRVYD
110 120 130 140 150
EEVEEQVLKA EAEKAEQEKT REQKEIDLIP KVQEAVNYGL QVLDSAFEQL
160 170 180 190 200
DIKAGNSDSE EDDANERVDL ILEPKDLYID RPLPYLIGSK LFMEQEDVGL
210 220 230 240 250
GELSSEEGSV GSDRGSIVDS EDEKEEEESD EDFASHSDND QNQHTTQISD
260 270 280 290 300
EEEDDDGDLF ADSEKEGDDI EDIEESAKSK RPTSFADELA ARIKGDISNQ
310 320 330 340 350
RKEGQTDGKP QKTVKEKKER RTPADDEEDI LFPPPTLTDE DFSPFGSRGG
360 370 380 390 400
LFSNGQGLFD DEDESDLFKE APRARPAQAP VSEELPPSPK PGKKIPAGAV
410 420 430 440 450
SVLLGHPDVS GSTSAPSLKE LQKHGQPTPG KSSHLPTPAG LFDDDDNDND
460 470 480 490 500
EDDNNFFMPS SSKPSKTDKV KSTAIIFDDD EGDLFKEKAE ALPAASVSQT
510 520 530 540 550
HESKTRADKT IALPSSKNLK LVSETKTQKG LFSDEEDSED LFSSQSSSKP
560 570 580 590 600
KSASLPSSQP PTSVSLFGDE DEEDSLFGSA AAKKQTSSLQ PQSQEKAKPS
610 620 630 640 650
EQPSKKTSAL LFSSDEEDQW NIADSHTKLA SDNKSKGELW DSGATQGQEA
660 670 680 690 700
KAVKKTNLFE DDDDDEVDLF AIAKDSQKKT QRTSLLFEDD AESGSSLFGL
710 720 730 740 750
PPTSVPSATT KKESVPKVPL LFSDEEDSEV PSGVKPEDLK VDNARVSPEV
760 770 780 790 800
GSADVASIAQ KEGLLPASDQ EAGGPSDIFS SSSPLDKGAK GRTRTVLSLF
810 820 830 840 850
DEDEDKVEDE SSTCAPQDGR EKGLKTDSRP KSTGVFQDEE LLFSHKLQKD
860 870 880 890 900
NDPDVDLFAG TKKIRSSVPS GGSLFGDDED DDLFSSAKTQ PVVPEKKGTL
910 920 930 940 950
KKDHPVSLKN QDPLDSTQGS KEKSTWKTEP AQDSSGLTPF KSREPSSRIG
960 970 980 990 1000
KIQANLAINP AALLPTVALQ IPGTKPVSSE LAFPSSEPGR SHILESVPTL
1010 1020 1030 1040 1050
PGSVEAGVSF DLPAQADTLH SANKSRVKVR GKRRPQTRAA RRLAAQESSE
1060 1070 1080 1090 1100
AEDVTVDRGP VAQLSSSPVL PNGHQPLLQP RMASGQTSSE TATAPPWEGG
1110 1120 1130 1140 1150
PVLSAADRSF FVKSRPQTGN EADLFDSGDI FPKSRGSQSV EGAGVMAGEP
1160 1170 1180 1190 1200
PSHSSGGRKE KSLAFPDLSE GSSTEDLFQS VKPRAAKNRN PFPLLEDEED
1210 1220 1230 1240 1250
LFADPRGKKN ERKPDSHQDS VSKTHDIFED DIFATEAIKP FPKKREKGRT
1260 1270 1280 1290 1300
LEPNLFDDNI DIFADLTVKP KEKSKKKVAA KSMFDDDTDD IFSSGLQAKA
1310 1320 1330
SKPKSQSAEA ASEQRSEHKV ASIFDDPLNA FGSQ
Length:1,334
Mass (Da):145,311
Last modified:July 4, 2004 - v1
Checksum:iAD35C3FFAC27C159
GO
Isoform 2 (identifier: Q6PGL7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     866-952: SSVPSGGSLF...REPSSRIGKI → V

Note: No experimental confirmation available.

Show »
Length:1,248
Mass (Da):136,082
Checksum:i410A9852587F5DB7
GO

Sequence cautioni

The sequence AAH49979.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti385 – 3851L → S in AAH49979 (PubMed:15489334).Curated
Sequence conflicti556 – 5561P → S in AAH49979 (PubMed:15489334).Curated
Sequence conflicti630 – 6301A → V in BAC65602 (PubMed:12693553).Curated
Sequence conflicti910 – 9101N → S in BAC29966 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei866 – 95287SSVPS…RIGKI → V in isoform 2. 1 PublicationVSP_030949Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122320 Transcribed RNA. Translation: BAC65602.2.
AK163765 mRNA. Translation: BAE37485.1.
AK038318 mRNA. Translation: BAC29966.1.
BC049979 mRNA. Translation: AAH49979.1. Sequence problems.
BC056942 mRNA. Translation: AAH56942.1.
CCDSiCCDS20450.1. [Q6PGL7-1]
RefSeqiNP_080861.2. NM_026585.3. [Q6PGL7-1]
UniGeneiMm.28524.

Genome annotation databases

EnsembliENSMUST00000036759; ENSMUSP00000038983; ENSMUSG00000024104. [Q6PGL7-1]
GeneIDi28006.
KEGGimmu:28006.
UCSCiuc009djs.2. mouse. [Q6PGL7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122320 Transcribed RNA. Translation: BAC65602.2.
AK163765 mRNA. Translation: BAE37485.1.
AK038318 mRNA. Translation: BAC29966.1.
BC049979 mRNA. Translation: AAH49979.1. Sequence problems.
BC056942 mRNA. Translation: AAH56942.1.
CCDSiCCDS20450.1. [Q6PGL7-1]
RefSeqiNP_080861.2. NM_026585.3. [Q6PGL7-1]
UniGeneiMm.28524.

3D structure databases

ProteinModelPortaliQ6PGL7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6PGL7. 3 interactions.
MINTiMINT-1864605.

PTM databases

PhosphoSiteiQ6PGL7.

Proteomic databases

MaxQBiQ6PGL7.
PaxDbiQ6PGL7.
PRIDEiQ6PGL7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036759; ENSMUSP00000038983; ENSMUSG00000024104. [Q6PGL7-1]
GeneIDi28006.
KEGGimmu:28006.
UCSCiuc009djs.2. mouse. [Q6PGL7-1]

Organism-specific databases

CTDi28006.
MGIiMGI:106463. Fam21.
RougeiSearch...

Phylogenomic databases

eggNOGiNOG76301.
GeneTreeiENSGT00510000047694.
HOGENOMiHOG000112469.
HOVERGENiHBG055529.
InParanoidiQ6PGL7.
KOiK18462.
OMAiHSDNDQN.
OrthoDBiEOG7GBFWP.
PhylomeDBiQ6PGL7.
TreeFamiTF329309.

Miscellaneous databases

NextBioi306510.
PROiQ6PGL7.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PGL7.
ExpressionAtlasiQ6PGL7. baseline and differential.
GenevestigatoriQ6PGL7.

Family and domain databases

InterProiIPR027308. FAM21.
IPR029341. FAM21/CAPZIP.
[Graphical view]
PANTHERiPTHR21669:SF4. PTHR21669:SF4. 1 hit.
PfamiPF15255. CAP-ZIP_m. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Head and Thymus.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6 and FVB/N-3.
    Tissue: Brain and Mammary tumor.
  4. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-284; SER-388; SER-533; SER-613; SER-614; SER-723; SER-747; SER-1169; SER-1172; SER-1173 AND SER-1333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614 AND SER-747, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiFAM21_MOUSE
AccessioniPrimary (citable) accession number: Q6PGL7
Secondary accession number(s): Q3TQ99
, Q80TW8, Q80UQ4, Q8CAP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 4, 2008
Last sequence update: July 4, 2004
Last modified: March 31, 2015
This is version 68 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

External Data

Dasty 3

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 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.