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Q6PGL7

- FAM21_MOUSE

UniProt

Q6PGL7 - FAM21_MOUSE

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Protein
WASH complex subunit FAM21
Gene
Fam21, D6Wsu116e, Kiaa0592
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the WASH complex, a complex present at the surface of endosomes that recruits and activates the Arp2/3 complex to induce actin polymerization. The WASH complex plays a key role in the fission of tubules that serve as transport intermediates during endosome sorting. In the complex, it probably mediates the recruitment of the complex to endosome membranes By similarity.

GO - Biological processi

  1. retrograde transport, endosome to Golgi Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

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: Chromosome 6

Organism-specific databases

MGIiMGI:106463. Fam21.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13341334WASH complex subunit FAM21
PRO_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

ArrayExpressiQ6PGL7.
BgeeiQ6PGL7.
GenevestigatoriQ6PGL7.

Interactioni

Subunit structurei

Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH1, FAM21, KIAA1033, KIAA0196 and CCDC53 By similarity. Interacts (via WHD1 region) with WASH1; the interaction is direct By similarity.

Protein-protein interaction databases

IntActiQ6PGL7. 3 interactions.
MINTiMINT-1864605.

Structurei

3D structure databases

ProteinModelPortaliQ6PGL7.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Belongs to the FAM21 family.

Phylogenomic databases

eggNOGiNOG76301.
GeneTreeiENSGT00510000047694.
HOGENOMiHOG000112469.
HOVERGENiHBG055529.
InParanoidiQ6PGL7.
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. Align

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

MNRTSPDSER PPASEPVWER PWSVEEIRRS SQNWSLAADA GLLQFLQEFS     50
QQTISRTHEI KKQVDGLIQE TKATHCRLHN VFNDFLMLSN TQFIENRVYD 100
EEVEEQVLKA EAEKAEQEKT REQKEIDLIP KVQEAVNYGL QVLDSAFEQL 150
DIKAGNSDSE EDDANERVDL ILEPKDLYID RPLPYLIGSK LFMEQEDVGL 200
GELSSEEGSV GSDRGSIVDS EDEKEEEESD EDFASHSDND QNQHTTQISD 250
EEEDDDGDLF ADSEKEGDDI EDIEESAKSK RPTSFADELA ARIKGDISNQ 300
RKEGQTDGKP QKTVKEKKER RTPADDEEDI LFPPPTLTDE DFSPFGSRGG 350
LFSNGQGLFD DEDESDLFKE APRARPAQAP VSEELPPSPK PGKKIPAGAV 400
SVLLGHPDVS GSTSAPSLKE LQKHGQPTPG KSSHLPTPAG LFDDDDNDND 450
EDDNNFFMPS SSKPSKTDKV KSTAIIFDDD EGDLFKEKAE ALPAASVSQT 500
HESKTRADKT IALPSSKNLK LVSETKTQKG LFSDEEDSED LFSSQSSSKP 550
KSASLPSSQP PTSVSLFGDE DEEDSLFGSA AAKKQTSSLQ PQSQEKAKPS 600
EQPSKKTSAL LFSSDEEDQW NIADSHTKLA SDNKSKGELW DSGATQGQEA 650
KAVKKTNLFE DDDDDEVDLF AIAKDSQKKT QRTSLLFEDD AESGSSLFGL 700
PPTSVPSATT KKESVPKVPL LFSDEEDSEV PSGVKPEDLK VDNARVSPEV 750
GSADVASIAQ KEGLLPASDQ EAGGPSDIFS SSSPLDKGAK GRTRTVLSLF 800
DEDEDKVEDE SSTCAPQDGR EKGLKTDSRP KSTGVFQDEE LLFSHKLQKD 850
NDPDVDLFAG TKKIRSSVPS GGSLFGDDED DDLFSSAKTQ PVVPEKKGTL 900
KKDHPVSLKN QDPLDSTQGS KEKSTWKTEP AQDSSGLTPF KSREPSSRIG 950
KIQANLAINP AALLPTVALQ IPGTKPVSSE LAFPSSEPGR SHILESVPTL 1000
PGSVEAGVSF DLPAQADTLH SANKSRVKVR GKRRPQTRAA RRLAAQESSE 1050
AEDVTVDRGP VAQLSSSPVL PNGHQPLLQP RMASGQTSSE TATAPPWEGG 1100
PVLSAADRSF FVKSRPQTGN EADLFDSGDI FPKSRGSQSV EGAGVMAGEP 1150
PSHSSGGRKE KSLAFPDLSE GSSTEDLFQS VKPRAAKNRN PFPLLEDEED 1200
LFADPRGKKN ERKPDSHQDS VSKTHDIFED DIFATEAIKP FPKKREKGRT 1250
LEPNLFDDNI DIFADLTVKP KEKSKKKVAA KSMFDDDTDD IFSSGLQAKA 1300
SKPKSQSAEA ASEQRSEHKV ASIFDDPLNA FGSQ 1334
Length:1,334
Mass (Da):145,311
Last modified:July 5, 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. Reason: Contaminating sequence. Potential poly-A sequence.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei866 – 95287SSVPS…RIGKI → V in isoform 2.
VSP_030949Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti385 – 3851L → S in AAH49979. 1 Publication
Sequence conflicti556 – 5561P → S in AAH49979. 1 Publication
Sequence conflicti630 – 6301A → V in BAC65602. 1 Publication
Sequence conflicti910 – 9101N → S in BAC29966. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS20450.1. [Q6PGL7-1 ]
RefSeqi NP_080861.2. NM_026585.3. [Q6PGL7-1 ]
UniGenei Mm.28524.

3D structure databases

ProteinModelPortali Q6PGL7.
ModBasei Search...

Protein-protein interaction databases

IntActi Q6PGL7. 3 interactions.
MINTi MINT-1864605.

PTM databases

PhosphoSitei Q6PGL7.

Proteomic databases

MaxQBi Q6PGL7.
PaxDbi Q6PGL7.
PRIDEi Q6PGL7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000036759 ; ENSMUSP00000038983 ; ENSMUSG00000024104 . [Q6PGL7-1 ]
GeneIDi 28006.
KEGGi mmu:28006.
UCSCi uc009djs.2. mouse. [Q6PGL7-1 ]

Organism-specific databases

CTDi 28006.
MGIi MGI:106463. Fam21.
Rougei Search...

Phylogenomic databases

eggNOGi NOG76301.
GeneTreei ENSGT00510000047694.
HOGENOMi HOG000112469.
HOVERGENi HBG055529.
InParanoidi Q6PGL7.
OMAi HSDNDQN.
OrthoDBi EOG7GBFWP.
PhylomeDBi Q6PGL7.
TreeFami TF329309.

Miscellaneous databases

ChiTaRSi D6Wsu116e. mouse.
NextBioi 306510.
PROi Q6PGL7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6PGL7.
Bgeei Q6PGL7.
Genevestigatori Q6PGL7.

Family and domain databases

InterProi IPR027308. FAM21.
IPR029341. FAM21/CAPZIP.
[Graphical view ]
PANTHERi PTHR21669:SF4. PTHR21669:SF4. 1 hit.
Pfami PF15255. CAP-ZIP_m. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2003) [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(2005) [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(2004) [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(2007) [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(2009) [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(2009) [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 5, 2008
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 62 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

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