Q6PGL7 (FAM21_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
WASH complex subunit FAM21

Gene names

Name:	Fam21
Synonyms:	D6Wsu116e, Kiaa0592

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1334 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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.
Subcellular location	Early endosome membrane By similarity.
Sequence similarities	Belongs to the FAM21 family.
Sequence caution	The sequence AAH49979.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Transport
Cellular component	Endosome Membrane
Coding sequence diversity	Alternative splicing
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	retrograde transport, endosome to Golgi Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	WASH complex Inferred from sequence or structural similarity. Source: UniProtKB early endosome Inferred from sequence or structural similarity. Source: UniProtKB early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6PGL7-1)

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.

Isoform 2 (identifier: Q6PGL7-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1334	1334	WASH complex subunit FAM21		PRO_0000317433
Regions
	Compositional bias	221 – 228	8	Poly-Glu
	Compositional bias	443 – 453	11	Poly-Asp
	Compositional bias	661 – 665	5	Poly-Asp
	Compositional bias	780 – 783	4	Poly-Ser
Amino acid modifications
	Modified residue	157	1	Phosphoserine Ref.7 Ref.8
	Modified residue	159	1	Phosphoserine Ref.7 Ref.8
	Modified residue	388	1	Phosphoserine Ref.8
	Modified residue	533	1	Phosphoserine Ref.7 Ref.8
	Modified residue	613	1	Phosphoserine Ref.8
	Modified residue	614	1	Phosphoserine Ref.6 Ref.8 Ref.9
	Modified residue	723	1	Phosphoserine Ref.7 Ref.8
	Modified residue	747	1	Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
	Modified residue	793	1	Phosphothreonine Ref.4
	Modified residue	795	1	Phosphothreonine Ref.4
	Modified residue	798	1	Phosphoserine Ref.6
	Modified residue	870	1	Phosphoserine Ref.6
	Modified residue	1049	1	Phosphoserine Ref.4
	Modified residue	1067	1	Phosphoserine Ref.6
	Modified residue	1172	1	Phosphoserine Ref.8
	Modified residue	1173	1	Phosphoserine Ref.8
	Modified residue	1222	1	Phosphoserine Ref.8
	Modified residue	1333	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	866 – 952	87	SSVPS…RIGKI → V in isoform 2.		VSP_030949
Experimental info
	Sequence conflict	385	1	L → S in AAH49979. Ref.3
	Sequence conflict	556	1	P → S in AAH49979. Ref.3
	Sequence conflict	630	1	A → V in BAC65602. Ref.1
	Sequence conflict	910	1	N → S in BAC29966. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: AD35C3FFAC27C159	FASTA	1,334	145,311
	10 20 30 40 50 60 MNRTSPDSER PPASEPVWER PWSVEEIRRS SQNWSLAADA GLLQFLQEFS QQTISRTHEI 70 80 90 100 110 120 KKQVDGLIQE TKATHCRLHN VFNDFLMLSN TQFIENRVYD EEVEEQVLKA EAEKAEQEKT 130 140 150 160 170 180 REQKEIDLIP KVQEAVNYGL QVLDSAFEQL DIKAGNSDSE EDDANERVDL ILEPKDLYID 190 200 210 220 230 240 RPLPYLIGSK LFMEQEDVGL GELSSEEGSV GSDRGSIVDS EDEKEEEESD EDFASHSDND 250 260 270 280 290 300 QNQHTTQISD EEEDDDGDLF ADSEKEGDDI EDIEESAKSK RPTSFADELA ARIKGDISNQ 310 320 330 340 350 360 RKEGQTDGKP QKTVKEKKER RTPADDEEDI LFPPPTLTDE DFSPFGSRGG LFSNGQGLFD 370 380 390 400 410 420 DEDESDLFKE APRARPAQAP VSEELPPSPK PGKKIPAGAV SVLLGHPDVS GSTSAPSLKE 430 440 450 460 470 480 LQKHGQPTPG KSSHLPTPAG LFDDDDNDND EDDNNFFMPS SSKPSKTDKV KSTAIIFDDD 490 500 510 520 530 540 EGDLFKEKAE ALPAASVSQT HESKTRADKT IALPSSKNLK LVSETKTQKG LFSDEEDSED 550 560 570 580 590 600 LFSSQSSSKP KSASLPSSQP PTSVSLFGDE DEEDSLFGSA AAKKQTSSLQ PQSQEKAKPS 610 620 630 640 650 660 EQPSKKTSAL LFSSDEEDQW NIADSHTKLA SDNKSKGELW DSGATQGQEA KAVKKTNLFE 670 680 690 700 710 720 DDDDDEVDLF AIAKDSQKKT QRTSLLFEDD AESGSSLFGL PPTSVPSATT KKESVPKVPL 730 740 750 760 770 780 LFSDEEDSEV PSGVKPEDLK VDNARVSPEV GSADVASIAQ KEGLLPASDQ EAGGPSDIFS 790 800 810 820 830 840 SSSPLDKGAK GRTRTVLSLF DEDEDKVEDE SSTCAPQDGR EKGLKTDSRP KSTGVFQDEE 850 860 870 880 890 900 LLFSHKLQKD NDPDVDLFAG TKKIRSSVPS GGSLFGDDED DDLFSSAKTQ PVVPEKKGTL 910 920 930 940 950 960 KKDHPVSLKN QDPLDSTQGS KEKSTWKTEP AQDSSGLTPF KSREPSSRIG KIQANLAINP 970 980 990 1000 1010 1020 AALLPTVALQ IPGTKPVSSE LAFPSSEPGR SHILESVPTL PGSVEAGVSF DLPAQADTLH 1030 1040 1050 1060 1070 1080 SANKSRVKVR GKRRPQTRAA RRLAAQESSE AEDVTVDRGP VAQLSSSPVL PNGHQPLLQP 1090 1100 1110 1120 1130 1140 RMASGQTSSE TATAPPWEGG PVLSAADRSF FVKSRPQTGN EADLFDSGDI FPKSRGSQSV 1150 1160 1170 1180 1190 1200 EGAGVMAGEP PSHSSGGRKE KSLAFPDLSE GSSTEDLFQS VKPRAAKNRN PFPLLEDEED 1210 1220 1230 1240 1250 1260 LFADPRGKKN ERKPDSHQDS VSKTHDIFED DIFATEAIKP FPKKREKGRT LEPNLFDDNI 1270 1280 1290 1300 1310 1320 DIFADLTVKP KEKSKKKVAA KSMFDDDTDD IFSSGLQAKA SKPKSQSAEA ASEQRSEHKV 1330 ASIFDDPLNA FGSQ
	Isoform 2 [UniParc]. Checksum: 410A9852587F5DB7	FASTA	1,248	136,082
	10 20 30 40 50 60 MNRTSPDSER PPASEPVWER PWSVEEIRRS SQNWSLAADA GLLQFLQEFS QQTISRTHEI 70 80 90 100 110 120 KKQVDGLIQE TKATHCRLHN VFNDFLMLSN TQFIENRVYD EEVEEQVLKA EAEKAEQEKT 130 140 150 160 170 180 REQKEIDLIP KVQEAVNYGL QVLDSAFEQL DIKAGNSDSE EDDANERVDL ILEPKDLYID 190 200 210 220 230 240 RPLPYLIGSK LFMEQEDVGL GELSSEEGSV GSDRGSIVDS EDEKEEEESD EDFASHSDND 250 260 270 280 290 300 QNQHTTQISD EEEDDDGDLF ADSEKEGDDI EDIEESAKSK RPTSFADELA ARIKGDISNQ 310 320 330 340 350 360 RKEGQTDGKP QKTVKEKKER RTPADDEEDI LFPPPTLTDE DFSPFGSRGG LFSNGQGLFD 370 380 390 400 410 420 DEDESDLFKE APRARPAQAP VSEELPPSPK PGKKIPAGAV SVLLGHPDVS GSTSAPSLKE 430 440 450 460 470 480 LQKHGQPTPG KSSHLPTPAG LFDDDDNDND EDDNNFFMPS SSKPSKTDKV KSTAIIFDDD 490 500 510 520 530 540 EGDLFKEKAE ALPAASVSQT HESKTRADKT IALPSSKNLK LVSETKTQKG LFSDEEDSED 550 560 570 580 590 600 LFSSQSSSKP KSASLPSSQP PTSVSLFGDE DEEDSLFGSA AAKKQTSSLQ PQSQEKAKPS 610 620 630 640 650 660 EQPSKKTSAL LFSSDEEDQW NIADSHTKLA SDNKSKGELW DSGATQGQEA KAVKKTNLFE 670 680 690 700 710 720 DDDDDEVDLF AIAKDSQKKT QRTSLLFEDD AESGSSLFGL PPTSVPSATT KKESVPKVPL 730 740 750 760 770 780 LFSDEEDSEV PSGVKPEDLK VDNARVSPEV GSADVASIAQ KEGLLPASDQ EAGGPSDIFS 790 800 810 820 830 840 SSSPLDKGAK GRTRTVLSLF DEDEDKVEDE SSTCAPQDGR EKGLKTDSRP KSTGVFQDEE 850 860 870 880 890 900 LLFSHKLQKD NDPDVDLFAG TKKIRVQANL AINPAALLPT VALQIPGTKP VSSELAFPSS 910 920 930 940 950 960 EPGRSHILES VPTLPGSVEA GVSFDLPAQA DTLHSANKSR VKVRGKRRPQ TRAARRLAAQ 970 980 990 1000 1010 1020 ESSEAEDVTV DRGPVAQLSS SPVLPNGHQP LLQPRMASGQ TSSETATAPP WEGGPVLSAA 1030 1040 1050 1060 1070 1080 DRSFFVKSRP QTGNEADLFD SGDIFPKSRG SQSVEGAGVM AGEPPSHSSG GRKEKSLAFP 1090 1100 1110 1120 1130 1140 DLSEGSSTED LFQSVKPRAA KNRNPFPLLE DEEDLFADPR GKKNERKPDS HQDSVSKTHD 1150 1160 1170 1180 1190 1200 IFEDDIFATE AIKPFPKKRE KGRTLEPNLF DDNIDIFADL TVKPKEKSKK KVAAKSMFDD 1210 1220 1230 1240 DTDDIFSSGL QAKASKPKSQ SAEAASEQRS EHKVASIFDD PLNAFGSQ

References

[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]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-793; THR-795 AND SER-1049, MASS SPECTROMETRY. Tissue: Liver.
[5]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, MASS SPECTROMETRY. Tissue: Brain cortex.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614; SER-747; SER-798; SER-870 AND SER-1067, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-533; SER-723 AND SER-747, MASS SPECTROMETRY. Tissue: Melanoma.
[8]	"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-388; SER-533; SER-613; SER-614; SER-723; SER-747; SER-1172; SER-1173; SER-1222 AND SER-1333, MASS SPECTROMETRY. Tissue: Macrophage.
[9]	"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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00468516. IPI00886310.
RefSeq	NP_080861.2. NM_026585.3.
UniGene	Mm.28524.
3D structure databases
ProteinModelPortal	Q6PGL7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6PGL7. 2 interactions.
MINT	MINT-1864605.
PTM databases
PhosphoSite	Q6PGL7.
Proteomic databases
PaxDb	Q6PGL7.
PRIDE	Q6PGL7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000036759; ENSMUSP00000038983; ENSMUSG00000024104.
GeneID	28006.
KEGG	mmu:28006.
UCSC	uc009djs.2. mouse.
Organism-specific databases
CTD	28006.
MGI	MGI:106463. Fam21.
Rouge	Search...
Phylogenomic databases
eggNOG	NOG76301.
GeneTree	ENSGT00510000047694.
HOGENOM	HOG000112469.
HOVERGEN	HBG055529.
InParanoid	Q6PGL7.
OMA	VRGKRRP.
OrthoDB	EOG4NVZJX.
Gene expression databases
ArrayExpress	Q6PGL7.
Bgee	Q6PGL7.
Genevestigator	Q6PGL7.
Family and domain databases
InterPro	IPR027308. FAM21. [Graphical view]
PANTHER	PTHR21669:SF4. PTHR21669:SF4. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	D6Wsu116e. mouse.
NextBio	306510.
SOURCE	Search...

Entry information

Entry name

FAM21_MOUSE

Accession

Primary (citable) accession number: Q6PGL7
Secondary accession number(s): Q3TQ99 , Q80TW8, Q80UQ4, Q8CAP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program