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Ubiquitin recognition factor in ER-associated degradation protein 1 (Ubiquitin fusion degradation protein 1) (UB fusion protein 1)

 UFD1_HUMAN              Reviewed;         307 AA.
Q92890; A8MW31; Q9Y5N0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 3.
25-OCT-2017, entry version 151.
RecName: Full=Ubiquitin recognition factor in ER-associated degradation protein 1 {ECO:0000312|HGNC:HGNC:12520};
AltName: Full=Ubiquitin fusion degradation protein 1;
Short=UB fusion protein 1;
Name=UFD1 {ECO:0000312|HGNC:HGNC:12520}; Synonyms=UFD1L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND VARIANT
ALA-130.
TISSUE=Brain;
PubMed=9063746; DOI=10.1093/hmg/6.2.259;
Pizzuti A., Novelli G., Ratti A., Amati F., Mari A., Calabrese G.,
Nicolis S., Silani V., Marino B., Scarlato G., Ottolenghi S.,
Dallapiccola B.;
"UFD1L, a developmentally expressed ubiquitination gene, is deleted in
CATCH 22 syndrome.";
Hum. Mol. Genet. 6:259-265(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
TISSUE=Heart;
Gong L., Yeh E.T.H.;
"Characterization of human UFD1, a ubiquitin fusion-degradation
protein.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
TISSUE=Brain, and Skin;
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).
[7]
INTERACTION WITH NPLOC4.
PubMed=11574150; DOI=10.1016/S0378-1119(01)00649-7;
Botta A., Tandoi C., Fini G., Calabrese G., Dallapiccola B.,
Novelli G.;
"Cloning and characterization of the gene encoding human NPL4, a
protein interacting with the ubiquitin fusion-degradation protein
(UFD1L).";
Gene 275:39-46(2001).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, 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).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-245; SER-247
AND SER-299, 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).
[12]
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).
[13]
INTERACTION WITH USP13.
PubMed=21571647; DOI=10.1073/pnas.1100028108;
Chen M., Gutierrez G.J., Ronai Z.A.;
"Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum
(ER) stress response to cell cycle control.";
Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-231; SER-245;
SER-247 AND SER-299, 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).
[16]
FUNCTION, AND INTERACTION WITH NPLOC4 AND VCP.
PubMed=26471729; DOI=10.15252/embj.201591888;
Hao Q., Jiao S., Shi Z., Li C., Meng X., Zhang Z., Wang Y., Song X.,
Wang W., Zhang R., Zhao Y., Wong C.C., Zhou Z.;
"A non-canonical role of the p97 complex in RIG-I antiviral
signaling.";
EMBO J. 34:2903-2920(2015).
[17]
STRUCTURE BY NMR OF 11-193.
RIKEN structural genomics initiative (RSGI);
"Solution structure of human ubiquitin fusion degradation protein 1
homolog UFD1.";
Submitted (APR-2008) to the PDB data bank.
-!- FUNCTION: Essential component of the ubiquitin-dependent
proteolytic pathway which degrades ubiquitin fusion proteins. The
ternary complex containing UFD1, VCP and NPLOC4 binds
ubiquitinated proteins and is necessary for the export of
misfolded proteins from the ER to the cytoplasm, where they are
degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates
spindle disassembly at the end of mitosis and is necessary for the
formation of a closed nuclear envelope. It may be involved in the
development of some ectoderm-derived structures (By similarity).
Acts as a negative regulator of type I interferon production via
the complex formed with VCP and NPLOC4, which binds to DDX58/RIG-I
and recruits RNF125 to promote ubiquitination and degradation of
DDX58/RIG-I (PubMed:26471729). {ECO:0000250|UniProtKB:Q9ES53,
ECO:0000269|PubMed:26471729}.
-!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent
pathway. {ECO:0000250|UniProtKB:Q9ES53}.
-!- SUBUNIT: Heterodimer with NPLOC4, this heterodimer binds VCP and
inhibits Golgi membrane fusion (PubMed:11574150, PubMed:26471729).
Interacts with USP13 (PubMed:21571647).
{ECO:0000269|PubMed:11574150, ECO:0000269|PubMed:21571647,
ECO:0000269|PubMed:26471729}.
-!- INTERACTION:
Q8TAT6:NPLOC4; NbExp=5; IntAct=EBI-1994090, EBI-1994109;
P55072:VCP; NbExp=5; IntAct=EBI-1994090, EBI-355164;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ES53}.
Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9ES53}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Short;
IsoId=Q92890-2; Sequence=Displayed;
Note=Major isoform.;
Name=Long;
IsoId=Q92890-1; Sequence=VSP_006707;
Name=3;
IsoId=Q92890-3; Sequence=VSP_045044;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Found in adult heart, skeletal muscle and
pancreas, and in fetal liver and kidney.
-!- SIMILARITY: Belongs to the UFD1 family. {ECO:0000305}.
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EMBL; U64444; AAD08720.1; -; mRNA.
EMBL; AF141201; AAD28788.1; -; mRNA.
EMBL; CR456607; CAG30493.1; -; mRNA.
EMBL; AK225877; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC000068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC000087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001049; AAH01049.1; -; mRNA.
EMBL; BC005087; AAH05087.1; -; mRNA.
CCDS; CCDS13761.1; -. [Q92890-2]
CCDS; CCDS33600.2; -. [Q92890-3]
RefSeq; NP_001030324.2; NM_001035247.2. [Q92890-3]
RefSeq; NP_005650.2; NM_005659.6. [Q92890-2]
UniGene; Hs.474213; -.
PDB; 2YUJ; NMR; -; A=11-193.
PDB; 5B6C; X-ray; 1.55 A; B=225-235.
PDB; 5C1B; X-ray; 3.08 A; U/V=221-241.
PDBsum; 2YUJ; -.
PDBsum; 5B6C; -.
PDBsum; 5C1B; -.
ProteinModelPortal; Q92890; -.
SMR; Q92890; -.
BioGrid; 113200; 103.
CORUM; Q92890; -.
DIP; DIP-45954N; -.
IntAct; Q92890; 32.
MINT; MINT-2837704; -.
STRING; 9606.ENSP00000263202; -.
iPTMnet; Q92890; -.
PhosphoSitePlus; Q92890; -.
BioMuta; UFD1L; -.
DMDM; 160332310; -.
OGP; Q92890; -.
EPD; Q92890; -.
PaxDb; Q92890; -.
PeptideAtlas; Q92890; -.
PRIDE; Q92890; -.
DNASU; 7353; -.
Ensembl; ENST00000263202; ENSP00000263202; ENSG00000070010. [Q92890-2]
Ensembl; ENST00000399523; ENSP00000382439; ENSG00000070010. [Q92890-3]
GeneID; 7353; -.
KEGG; hsa:7353; -.
UCSC; uc002zpm.3; human. [Q92890-2]
CTD; 7353; -.
DisGeNET; 7353; -.
EuPathDB; HostDB:ENSG00000070010.18; -.
GeneCards; UFD1; -.
HGNC; HGNC:12520; UFD1.
HPA; HPA030287; -.
HPA; HPA030288; -.
HPA; HPA073425; -.
MalaCards; UFD1; -.
MIM; 601754; gene.
neXtProt; NX_Q92890; -.
OpenTargets; ENSG00000070010; -.
Orphanet; 567; 22q11.2 deletion syndrome.
PharmGKB; PA37167; -.
eggNOG; KOG1816; Eukaryota.
eggNOG; COG5140; LUCA.
GeneTree; ENSGT00390000002408; -.
HOGENOM; HOG000212737; -.
HOVERGEN; HBG001266; -.
InParanoid; Q92890; -.
KO; K14016; -.
OMA; KDHSETQ; -.
OrthoDB; EOG091G0KO7; -.
PhylomeDB; Q92890; -.
TreeFam; TF314581; -.
Reactome; R-HSA-110320; Translesion Synthesis by POLH.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
SIGNOR; Q92890; -.
UniPathway; UPA00144; -.
ChiTaRS; UFD1L; human.
EvolutionaryTrace; Q92890; -.
GeneWiki; UFD1L; -.
GenomeRNAi; 7353; -.
PRO; PR:Q92890; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000070010; -.
CleanEx; HS_UFD1L; -.
ExpressionAtlas; Q92890; baseline and differential.
Genevisible; Q92890; HS.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0036501; C:UFD1-NPL4 complex; IPI:ParkinsonsUK-UCL.
GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; TAS:ProtInc.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IMP:UniProtKB.
GO; GO:0032480; P:negative regulation of type I interferon production; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
InterPro; IPR004854; Ufd1-like.
PANTHER; PTHR12555; PTHR12555; 1.
Pfam; PF03152; UFD1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Ubl conjugation pathway.
CHAIN 1 307 Ubiquitin recognition factor in ER-
associated degradation protein 1.
/FTId=PRO_0000194984.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 106 106 E -> EDGLVQLETVNLQVATYSKSKFCYLPHWMMQNLLLE
E (in isoform Long).
{ECO:0000303|PubMed:9063746}.
/FTId=VSP_006707.
VAR_SEQ 267 307 Missing (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_045044.
VARIANT 130 130 P -> A (in dbSNP:rs17744624).
{ECO:0000269|PubMed:9063746}.
/FTId=VAR_052436.
CONFLICT 25 25 C -> R (in Ref. 4; AK225877).
{ECO:0000305}.
CONFLICT 33 33 G -> W (in Ref. 1; AAD08720).
{ECO:0000305}.
CONFLICT 183 183 I -> H (in Ref. 1; AAD08720).
{ECO:0000305}.
STRAND 16 18 {ECO:0000244|PDB:2YUJ}.
STRAND 20 26 {ECO:0000244|PDB:2YUJ}.
STRAND 31 35 {ECO:0000244|PDB:2YUJ}.
TURN 39 44 {ECO:0000244|PDB:2YUJ}.
STRAND 45 47 {ECO:0000244|PDB:2YUJ}.
HELIX 50 58 {ECO:0000244|PDB:2YUJ}.
STRAND 66 71 {ECO:0000244|PDB:2YUJ}.
TURN 72 75 {ECO:0000244|PDB:2YUJ}.
STRAND 76 84 {ECO:0000244|PDB:2YUJ}.
STRAND 91 93 {ECO:0000244|PDB:2YUJ}.
HELIX 97 102 {ECO:0000244|PDB:2YUJ}.
STRAND 108 115 {ECO:0000244|PDB:2YUJ}.
STRAND 121 129 {ECO:0000244|PDB:2YUJ}.
HELIX 130 134 {ECO:0000244|PDB:2YUJ}.
HELIX 138 146 {ECO:0000244|PDB:2YUJ}.
STRAND 157 164 {ECO:0000244|PDB:2YUJ}.
STRAND 166 181 {ECO:0000244|PDB:2YUJ}.
STRAND 188 191 {ECO:0000244|PDB:2YUJ}.
SEQUENCE 307 AA; 34500 MW; FC69860002C042C6 CRC64;
MFSFNMFDHP IPRVFQNRFS TQYRCFSVSM LAGPNDRSDV EKGGKIIMPP SALDQLSRLN
ITYPMLFKLT NKNSDRMTHC GVLEFVADEG ICYLPHWMMQ NLLLEEGGLV QVESVNLQVA
TYSKFQPQSP DFLDITNPKA VLENALRNFA CLTTGDVIAI NYNEKIYELR VMETKPDKAV
SIIECDMNVD FDAPLGYKEP ERQVQHEEST EGEADHSGYA GELGFRAFSG SGNRLDGKKK
GVEPSPSPIK PGDIKRGIPN YEFKLGKITF IRNSRPLVKK VEEDEAGGRF VAFSGEGQSL
RKKGRKP


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UFD1_RAT ELISA Kit FOR Ubiquitin fusion degradation protein 1 homolog; organism: Rat; gene name: Ufd1l 96T
CSB-EL025559MO Mouse Ubiquitin fusion degradation protein 1 homolog(UFD1L) ELISA kit SpeciesMouse 96T
pro-1625 Recombinant Human Ubiquitin Fusion Degradation 1 Like 2
pro-1625 Recombinant Human Ubiquitin Fusion Degradation 1 Like 10
pro-1625 Recombinant Human Ubiquitin Fusion Degradation 1 Like 1mg
201-20-6241 UFD1L{ubiquitin fusion degradation 1 like (yeast)}rabbit.pAb 0.2ml
GS-2383a ubiquitin fusion degradation 1 like (yeast) primary antibody, Host: Rabbit 200ul


 

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