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Protein

WD repeat-containing protein 48

Gene

WDR48

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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). Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate. 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. In case of infection by papillomavirus HPV11, promotes the maintenance of the viral genome via its interaction with HPV11 helicase E1.4 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

SignaLinkiQ8TAF3.

Names & Taxonomyi

Protein namesi
Recommended name:
WD repeat-containing protein 48
Alternative name(s):
USP1-associated factor 1
WD repeat endosomal protein
p801 Publication
Gene namesi
Name:WDR48
Synonyms:KIAA1449, UAF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:30914. WDR48.

Subcellular locationi

GO - Cellular componenti

  • late endosome Source: UniProtKB-SubCell
  • lysosome Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Lysosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi170 – 1701S → Y: Strongly reduces interaction with USP46 and abolishes stimulation of USP46 enzyme activity. 1 Publication
Mutagenesisi214 – 2141K → E: Strongly reduces interaction with USP46 and abolishes stimulation of USP46 enzyme activity; when associated with A-256 and D-272. 1 Publication
Mutagenesisi256 – 2561W → A: Strongly reduces interaction with USP46 and abolishes stimulation of USP46 enzyme activity; when associated with E-214 and D-272. 1 Publication
Mutagenesisi272 – 2721R → D: Strongly reduces interaction with USP46 and abolishes stimulation of USP46 enzyme activity; when associated with E-214 and A-256. 1 Publication

Organism-specific databases

MalaCardsiWDR48.
Orphaneti401800. Autosomal recessive spastic paraplegia type 60.
PharmGKBiPA134956949.

Polymorphism and mutation databases

BioMutaiWDR48.
DMDMi74760390.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 677677WD repeat-containing protein 48PRO_0000051399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281PhosphotyrosineBy similarity
Modified residuei214 – 2141N6-acetyllysineCombined sources
Modified residuei578 – 5781N6-acetyllysineBy similarity
Modified residuei613 – 6131PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8TAF3.
MaxQBiQ8TAF3.
PaxDbiQ8TAF3.
PeptideAtlasiQ8TAF3.
PRIDEiQ8TAF3.

PTM databases

iPTMnetiQ8TAF3.
PhosphoSiteiQ8TAF3.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ8TAF3.
CleanExiHS_WDR48.
ExpressionAtlasiQ8TAF3. baseline and differential.
GenevisibleiQ8TAF3. HS.

Organism-specific databases

HPAiHPA038421.

Interactioni

Subunit structurei

Interacts with USP46 (PubMed:26388029, PubMed:19075014). Interacts with USP1 (PubMed:18082604, PubMed:26388029). Interacts with USP12 (PubMed:19075014). Interacts with Saimiriine herpesvirus TIP protein (PubMed:12196293, PubMed:12885920). Interacts with papillomavirus HPV11 E1 protein (PubMed:18032488).6 Publications

Protein-protein interaction databases

BioGridi121649. 76 interactions.
IntActiQ8TAF3. 62 interactions.
MINTiMINT-3043701.
STRINGi9606.ENSP00000307491.

Structurei

Secondary structure

1
677
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 217Combined sources
Beta strandi28 – 314Combined sources
Beta strandi33 – 397Combined sources
Turni40 – 434Combined sources
Beta strandi44 – 496Combined sources
Beta strandi54 – 585Combined sources
Beta strandi67 – 715Combined sources
Beta strandi78 – 847Combined sources
Turni85 – 884Combined sources
Beta strandi89 – 946Combined sources
Beta strandi99 – 1035Combined sources
Turni104 – 1074Combined sources
Beta strandi108 – 1136Combined sources
Beta strandi120 – 1267Combined sources
Turni127 – 1304Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi141 – 1455Combined sources
Helixi146 – 1505Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi171 – 1766Combined sources
Beta strandi183 – 1875Combined sources
Beta strandi190 – 1956Combined sources
Turni197 – 1993Combined sources
Beta strandi202 – 2065Combined sources
Beta strandi213 – 2186Combined sources
Beta strandi222 – 2298Combined sources
Beta strandi232 – 2387Combined sources
Turni239 – 2424Combined sources
Beta strandi243 – 2497Combined sources
Beta strandi255 – 2606Combined sources
Beta strandi266 – 2716Combined sources
Beta strandi275 – 2839Combined sources
Beta strandi287 – 2926Combined sources
Beta strandi297 – 3026Combined sources
Beta strandi305 – 3084Combined sources
Beta strandi311 – 3199Combined sources
Beta strandi321 – 3255Combined sources
Helixi329 – 3346Combined sources
Beta strandi354 – 3574Combined sources
Beta strandi363 – 3686Combined sources
Beta strandi372 – 3798Combined sources
Beta strandi384 – 3885Combined sources
Turni389 – 3924Combined sources
Beta strandi393 – 4008Combined sources
Helixi403 – 4097Combined sources
Beta strandi421 – 4233Combined sources
Beta strandi427 – 4337Combined sources
Turni435 – 4373Combined sources
Beta strandi442 – 4443Combined sources
Turni445 – 4495Combined sources
Beta strandi453 – 4553Combined sources
Beta strandi459 – 4613Combined sources
Helixi462 – 4709Combined sources
Turni471 – 4733Combined sources
Helixi475 – 4773Combined sources
Beta strandi514 – 5229Combined sources
Beta strandi524 – 5296Combined sources
Helixi530 – 5345Combined sources
Helixi536 – 54510Combined sources
Helixi548 – 5547Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5CVLX-ray3.00A2-580[»]
5CVNX-ray3.36A2-580[»]
5CVOX-ray3.88A/D1-677[»]
ProteinModelPortaliQ8TAF3.
SMRiQ8TAF3. Positions 12-563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati28 – 6740WD 1Add
BLAST
Repeati73 – 11240WD 2Add
BLAST
Repeati115 – 15440WD 3Add
BLAST
Repeati166 – 20540WD 4Add
BLAST
Repeati208 – 24740WD 5Add
BLAST
Repeati250 – 28940WD 6Add
BLAST
Repeati292 – 33443WD 7Add
BLAST
Repeati358 – 39740WD 8Add
BLAST

Domaini

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.Curated1 Publication

Sequence similaritiesi

Belongs to the WD repeat WDR48 family.Curated
Contains 8 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0308. Eukaryota.
ENOG410XRJ5. LUCA.
GeneTreeiENSGT00820000127095.
HOVERGENiHBG079413.
InParanoidiQ8TAF3.
KOiK15361.
OMAiENEINHV.
OrthoDBiEOG7JDQX1.
PhylomeDBiQ8TAF3.
TreeFamiTF315205.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR021772. DUF3337.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF11816. DUF3337. 1 hit.
PF00400. WD40. 4 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TAF3-1) [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

        10         20         30         40         50
MAAHHRQNTA GRRKVQVSYV IRDEVEKYNR NGVNALQLDP ALNRLFTAGR
60 70 80 90 100
DSIIRIWSVN QHKQDPYIAS MEHHTDWVND IVLCCNGKTL ISASSDTTVK
110 120 130 140 150
VWNAHKGFCM STLRTHKDYV KALAYAKDKE LVASAGLDRQ IFLWDVNTLT
160 170 180 190 200
ALTASNNTVT TSSLSGNKDS IYSLAMNQLG TIIVSGSTEK VLRVWDPRTC
210 220 230 240 250
AKLMKLKGHT DNVKALLLNR DGTQCLSGSS DGTIRLWSLG QQRCIATYRV
260 270 280 290 300
HDEGVWALQV NDAFTHVYSG GRDRKIYCTD LRNPDIRVLI CEEKAPVLKM
310 320 330 340 350
ELDRSADPPP AIWVATTKST VNKWTLKGIH NFRASGDYDN DCTNPITPLC
360 370 380 390 400
TQPDQVIKGG ASIIQCHILN DKRHILTKDT NNNVAYWDVL KACKVEDLGK
410 420 430 440 450
VDFEDEIKKR FKMVYVPNWF SVDLKTGMLT ITLDESDCFA AWVSAKDAGF
460 470 480 490 500
SSPDGSDPKL NLGGLLLQAL LEYWPRTHVN PMDEEENEVN HVNGEQENRV
510 520 530 540 550
QKGNGYFQVP PHTPVIFGEA GGRTLFRLLC RDSGGETESM LLNETVPQWV
560 570 580 590 600
IDITVDKNMP KFNKIPFYLQ PHASSGAKTL KKDRLSASDM LQVRKVMEHV
610 620 630 640 650
YEKIINLDNE SQTTSSSNNE KPGEQEKEED IAVLAEEKIE LLCQDQVLDP
660 670
NMDLRTVKHF IWKSGGDLTL HYRQKST
Length:677
Mass (Da):76,210
Last modified:June 1, 2002 - v1
Checksum:i20FDA620E02696E0
GO
Isoform 2 (identifier: Q8TAF3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-558: Missing.
     645-645: D → DQV

Note: No experimental confirmation available.
Show »
Length:121
Mass (Da):13,931
Checksum:iA1F40FA39E591BD9
GO
Isoform 3 (identifier: Q8TAF3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     91-99: Missing.

Note: No experimental confirmation available.
Show »
Length:668
Mass (Da):75,349
Checksum:i379C3527CC632FCF
GO
Isoform 4 (identifier: Q8TAF3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: MAAHHRQNTA...IVLCCNGKTL → MECQSAQV

Note: No experimental confirmation available.
Show »
Length:595
Mass (Da):66,707
Checksum:i3752FA8E527D8F7E
GO
Isoform 5 (identifier: Q8TAF3-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     16-223: Missing.
     325-391: Missing.

Note: No experimental confirmation available.
Show »
Length:402
Mass (Da):45,552
Checksum:iF524F725C929EBD6
GO

Sequence cautioni

The sequence AAH37168.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA95973.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAH56182.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAH56300.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611T → A in AAH37168 (PubMed:15489334).Curated
Sequence conflicti286 – 2861I → V in BAG63646 (PubMed:14702039).Curated
Sequence conflicti319 – 3191S → F in BAG63646 (PubMed:14702039).Curated
Sequence conflicti328 – 3281G → E in BAG63646 (PubMed:14702039).Curated
Sequence conflicti585 – 5851L → P in BAG63646 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 558558Missing in isoform 2. 1 PublicationVSP_016776Add
BLAST
Alternative sequencei1 – 9090MAAHH…NGKTL → MECQSAQV in isoform 4. 1 PublicationVSP_037623Add
BLAST
Alternative sequencei16 – 223208Missing in isoform 5. 1 PublicationVSP_037624Add
BLAST
Alternative sequencei91 – 999Missing in isoform 3. 1 PublicationVSP_037625
Alternative sequencei325 – 39167Missing in isoform 5. 1 PublicationVSP_037626Add
BLAST
Alternative sequencei645 – 6451D → DQV in isoform 2. 1 PublicationVSP_016777

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF468833 mRNA. Translation: AAL78650.1.
AB040882 mRNA. Translation: BAA95973.2. Different initiation.
AK297349 mRNA. Translation: BAG59798.1.
AK298810 mRNA. Translation: BAG60944.1.
AK302307 mRNA. Translation: BAG63646.1.
AL162064 mRNA. Translation: CAB82402.1.
AL832926 mRNA. Translation: CAH56300.1. Different initiation.
BX649170 mRNA. Translation: CAH56182.1. Different initiation.
BC026353 mRNA. Translation: AAH26353.1.
BC037168 mRNA. Translation: AAH37168.1. Different initiation.
CCDSiCCDS33738.1. [Q8TAF3-1]
PIRiT47168.
RefSeqiNP_001290331.1. NM_001303402.1. [Q8TAF3-4]
NP_001290332.1. NM_001303403.1. [Q8TAF3-3]
NP_065890.1. NM_020839.3. [Q8TAF3-1]
UniGeneiHs.109778.

Genome annotation databases

EnsembliENST00000302313; ENSP00000307491; ENSG00000114742. [Q8TAF3-1]
GeneIDi57599.
KEGGihsa:57599.
UCSCiuc003cit.4. human. [Q8TAF3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF468833 mRNA. Translation: AAL78650.1.
AB040882 mRNA. Translation: BAA95973.2. Different initiation.
AK297349 mRNA. Translation: BAG59798.1.
AK298810 mRNA. Translation: BAG60944.1.
AK302307 mRNA. Translation: BAG63646.1.
AL162064 mRNA. Translation: CAB82402.1.
AL832926 mRNA. Translation: CAH56300.1. Different initiation.
BX649170 mRNA. Translation: CAH56182.1. Different initiation.
BC026353 mRNA. Translation: AAH26353.1.
BC037168 mRNA. Translation: AAH37168.1. Different initiation.
CCDSiCCDS33738.1. [Q8TAF3-1]
PIRiT47168.
RefSeqiNP_001290331.1. NM_001303402.1. [Q8TAF3-4]
NP_001290332.1. NM_001303403.1. [Q8TAF3-3]
NP_065890.1. NM_020839.3. [Q8TAF3-1]
UniGeneiHs.109778.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5CVLX-ray3.00A2-580[»]
5CVNX-ray3.36A2-580[»]
5CVOX-ray3.88A/D1-677[»]
ProteinModelPortaliQ8TAF3.
SMRiQ8TAF3. Positions 12-563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121649. 76 interactions.
IntActiQ8TAF3. 62 interactions.
MINTiMINT-3043701.
STRINGi9606.ENSP00000307491.

PTM databases

iPTMnetiQ8TAF3.
PhosphoSiteiQ8TAF3.

Polymorphism and mutation databases

BioMutaiWDR48.
DMDMi74760390.

Proteomic databases

EPDiQ8TAF3.
MaxQBiQ8TAF3.
PaxDbiQ8TAF3.
PeptideAtlasiQ8TAF3.
PRIDEiQ8TAF3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302313; ENSP00000307491; ENSG00000114742. [Q8TAF3-1]
GeneIDi57599.
KEGGihsa:57599.
UCSCiuc003cit.4. human. [Q8TAF3-1]

Organism-specific databases

CTDi57599.
GeneCardsiWDR48.
HGNCiHGNC:30914. WDR48.
HPAiHPA038421.
MalaCardsiWDR48.
MIMi612167. gene.
neXtProtiNX_Q8TAF3.
Orphaneti401800. Autosomal recessive spastic paraplegia type 60.
PharmGKBiPA134956949.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0308. Eukaryota.
ENOG410XRJ5. LUCA.
GeneTreeiENSGT00820000127095.
HOVERGENiHBG079413.
InParanoidiQ8TAF3.
KOiK15361.
OMAiENEINHV.
OrthoDBiEOG7JDQX1.
PhylomeDBiQ8TAF3.
TreeFamiTF315205.

Enzyme and pathway databases

SignaLinkiQ8TAF3.

Miscellaneous databases

ChiTaRSiWDR48. human.
GenomeRNAii57599.
PROiQ8TAF3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TAF3.
CleanExiHS_WDR48.
ExpressionAtlasiQ8TAF3. baseline and differential.
GenevisibleiQ8TAF3. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR021772. DUF3337.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF11816. DUF3337. 1 hit.
PF00400. WD40. 4 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Herpesviral protein targets a cellular WD repeat endosomal protein to downregulate T lymphocyte receptor expression."
    Park J., Lee B.-S., Choi J.-K., Means R.E., Choe J., Jung J.U.
    Immunity 17:221-233(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH TIP.
  2. "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."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
    Tissue: Brain, Teratocarcinoma and Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-677 (ISOFORM 1).
    Tissue: Melanoma, Retina and Stomach.
  6. "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).
    Tissue: Brain and Eye.
  7. "Distinct roles of cellular Lck and p80 proteins in herpesvirus saimiri Tip function on lipid rafts."
    Park J., Cho N.-H., Choi J.-K., Feng P., Choe J., Jung J.U.
    J. Virol. 77:9041-9051(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HERPESVIRUS SAIMIRI TIP.
  8. "A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway."
    Cohn M.A., Kowal P., Yang K., Haas W., Huang T.T., Gygi S.P., D'Andrea A.D.
    Mol. Cell 28:786-797(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH USP1.
  9. "Human papillomavirus E1 helicase interacts with the WD repeat protein p80 to promote maintenance of the viral genome in keratinocytes."
    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.
    J. Virol. 82:1271-1283(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HPV11 E1.
  10. "UAF1 is a subunit of multiple deubiquitinating enzyme complexes."
    Cohn M.A., Kee Y., Haas W., Gygi S.P., D'Andrea A.D.
    J. Biol. Chem. 284:5343-5351(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH USP12 AND USP46.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-613, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Structural insights into WD-repeat 48 activation of ubiquitin-specific protease 46."
    Yin J., Schoeffler A.J., Wickliffe K., Newton K., Starovasnik M.A., Dueber E.C., Harris S.F.
    Structure 23:2043-2054(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-580 IN COMPLEX WITH USP46 AND UBIQUITIN, INTERACTION WITH USP46 AND USP1, FUNCTION, MUTAGENESIS OF SER-170; LYS-214; TRP-256 AND ARG-272.

Entry informationi

Entry nameiWDR48_HUMAN
AccessioniPrimary (citable) accession number: Q8TAF3
Secondary accession number(s): B4DM86
, B4DQI2, B4DY84, Q63HJ2, Q658Y1, Q8N3Z1, Q9NSK8, Q9P279
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.