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WD repeat-containing protein 48 (USP1-associated factor 1) (WD repeat endosomal protein) (p80)

 WDR48_HUMAN             Reviewed;         677 AA.
Q8TAF3; B4DM86; B4DQI2; B4DY84; Q63HJ2; Q658Y1; Q8N3Z1; Q9NSK8;
Q9P279;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
12-SEP-2018, entry version 155.
RecName: Full=WD repeat-containing protein 48;
AltName: Full=USP1-associated factor 1;
AltName: Full=WD repeat endosomal protein;
AltName: Full=p80 {ECO:0000303|PubMed:12196293};
Name=WDR48; Synonyms=KIAA1449, UAF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND INTERACTION WITH HERPESVIRUS SAIMIRI TIP
(MICROBIAL INFECTION).
PubMed=12196293; DOI=10.1016/S1074-7613(02)00368-0;
Park J., Lee B.-S., Choi J.-K., Means R.E., Choe J., Jung J.U.;
"Herpesviral protein targets a cellular WD repeat endosomal protein to
downregulate T lymphocyte receptor expression.";
Immunity 17:221-233(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:143-150(2000).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
TISSUE=Brain, Teratocarcinoma, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 3-677 (ISOFORM 1).
TISSUE=Melanoma, Retina, and Stomach;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Eye;
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 HERPESVIRUS SAIMIRI TIP (MICROBIAL INFECTION).
PubMed=12885920; DOI=10.1128/JVI.77.16.9041-9051.2003;
Park J., Cho N.-H., Choi J.-K., Feng P., Choe J., Jung J.U.;
"Distinct roles of cellular Lck and p80 proteins in herpesvirus
saimiri Tip function on lipid rafts.";
J. Virol. 77:9041-9051(2003).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
AND INTERACTION WITH USP1.
PubMed=18082604; DOI=10.1016/j.molcel.2007.09.031;
Cohn M.A., Kowal P., Yang K., Haas W., Huang T.T., Gygi S.P.,
D'Andrea A.D.;
"A UAF1-containing multisubunit protein complex regulates the Fanconi
anemia pathway.";
Mol. Cell 28:786-797(2007).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HPV11 E1
(MICROBIAL INFECTION).
PubMed=18032488; DOI=10.1128/JVI.01405-07;
Cote-Martin A., Moody C., Fradet-Turcotte A., D'Abramo C.M.,
Lehoux M., Joubert S., Poirier G.G., Coulombe B., Laimins L.A.,
Archambault J.;
"Human papillomavirus E1 helicase interacts with the WD repeat protein
p80 to promote maintenance of the viral genome in keratinocytes.";
J. Virol. 82:1271-1283(2008).
[10]
FUNCTION, AND INTERACTION WITH USP12 AND USP46.
PubMed=19075014; DOI=10.1074/jbc.M808430200;
Cohn M.A., Kee Y., Haas W., Gygi S.P., D'Andrea A.D.;
"UAF1 is a subunit of multiple deubiquitinating enzyme complexes.";
J. Biol. Chem. 284:5343-5351(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-214, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[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]
FUNCTION, MUTAGENESIS OF LEU-580, AND INTERACTION WITH PHLPP1.
PubMed=24145035; DOI=10.1074/jbc.M113.503383;
Gangula N.R., Maddika S.;
"WD repeat protein WDR48 in complex with deubiquitinase USP12
suppresses Akt-dependent cell survival signaling by stabilizing PH
domain leucine-rich repeat protein phosphatase 1 (PHLPP1).";
J. Biol. Chem. 288:34545-34554(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-613, AND 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).
[15] {ECO:0000244|PDB:5CVL, ECO:0000244|PDB:5CVN, ECO:0000244|PDB:5CVO}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-580 IN COMPLEX WITH USP46
AND UBIQUITIN, INTERACTION WITH USP46 AND USP1, FUNCTION, AND
MUTAGENESIS OF SER-170; LYS-214; TRP-256 AND ARG-272.
PubMed=26388029; DOI=10.1016/j.str.2015.08.010;
Yin J., Schoeffler A.J., Wickliffe K., Newton K., Starovasnik M.A.,
Dueber E.C., Harris S.F.;
"Structural insights into WD-repeat 48 activation of ubiquitin-
specific protease 46.";
Structure 23:2043-2054(2015).
[16] {ECO:0000244|PDB:5L8E, ECO:0000244|PDB:5L8W}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 9-580, X-RAY CRYSTALLOGRAPHY
(2.79 ANGSTROMS) OF 9-580 IN COMPLEX WITH USP12 AND UBIQUITIN,
INTERACTION WITH USP12, FUNCTION, AND MUTAGENESIS OF LYS-214; TRP-256
AND ARG-272.
PubMed=27650958; DOI=10.1016/j.jsb.2016.09.011;
Dharadhar S., Clerici M., van Dijk W.J., Fish A., Sixma T.K.;
"A conserved two-step binding for the UAF1 regulator to the USP12
deubiquitinating enzyme.";
J. Struct. Biol. 196:437-447(2016).
[17] {ECO:0000244|PDB:5K1A, ECO:0000244|PDB:5K1B, ECO:0000244|PDB:5K1C}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH USP12 AND
WDR20, INTERACTION WITH USP12, FUNCTION, AND MUTAGENESIS OF TRP-77;
TYR-119; TYR-172 AND TRP-256.
PubMed=27373336; DOI=10.1016/j.molcel.2016.05.031;
Li H., Lim K.S., Kim H., Hinds T.R., Jo U., Mao H., Weller C.E.,
Sun J., Chatterjee C., D'Andrea A.D., Zheng N.;
"Allosteric activation of ubiquitin-specific proteases by beta-
propeller proteins UAF1 and WDR20.";
Mol. Cell 63:249-260(2016).
[18]
VARIANT GLU-628 DEL.
PubMed=24482476; DOI=10.1126/science.1247363;
Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L.,
Masri A., Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A.,
Kara M., Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F.,
Mahmoud I.G., Bouslam N., Bouhouche A., Benomar A., Hanein S.,
Raymond L., Forlani S., Mascaro M., Selim L., Shehata N.,
Al-Allawi N., Bindu P.S., Azam M., Gunel M., Caglayan A., Bilguvar K.,
Tolun A., Issa M.Y., Schroth J., Spencer E.G., Rosti R.O., Akizu N.,
Vaux K.K., Johansen A., Koh A.A., Megahed H., Durr A., Brice A.,
Stevanin G., Gabriel S.B., Ideker T., Gleeson J.G.;
"Exome sequencing links corticospinal motor neuron disease to common
neurodegenerative disorders.";
Science 343:506-511(2014).
-!- FUNCTION: Regulator of deubiquitinating complexes. Acts as a
strong activator of USP1 and USP46 (PubMed:18082604,
PubMed:19075014, PubMed:26388029). Enhances the USP1-mediated
deubiquitination of FANCD2; USP1 being almost inactive by itself
(PubMed:18082604). Also activates deubiquitinating activity of
complexes containing USP12 (PubMed:19075014, PubMed:27650958,
PubMed:27373336). Docks at the distal end of the USP12 fingers
domain and induces a cascade of structural changes leading to the
activation of the enzyme (PubMed:27650958, PubMed:27373336).
Activates deubiquitination by increasing the catalytic turnover
without increasing the affinity of deubiquitinating enzymes for
the substrate (PubMed:19075014, PubMed:27373336). In complex with
USP12, acts as a potential tumor suppressor by positively
regulating PHLPP1 stability (PubMed:24145035). In case of
infection by Herpesvirus saimiri, may play a role in vesicular
transport or membrane fusion events necessary for transport to
lysosomes. Induces lysosomal vesicle formation via interaction
with Herpesvirus saimiri tyrosine kinase-interacting protein
(TIP). Subsequently, TIP recruits tyrosine-protein kinase LCK,
resulting in down-regulation of T-cell antigen receptor TCR. May
play a role in generation of enlarged endosomal vesicles via
interaction with TIP (PubMed:12196293). In case of infection by
papillomavirus HPV11, promotes the maintenance of the viral genome
via its interaction with HPV11 helicase E1 (PubMed:18032488).
{ECO:0000269|PubMed:12196293, ECO:0000269|PubMed:18032488,
ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:19075014,
ECO:0000269|PubMed:24145035, ECO:0000269|PubMed:26388029,
ECO:0000269|PubMed:27373336, ECO:0000269|PubMed:27650958}.
-!- SUBUNIT: Interacts with USP46 (PubMed:19075014, PubMed:26388029).
Interacts with USP1 (PubMed:18082604, PubMed:26388029). Interacts
with USP12 (PubMed:19075014, PubMed:27650958, PubMed:27373336).
Component of the USP12/WDR20/WDR48 deubiquitinating complex
(PubMed:27373336). Interacts with PHLPP1 (PubMed:24145035).
{ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:19075014,
ECO:0000269|PubMed:24145035, ECO:0000269|PubMed:26388029,
ECO:0000269|PubMed:27373336, ECO:0000269|PubMed:27650958}.
-!- SUBUNIT: (Microbial infection) Interacts with papillomavirus HPV11
E1 protein. {ECO:0000269|PubMed:18032488}.
-!- SUBUNIT: (Microbial infection) Interacts with Saimiriine
herpesvirus TIP protein. {ECO:0000269|PubMed:12196293,
ECO:0000269|PubMed:12885920}.
-!- INTERACTION:
O94782:USP1; NbExp=2; IntAct=EBI-16178048, EBI-2513396;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18032488}.
Cytoplasm {ECO:0000269|PubMed:12196293,
ECO:0000269|PubMed:18032488}. Lysosome
{ECO:0000269|PubMed:12196293}. Late endosome
{ECO:0000269|PubMed:12196293}. Note=Mainly in cytoplasmic
compartments (PubMed:12196293, PubMed:18032488). In case of
infection by papillomavirus HPV11, translocates to the nucleus via
its interaction with papillomavirus HPV11 (PubMed:18032488).
{ECO:0000269|PubMed:12196293, ECO:0000269|PubMed:18032488}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q8TAF3-1; Sequence=Displayed;
Name=2;
IsoId=Q8TAF3-2; Sequence=VSP_016776, VSP_016777;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8TAF3-3; Sequence=VSP_037625;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q8TAF3-4; Sequence=VSP_037623;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q8TAF3-5; Sequence=VSP_037624, VSP_037626;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12196293}.
-!- DOMAIN: N-terminal WD region interacts with TIP and C-terminal
region mediates lysosomal localization (Probable). The WD repeats
are required for the interaction with deubiquitinating enzymes
USP1, USP12 and USP46. {ECO:0000269|PubMed:26388029, ECO:0000305}.
-!- MISCELLANEOUS: Knockdown of WDR48 increases Akt activation.
{ECO:0000269|PubMed:24145035}.
-!- SIMILARITY: Belongs to the WD repeat WDR48 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH37168.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA95973.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAH56182.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAH56300.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF468833; AAL78650.1; -; mRNA.
EMBL; AB040882; BAA95973.2; ALT_INIT; mRNA.
EMBL; AK297349; BAG59798.1; -; mRNA.
EMBL; AK298810; BAG60944.1; -; mRNA.
EMBL; AK302307; BAG63646.1; -; mRNA.
EMBL; AL162064; CAB82402.1; -; mRNA.
EMBL; AL832926; CAH56300.1; ALT_INIT; mRNA.
EMBL; BX649170; CAH56182.1; ALT_INIT; mRNA.
EMBL; BC026353; AAH26353.1; -; mRNA.
EMBL; BC037168; AAH37168.1; ALT_INIT; mRNA.
CCDS; CCDS33738.1; -. [Q8TAF3-1]
PIR; T47168; T47168.
RefSeq; NP_001290331.1; NM_001303402.1. [Q8TAF3-4]
RefSeq; NP_001290332.1; NM_001303403.1. [Q8TAF3-3]
RefSeq; NP_001333156.1; NM_001346227.1.
RefSeq; NP_001333157.1; NM_001346228.1.
RefSeq; NP_065890.1; NM_020839.3. [Q8TAF3-1]
UniGene; Hs.109778; -.
PDB; 5CVL; X-ray; 3.00 A; A=2-580.
PDB; 5CVN; X-ray; 3.36 A; A=2-580.
PDB; 5CVO; X-ray; 3.88 A; A/D=1-677.
PDB; 5K1A; X-ray; 2.30 A; B/D/F/H=1-677.
PDB; 5K1B; X-ray; 3.30 A; B=1-677.
PDB; 5K1C; X-ray; 3.00 A; B=1-563.
PDB; 5L8E; X-ray; 2.30 A; A/B=9-580.
PDB; 5L8W; X-ray; 2.79 A; B=9-580.
PDBsum; 5CVL; -.
PDBsum; 5CVN; -.
PDBsum; 5CVO; -.
PDBsum; 5K1A; -.
PDBsum; 5K1B; -.
PDBsum; 5K1C; -.
PDBsum; 5L8E; -.
PDBsum; 5L8W; -.
ProteinModelPortal; Q8TAF3; -.
SMR; Q8TAF3; -.
BioGrid; 121649; 83.
CORUM; Q8TAF3; -.
DIP; DIP-50841N; -.
IntAct; Q8TAF3; 67.
MINT; Q8TAF3; -.
STRING; 9606.ENSP00000307491; -.
ChEMBL; CHEMBL3430885; -.
iPTMnet; Q8TAF3; -.
PhosphoSitePlus; Q8TAF3; -.
BioMuta; WDR48; -.
DMDM; 74760390; -.
EPD; Q8TAF3; -.
MaxQB; Q8TAF3; -.
PaxDb; Q8TAF3; -.
PeptideAtlas; Q8TAF3; -.
PRIDE; Q8TAF3; -.
ProteomicsDB; 73870; -.
ProteomicsDB; 73871; -. [Q8TAF3-2]
ProteomicsDB; 73872; -. [Q8TAF3-3]
ProteomicsDB; 73873; -. [Q8TAF3-4]
ProteomicsDB; 73874; -. [Q8TAF3-5]
Ensembl; ENST00000302313; ENSP00000307491; ENSG00000114742. [Q8TAF3-1]
GeneID; 57599; -.
KEGG; hsa:57599; -.
UCSC; uc003cit.4; human. [Q8TAF3-1]
CTD; 57599; -.
DisGeNET; 57599; -.
EuPathDB; HostDB:ENSG00000114742.13; -.
GeneCards; WDR48; -.
HGNC; HGNC:30914; WDR48.
HPA; HPA038421; -.
HPA; HPA058015; -.
MalaCards; WDR48; -.
MIM; 612167; gene.
neXtProt; NX_Q8TAF3; -.
OpenTargets; ENSG00000114742; -.
Orphanet; 401800; Autosomal recessive spastic paraplegia type 60.
PharmGKB; PA134956949; -.
eggNOG; KOG0308; Eukaryota.
eggNOG; ENOG410XRJ5; LUCA.
GeneTree; ENSGT00920000149157; -.
HOVERGEN; HBG079413; -.
InParanoid; Q8TAF3; -.
KO; K15361; -.
OMA; YVPNWFN; -.
OrthoDB; EOG091G03SS; -.
PhylomeDB; Q8TAF3; -.
TreeFam; TF315205; -.
Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
SignaLink; Q8TAF3; -.
ChiTaRS; WDR48; human.
GenomeRNAi; 57599; -.
PRO; PR:Q8TAF3; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114742; Expressed in 227 organ(s), highest expression level in corpus callosum.
CleanEx; HS_WDR48; -.
ExpressionAtlas; Q8TAF3; baseline and differential.
Genevisible; Q8TAF3; HS.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; TAS:Reactome.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:1902525; P:regulation of protein monoubiquitination; IEA:Ensembl.
GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
GO; GO:0007338; P:single fertilization; IEA:Ensembl.
GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
GO; GO:0043588; P:skin development; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR021772; DUF3337.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF11816; DUF3337; 1.
Pfam; PF00400; WD40; 4.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 2.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Endosome; Host-virus interaction; Lysosome; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Ubl conjugation pathway; WD repeat.
CHAIN 1 677 WD repeat-containing protein 48.
/FTId=PRO_0000051399.
REPEAT 28 67 WD 1.
REPEAT 73 112 WD 2.
REPEAT 115 154 WD 3.
REPEAT 166 205 WD 4.
REPEAT 208 247 WD 5.
REPEAT 250 289 WD 6.
REPEAT 292 334 WD 7.
REPEAT 358 397 WD 8.
MOD_RES 28 28 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8BH57}.
MOD_RES 214 214 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 578 578 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BH57}.
MOD_RES 613 613 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 558 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_016776.
VAR_SEQ 1 90 MAAHHRQNTAGRRKVQVSYVIRDEVEKYNRNGVNALQLDPA
LNRLFTAGRDSIIRIWSVNQHKQDPYIASMEHHTDWVNDIV
LCCNGKTL -> MECQSAQV (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037623.
VAR_SEQ 16 223 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037624.
VAR_SEQ 91 99 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037625.
VAR_SEQ 325 391 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037626.
VAR_SEQ 645 645 D -> DQV (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_016777.
VARIANT 628 628 Missing (found in a patient with spastic
paraplegia; unknown pathological
significance).
{ECO:0000269|PubMed:24482476}.
/FTId=VAR_077846.
MUTAGEN 77 77 W->A: Impaired binding to USP12; when
associated with Ala-256.
{ECO:0000269|PubMed:27373336}.
MUTAGEN 119 119 Y->A: Impaired binding to USP12; when
associated with Ala-172.
{ECO:0000269|PubMed:27373336}.
MUTAGEN 170 170 S->Y: Strongly reduces interaction with
USP46 and abolishes stimulation of USP46
enzyme activity.
{ECO:0000269|PubMed:26388029}.
MUTAGEN 172 172 Y->A: Impaired binding to USP12; when
associated with Ala-119.
{ECO:0000269|PubMed:27373336}.
MUTAGEN 214 214 K->E: Strongly reduces interaction with
USP12 or USP46 and abolishes stimulation
of their enzyme activity; when associated
with A-256 and D-272.
{ECO:0000269|PubMed:26388029,
ECO:0000269|PubMed:27650958}.
MUTAGEN 256 256 W->A: Strongly reduces interaction with
USP12 or USP46 and abolishes stimulation
of their enzyme activity; when associated
with E-214 and D-272. Impaired binding to
USP12; when associated with Ala-77.
{ECO:0000269|PubMed:26388029,
ECO:0000269|PubMed:27373336,
ECO:0000269|PubMed:27650958}.
MUTAGEN 272 272 R->D: Strongly reduces interaction with
USP12 or USP46 and abolishes stimulation
of their enzyme activity; when associated
with E-214 and A-256.
{ECO:0000269|PubMed:26388029,
ECO:0000269|PubMed:27650958}.
MUTAGEN 580 580 L->F: Impaired binding to PHLPP1.
Defective in stabilizing PHLPP1.
{ECO:0000269|PubMed:24145035}.
CONFLICT 161 161 T -> A (in Ref. 6; AAH37168).
{ECO:0000305}.
CONFLICT 286 286 I -> V (in Ref. 4; BAG63646).
{ECO:0000305}.
CONFLICT 319 319 S -> F (in Ref. 4; BAG63646).
{ECO:0000305}.
CONFLICT 328 328 G -> E (in Ref. 4; BAG63646).
{ECO:0000305}.
CONFLICT 585 585 L -> P (in Ref. 4; BAG63646).
{ECO:0000305}.
STRAND 15 21 {ECO:0000244|PDB:5K1A}.
STRAND 28 31 {ECO:0000244|PDB:5CVL}.
STRAND 33 39 {ECO:0000244|PDB:5K1A}.
TURN 40 43 {ECO:0000244|PDB:5K1A}.
STRAND 44 49 {ECO:0000244|PDB:5K1A}.
STRAND 54 58 {ECO:0000244|PDB:5K1A}.
STRAND 67 71 {ECO:0000244|PDB:5K1A}.
STRAND 78 84 {ECO:0000244|PDB:5K1A}.
TURN 85 88 {ECO:0000244|PDB:5K1A}.
STRAND 89 94 {ECO:0000244|PDB:5K1A}.
STRAND 99 103 {ECO:0000244|PDB:5K1A}.
TURN 104 107 {ECO:0000244|PDB:5K1A}.
STRAND 108 113 {ECO:0000244|PDB:5K1A}.
STRAND 120 126 {ECO:0000244|PDB:5K1A}.
HELIX 127 129 {ECO:0000244|PDB:5K1A}.
STRAND 131 136 {ECO:0000244|PDB:5K1A}.
STRAND 141 145 {ECO:0000244|PDB:5K1A}.
HELIX 146 150 {ECO:0000244|PDB:5K1A}.
STRAND 154 156 {ECO:0000244|PDB:5K1A}.
STRAND 158 161 {ECO:0000244|PDB:5K1A}.
STRAND 162 164 {ECO:0000244|PDB:5L8E}.
STRAND 171 176 {ECO:0000244|PDB:5K1A}.
STRAND 183 187 {ECO:0000244|PDB:5K1A}.
STRAND 191 195 {ECO:0000244|PDB:5K1A}.
TURN 197 199 {ECO:0000244|PDB:5K1A}.
STRAND 202 206 {ECO:0000244|PDB:5K1A}.
STRAND 213 218 {ECO:0000244|PDB:5K1A}.
STRAND 222 229 {ECO:0000244|PDB:5K1A}.
STRAND 234 238 {ECO:0000244|PDB:5K1A}.
TURN 239 242 {ECO:0000244|PDB:5K1A}.
STRAND 243 248 {ECO:0000244|PDB:5K1A}.
STRAND 255 260 {ECO:0000244|PDB:5K1A}.
STRAND 266 271 {ECO:0000244|PDB:5K1A}.
STRAND 275 282 {ECO:0000244|PDB:5K1A}.
STRAND 287 292 {ECO:0000244|PDB:5K1A}.
STRAND 297 302 {ECO:0000244|PDB:5K1A}.
STRAND 305 308 {ECO:0000244|PDB:5K1A}.
STRAND 310 319 {ECO:0000244|PDB:5K1A}.
STRAND 321 325 {ECO:0000244|PDB:5K1A}.
HELIX 329 334 {ECO:0000244|PDB:5CVL}.
STRAND 354 357 {ECO:0000244|PDB:5K1A}.
STRAND 363 368 {ECO:0000244|PDB:5K1A}.
STRAND 372 379 {ECO:0000244|PDB:5K1A}.
STRAND 384 388 {ECO:0000244|PDB:5K1A}.
TURN 389 392 {ECO:0000244|PDB:5K1A}.
STRAND 393 400 {ECO:0000244|PDB:5K1A}.
HELIX 403 409 {ECO:0000244|PDB:5K1A}.
STRAND 421 423 {ECO:0000244|PDB:5K1A}.
STRAND 427 433 {ECO:0000244|PDB:5K1A}.
TURN 435 439 {ECO:0000244|PDB:5K1A}.
STRAND 442 444 {ECO:0000244|PDB:5K1A}.
TURN 445 449 {ECO:0000244|PDB:5K1A}.
STRAND 453 455 {ECO:0000244|PDB:5L8E}.
STRAND 459 461 {ECO:0000244|PDB:5K1A}.
HELIX 462 470 {ECO:0000244|PDB:5K1A}.
TURN 471 473 {ECO:0000244|PDB:5K1A}.
HELIX 475 477 {ECO:0000244|PDB:5K1A}.
STRAND 514 522 {ECO:0000244|PDB:5K1A}.
STRAND 524 529 {ECO:0000244|PDB:5K1A}.
HELIX 530 534 {ECO:0000244|PDB:5K1A}.
HELIX 536 545 {ECO:0000244|PDB:5K1A}.
HELIX 548 554 {ECO:0000244|PDB:5K1A}.
STRAND 564 571 {ECO:0000244|PDB:5K1A}.
STRAND 583 588 {ECO:0000244|PDB:5K1A}.
HELIX 593 603 {ECO:0000244|PDB:5K1A}.
HELIX 631 638 {ECO:0000244|PDB:5K1A}.
STRAND 639 643 {ECO:0000244|PDB:5K1A}.
HELIX 654 660 {ECO:0000244|PDB:5K1A}.
STRAND 664 674 {ECO:0000244|PDB:5K1A}.
SEQUENCE 677 AA; 76210 MW; 20FDA620E02696E0 CRC64;
MAAHHRQNTA GRRKVQVSYV IRDEVEKYNR NGVNALQLDP ALNRLFTAGR DSIIRIWSVN
QHKQDPYIAS MEHHTDWVND IVLCCNGKTL ISASSDTTVK VWNAHKGFCM STLRTHKDYV
KALAYAKDKE LVASAGLDRQ IFLWDVNTLT ALTASNNTVT TSSLSGNKDS IYSLAMNQLG
TIIVSGSTEK VLRVWDPRTC AKLMKLKGHT DNVKALLLNR DGTQCLSGSS DGTIRLWSLG
QQRCIATYRV HDEGVWALQV NDAFTHVYSG GRDRKIYCTD LRNPDIRVLI CEEKAPVLKM
ELDRSADPPP AIWVATTKST VNKWTLKGIH NFRASGDYDN DCTNPITPLC TQPDQVIKGG
ASIIQCHILN DKRHILTKDT NNNVAYWDVL KACKVEDLGK VDFEDEIKKR FKMVYVPNWF
SVDLKTGMLT ITLDESDCFA AWVSAKDAGF SSPDGSDPKL NLGGLLLQAL LEYWPRTHVN
PMDEEENEVN HVNGEQENRV QKGNGYFQVP PHTPVIFGEA GGRTLFRLLC RDSGGETESM
LLNETVPQWV IDITVDKNMP KFNKIPFYLQ PHASSGAKTL KKDRLSASDM LQVRKVMEHV
YEKIINLDNE SQTTSSSNNE KPGEQEKEED IAVLAEEKIE LLCQDQVLDP NMDLRTVKHF
IWKSGGDLTL HYRQKST


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