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WASH complex subunit 2A

 WAC2A_HUMAN             Reviewed;        1341 AA.
Q641Q2; A2A3S2; A2A3U6; Q5SNT6; Q6DHY0;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 3.
20-JUN-2018, entry version 107.
RecName: Full=WASH complex subunit 2A {ECO:0000312|HGNC:HGNC:23416};
Name=WASHC2A {ECO:0000312|HGNC:HGNC:23416};
Synonyms=FAM21A {ECO:0000312|HGNC:HGNC:23416},
FAM21B {ECO:0000312|HGNC:HGNC:23416};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Eye, and Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539; SER-1087 AND
SER-1114, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539; SER-1087 AND
SER-1114, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539 AND SER-1114, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539 AND SER-1054, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
INTERACTION WITH TBC1D23.
PubMed=29084197; DOI=10.1038/ncb3627;
Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
"TBC1D23 is a bridging factor for endosomal vesicle capture by golgins
at the trans-Golgi.";
Nat. Cell Biol. 19:1424-1432(2017).
-!- FUNCTION: 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-(4)P), phosphatidylinositol 5-phosphate (PtdIns-(5)P) 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. Plays a role in
fluid-phase endocytosis, a process exploited by vaccinia
intracellular mature virus (IMV) to enter cells. As a result, may
facilitate the penetration of IMV into cells (By similarity).
{ECO:0000250|UniProtKB:Q9Y4E1}.
-!- SUBUNIT: Component of the WASH core complex also described as WASH
regulatory complex (SHRC) composed of WASH (WASHC1, WASH2P or
WASH3P), WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5;
in the complex interacts (via N-terminus) directly with WASHC1.
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; indicative for an
association of the WASH core complex with the CCC complex (By
similarity). Directly interacts with TBC1D23 (PubMed:29084197).
{ECO:0000250|UniProtKB:Q9Y4E1, ECO:0000269|PubMed:29084197}.
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000250|UniProtKB:Q9Y4E1}. Cell membrane
{ECO:0000250|UniProtKB:Q9Y4E1}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q641Q2-1; Sequence=Displayed;
Name=2;
IsoId=Q641Q2-2; Sequence=VSP_030948;
-!- DOMAIN: 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.
{ECO:0000250|UniProtKB:Q9Y4E1}.
-!- MISCELLANEOUS: In human, WASHC2 has undergone evolutionary
duplication, with 4 highly homologous family members existing,
including WASHC2A, WASHC2C, and an N-terminally truncated WASHC2D
form.
-!- SIMILARITY: Belongs to the FAM21 family. {ECO:0000305}.
-!- CAUTION: A WASHC2C construct with WASHC2A-specific sequence
insertions has been used in a number of experiments; the results
are included in the WASHC2C entry. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI17187.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AL442003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL450382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL954360; CAI17187.1; ALT_SEQ; Genomic_DNA.
EMBL; BC075815; AAH75815.1; -; mRNA.
EMBL; BC082258; AAH82258.2; -; mRNA.
CCDS; CCDS41527.1; -. [Q641Q2-1]
CCDS; CCDS76303.1; -. [Q641Q2-2]
RefSeq; NP_001005751.1; NM_001005751.2. [Q641Q2-1]
RefSeq; NP_001278327.1; NM_001291398.1. [Q641Q2-2]
UniGene; Hs.365286; -.
UniGene; Hs.449662; -.
UniGene; Hs.645272; -.
ProteinModelPortal; Q641Q2; -.
SMR; Q641Q2; -.
BioGrid; 132390; 37.
ComplexPortal; CPX-1172; WASH complex, variant WASHC1/WASHC2A.
ComplexPortal; CPX-1173; WASH complex, variant WASH2P/WASHC2A.
ComplexPortal; CPX-1174; WASH complex, variant WASH3P/WASHC2A.
ComplexPortal; CPX-1175; WASH complex, variant WASH4P/WASHC2A.
ComplexPortal; CPX-1176; WASH complex, variant WASH6P/WASHC2A.
CORUM; Q641Q2; -.
IntAct; Q641Q2; 25.
STRING; 9606.ENSP00000282633; -.
iPTMnet; Q641Q2; -.
PhosphoSitePlus; Q641Q2; -.
BioMuta; FAM21A; -.
BioMuta; FAM21B; -.
DMDM; 166971548; -.
DMDM; 166971555; -.
EPD; Q641Q2; -.
MaxQB; Q641Q2; -.
PaxDb; Q641Q2; -.
PeptideAtlas; Q641Q2; -.
PRIDE; Q641Q2; -.
ProteomicsDB; 63762; -.
ProteomicsDB; 65910; -.
ProteomicsDB; 65911; -. [Q641Q2-2]
Ensembl; ENST00000282633; ENSP00000282633; ENSG00000099290. [Q641Q2-1]
Ensembl; ENST00000351071; ENSP00000344037; ENSG00000099290. [Q641Q2-2]
GeneID; 387680; -.
KEGG; hsa:387680; -.
UCSC; uc001jjb.4; human. [Q641Q2-1]
CTD; 387680; -.
EuPathDB; HostDB:ENSG00000099290.15; -.
GeneCards; WASHC2A; -.
H-InvDB; HIX0008825; -.
H-InvDB; HIX0025987; -.
HGNC; HGNC:23416; WASHC2A.
HPA; HPA047844; -.
HPA; HPA060975; -.
HPA; HPA061022; -.
neXtProt; NX_Q641Q2; -.
PharmGKB; PA134877872; -.
PharmGKB; PA134902481; -.
eggNOG; ENOG410IEJH; Eukaryota.
eggNOG; ENOG4110AMY; LUCA.
GeneTree; ENSGT00510000047694; -.
HOGENOM; HOG000112469; -.
HOVERGEN; HBG055529; -.
InParanoid; Q641Q2; -.
KO; K18462; -.
OMA; RIHTIFY; -.
OrthoDB; EOG091G05P8; -.
PhylomeDB; Q641Q2; -.
TreeFam; TF329309; -.
GenomeRNAi; 387680; -.
PRO; PR:Q641Q2; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000099290; -.
CleanEx; HS_FAM21A; -.
CleanEx; HS_FAM21B; -.
ExpressionAtlas; Q641Q2; baseline and differential.
Genevisible; Q641Q2; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
InterPro; IPR027308; FAM21.
InterPro; IPR029341; FAM21/CAPZIP.
PANTHER; PTHR21669:SF24; PTHR21669:SF24; 1.
Pfam; PF15255; CAP-ZIP_m; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Endosome;
Lipid-binding; Membrane; Phosphoprotein; Protein transport;
Reference proteome; Transport.
CHAIN 1 1341 WASH complex subunit 2A.
/FTId=PRO_0000317299.
REGION 1 220 Sufficient for interaction with WASHC3,
WASHC4 and WASHC5; required for
interaction with WASHC1.
{ECO:0000250|UniProtKB:Q9Y4E1}.
REGION 356 600 Sufficient for interaction with CCDC93.
{ECO:0000250|UniProtKB:Q9Y4E1}.
REGION 357 1341 Interaction with VPS35.
{ECO:0000250|UniProtKB:Q9Y4E1}.
REGION 937 1341 Interaction with phospholipids.
{ECO:0000250|UniProtKB:Q9Y4E1}.
REGION 1029 1047 Required for interaction with F-actin-
capping protein subunit alpha (CAPZA1 or
CAPZA2 or CAPZA3).
{ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 367 378 LFa 1. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 411 419 LFa 2. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 450 463 LFa 3. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 482 491 LFa 4. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 537 548 LFa 5. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 572 583 LFa 6. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 617 629 LFa 7. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 664 674 LFa 8. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 690 702 LFa 9. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 726 738 LFa 10. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 803 817 LFa 11. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 839 847 LFa 12. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 856 862 LFa 13. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 878 888 LFa 14. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1129 1136 LFa 15. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1171 1185 LFa 16. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1201 1209 LFa 17. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1234 1240 LFa 18. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1262 1270 LFa 19. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1290 1299 LFa 20. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1330 1338 LFa 21. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOD_RES 539 539 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1054 1054 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1087 1087 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1114 1114 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 938 958 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030948.
CONFLICT 342 342 A -> T (in Ref. 1; CAI17187).
{ECO:0000305}.
CONFLICT 444 444 G -> E (in Ref. 2; AAH75815).
{ECO:0000305}.
CONFLICT 569 569 L -> S (in Ref. 1; CAI17187).
{ECO:0000305}.
CONFLICT 698 698 G -> R (in Ref. 1; CAI17187).
{ECO:0000305}.
CONFLICT 816 816 I -> T (in Ref. 2; AAH75815).
{ECO:0000305}.
CONFLICT 997 997 H -> Y (in Ref. 2; AAH82258).
{ECO:0000305}.
CONFLICT 1198 1198 P -> T (in Ref. 1; CAI17187).
{ECO:0000305}.
SEQUENCE 1341 AA; 147184 MW; 8F0F755EB1493EA7 CRC64;
MMNRTTPDQE LAPASEPVWE RPWSVEEIRR SSQSWSLAAD AGLLQFLQEF SQQTISRTHE
IKKQVDGLIR ETKATDCRLH NVFNDFLMLS NTQFIENRVY DEEVEEPVLK AEAEKTEQEK
TREQKEVDLI PKVQEAVNYG LQVLDSAFEQ LDIKAGNSDS EEDDANGRVE LILEPKDLYI
DRPLPYLIGS KLFMEQEDVG LGELSSEEGS VGSDRGSIVD TEEEKEEEES DEDFAHHSDN
EQNRHTTQMS DEEEDDDGCD LFADSEKEEE DIEDIEENTR PKRSRPTSFA DELAARIKGD
AVGRVDEEPT TLPSGEAKPR KTLKEKKERR TPSDDEEDNL FAPPKLTDED FSPFGSGGGL
FSGGKGLFDD EDEESDLFTE APQDRQAGAS VKEESSSSKP GKKIPAGAVS VFLGDTDVFG
AASVPSMKEP QKPEQPTPRK SPYGPPPTGL FDDDDGDDDD DFFSAPHSKP SKTGKVQSTA
DIFGDEEGDL FKEKAVASPE ATVSQTDENK ARAEKKVTLS SSKNLKPSSE TKTQKGLFSD
EEDSEDLFSS QSASKLKGAS LLPGKLPTLV SLFDDEDEED NLFGGTAAKK QTLCLQAQRE
EKAKASELSK KKASALLFSS DEEDQWNIPA SQTHLASDSR SKGEPRDSGT LQSQEAKAVK
KTSLFEEDEE DDLFAIAKDS QKKTQRVSLL FEDDVDSGGS LFGSPPTSVP PATKKKETVS
EAPPLLFSDE EEKEAQLGVK SVDKKVESAK ESLKFGRTDV AESEKEGLLT RSAQETVKHS
DLFSSSSPWD KGTKPRTKTV LSLFDEEEDK MEDQNIIQAP QKEVGKGRDP DAHPKSTGVF
QDEELLFSHK LQKDNDPDVD LFAGTKKTKL LEPSVGSLFG DDEDDDLFSS AKSQPLVQEK
KRVVKKDHSV DSFKNQKHPE SIQGSKEKGI WKPETPQDSS GLAPFKTKEP STRIGKIQAN
LAINPAALLP TAASQISEVK PVLPELAFPS SEHRRSHGLE SVPVLPGSGE AGVSFDLPAQ
ADTLHSANKS RVKMRGKRRP QTRAARRLAA QESSETEDMS VPRGPIAQWA DGAISPNGHR
PQLRAASGED STEEALAAAA APWEGGPVPG VDRSPFAKSL GHSRGEADLF DSGDIFSTGT
GSQSVERTKP KAKIAENPAN PPVGGKAKSP MFPALGEASS DDDLFQSAKP KPAKKTNPFP
LLEDEDDLFT DQKVKKNETK SNSQQDVILT TQDIFEDDIF ATEAIKPSQK TREKEKTLES
NLFDDNIDIF ADLTVKPKEK SKKKVEAKSI FDDDMDDIFS SGIQAKTTKP KSRSAQAAPE
PRFEHKVSNI FDDPLNAFGG Q


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EIAAB33310 Complex III subunit 7,Complex III subunit VII,Cytochrome b-c1 complex subunit 7,Homo sapiens,Human,QP-C,Ubiquinol-cytochrome c reductase complex 14 kDa protein,UQBP,UQCRB
EIAAB14062 FAM21D,Homo sapiens,Human,Putative WASH complex subunit FAM21
CSB-EL008178HU Human Putative WASH complex subunit FAM21(FAM21D) ELISA kit SpeciesHuman 96T


 

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