WDR44_HUMAN
ID WDR44_HUMAN Reviewed; 913 AA.
AC Q5JSH3; B4DSE9; F8W913; Q0JS52; Q0JTF3; Q5JSH2; Q6ZSC1; Q7Z365; Q7Z3P6;
AC Q8NAU8; Q8NHU5; Q9NUV4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=WD repeat-containing protein 44;
DE AltName: Full=Rabphilin-11;
GN Name=WDR44; Synonyms=RPH11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 190-913 (ISOFORM 1).
RC TISSUE=Brain, Teratocarcinoma, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-289.
RC TISSUE=Colon endothelium, and Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-296.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11; SER-27; SER-262 AND
RP SER-403, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-96, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; THR-219; SER-262;
RP SER-403; SER-470; SER-471 AND SER-472, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-403, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3; SER-27; SER-50; SER-96; THR-219; SER-262; SER-342 AND
RP SER-403, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-262; THR-271;
RP SER-403; SER-561 AND SER-565, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-66; SER-71; SER-81;
RP SER-96; SER-126; THR-158; THR-219; SER-262; SER-344; SER-403 AND SER-561,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-96; THR-349; SER-403
RP AND SER-561, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Downstream effector for RAB11. May be involved in vesicle
CC recycling (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the GTP-bound form of RAB11 when membrane-
CC associated. Does not bind to other Rab and Rho small G proteins (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q5JSH3; P16284: PECAM1; NbExp=3; IntAct=EBI-3441235, EBI-716404;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, perinuclear
CC region. Endosome membrane. Golgi apparatus, trans-Golgi network.
CC Note=Colocalized with RAB11 along microtubules oriented toward
CC lamellipodia. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5JSH3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JSH3-2; Sequence=VSP_021809;
CC Name=3;
CC IsoId=Q5JSH3-3; Sequence=VSP_021807, VSP_021808, VSP_021810;
CC Name=4;
CC IsoId=Q5JSH3-4; Sequence=VSP_046637, VSP_046638;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92015.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC03799.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK001978; BAA92015.1; ALT_SEQ; mRNA.
DR EMBL; AK092077; BAC03799.1; ALT_INIT; mRNA.
DR EMBL; AK127556; BAC87033.1; -; mRNA.
DR EMBL; AK299711; BAG61611.1; -; mRNA.
DR EMBL; AM393332; CAL38210.1; -; mRNA.
DR EMBL; AM393787; CAL38662.1; -; mRNA.
DR EMBL; BX537578; CAD97788.1; -; mRNA.
DR EMBL; BX538087; CAD98010.1; -; mRNA.
DR EMBL; AL391474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028697; AAH28697.3; -; mRNA.
DR CCDS; CCDS14572.1; -. [Q5JSH3-1]
DR CCDS; CCDS55482.1; -. [Q5JSH3-2]
DR CCDS; CCDS55483.1; -. [Q5JSH3-4]
DR RefSeq; NP_001171894.1; NM_001184965.1. [Q5JSH3-2]
DR RefSeq; NP_001171895.1; NM_001184966.1. [Q5JSH3-4]
DR RefSeq; NP_061918.3; NM_019045.4. [Q5JSH3-1]
DR AlphaFoldDB; Q5JSH3; -.
DR SMR; Q5JSH3; -.
DR BioGRID; 120014; 81.
DR ELM; Q5JSH3; -.
DR IntAct; Q5JSH3; 17.
DR STRING; 9606.ENSP00000254029; -.
DR GlyGen; Q5JSH3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5JSH3; -.
DR MetOSite; Q5JSH3; -.
DR PhosphoSitePlus; Q5JSH3; -.
DR BioMuta; WDR44; -.
DR DMDM; 74762196; -.
DR EPD; Q5JSH3; -.
DR jPOST; Q5JSH3; -.
DR MassIVE; Q5JSH3; -.
DR MaxQB; Q5JSH3; -.
DR PaxDb; Q5JSH3; -.
DR PeptideAtlas; Q5JSH3; -.
DR PRIDE; Q5JSH3; -.
DR ProteomicsDB; 30239; -.
DR ProteomicsDB; 63151; -. [Q5JSH3-1]
DR ProteomicsDB; 63152; -. [Q5JSH3-2]
DR ProteomicsDB; 63153; -. [Q5JSH3-3]
DR Antibodypedia; 29682; 36 antibodies from 13 providers.
DR DNASU; 54521; -.
DR Ensembl; ENST00000254029.8; ENSP00000254029.3; ENSG00000131725.14. [Q5JSH3-1]
DR Ensembl; ENST00000371822.9; ENSP00000360887.5; ENSG00000131725.14. [Q5JSH3-4]
DR Ensembl; ENST00000371825.7; ENSP00000360890.3; ENSG00000131725.14. [Q5JSH3-2]
DR GeneID; 54521; -.
DR KEGG; hsa:54521; -.
DR MANE-Select; ENST00000254029.8; ENSP00000254029.3; NM_019045.5; NP_061918.3.
DR UCSC; uc004eqn.4; human. [Q5JSH3-1]
DR CTD; 54521; -.
DR GeneCards; WDR44; -.
DR HGNC; HGNC:30512; WDR44.
DR HPA; ENSG00000131725; Low tissue specificity.
DR MIM; 301070; gene.
DR neXtProt; NX_Q5JSH3; -.
DR OpenTargets; ENSG00000131725; -.
DR PharmGKB; PA128394668; -.
DR VEuPathDB; HostDB:ENSG00000131725; -.
DR eggNOG; KOG0283; Eukaryota.
DR GeneTree; ENSGT00940000157557; -.
DR HOGENOM; CLU_009835_2_1_1; -.
DR InParanoid; Q5JSH3; -.
DR OMA; MENANRP; -.
DR OrthoDB; 1332590at2759; -.
DR PhylomeDB; Q5JSH3; -.
DR TreeFam; TF329226; -.
DR PathwayCommons; Q5JSH3; -.
DR SignaLink; Q5JSH3; -.
DR BioGRID-ORCS; 54521; 32 hits in 717 CRISPR screens.
DR ChiTaRS; WDR44; human.
DR GeneWiki; WDR44; -.
DR GenomeRNAi; 54521; -.
DR Pharos; Q5JSH3; Tdark.
DR PRO; PR:Q5JSH3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q5JSH3; protein.
DR Bgee; ENSG00000131725; Expressed in buccal mucosa cell and 194 other tissues.
DR ExpressionAtlas; Q5JSH3; baseline and differential.
DR Genevisible; Q5JSH3; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR040324; WDR44/Dgr2.
DR PANTHER; PTHR14221; PTHR14221; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Endosome;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231"
FT CHAIN 2..913
FT /note="WD repeat-containing protein 44"
FT /id="PRO_0000262769"
FT REPEAT 509..548
FT /note="WD 1"
FT REPEAT 605..643
FT /note="WD 2"
FT REPEAT 645..685
FT /note="WD 3"
FT REPEAT 690..729
FT /note="WD 4"
FT REPEAT 740..779
FT /note="WD 5"
FT REPEAT 784..823
FT /note="WD 6"
FT REPEAT 876..913
FT /note="WD 7"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..170
FT /note="Binding activity"
FT REGION 205..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..184
FT /evidence="ECO:0000255"
FT COMPBIAS 231..255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 11
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 349
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 479
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6NVE8"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..473
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021807"
FT VAR_SEQ 37..61
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046637"
FT VAR_SEQ 474..477
FT /note="DEGM -> MVNV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021808"
FT VAR_SEQ 659..722
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046638"
FT VAR_SEQ 796..803
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_021809"
FT VAR_SEQ 884..913
FT /note="IMKTDNTEVLLSADFTGAIKVFVNKRKNVS -> AVAHACNPSTLGGRGRRI
FT T (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021810"
FT VARIANT 289
FT /note="A -> T (in dbSNP:rs17271416)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_029538"
FT VARIANT 296
FT /note="T -> A (in dbSNP:rs17855531)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029539"
FT CONFLICT 89
FT /note="L -> P (in Ref. 2; CAD97788)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="S -> G (in Ref. 2; CAL38210)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="S -> P (in Ref. 4; AAH28697)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="V -> A (in Ref. 2; CAL38662)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="P -> L (in Ref. 2; CAL38662)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="V -> A (in Ref. 1; BAG61611)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> P (in Ref. 2; CAD98010)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="G -> D (in Ref. 2; CAL38210)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="D -> N (in Ref. 2; CAL38662)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="V -> A (in Ref. 2; CAD97788)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="A -> L (in Ref. 2; CAD97788)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="F -> L (in Ref. 1; BAG61611)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="E -> G (in Ref. 2; CAD97788)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="L -> P (in Ref. 2; CAL38662)"
FT /evidence="ECO:0000305"
FT CONFLICT 649..650
FT /note="Missing (in Ref. 1; BAA92015)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="K -> R (in Ref. 2; CAL38210/CAL38662)"
FT /evidence="ECO:0000305"
FT CONFLICT 858
FT /note="L -> S (in Ref. 2; CAL38662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 913 AA; 101366 MW; 8E43761C542DD6B9 CRC64;
MASESDTEEF YDAPEDVHLG GGYPVGSPGK VGLSTFKETE NTAYKVGNES PVQELKQDVS
KKIIESIIEE SQKVLQLEDD SLDSKGKELS DQATASPIVA RTDLSNIPGL LAIDQVLPEE
SQKAESQNTF EETELELKKC FPSDETCEKP VDETTKLTQT SSTEQLNVLE TETEVLNKEA
VEVKGGGDVL EPVSSDSLST KDFAAVEEVA PAKPPRHLTP EPDIVASTKK PVPARPPPPT
NFPPPRPPPP SRPAPPPRKR KSELEFETLK TPDIDVPKEN ITSDSLLTAS MASESTVKDS
QPSLDLASAT SGDKIVTAQE NGKAPDGQTV AGEVMGPQRP RSNSGRELTD EEILASVMIK
NLDTGEEIPL SLAEEKLPTG INPLTLHIMR RTKEYVSNDA AQSDDEEKLQ SQPTDTDGGR
LKQKTTQLKK FLGKSVKRAK HLAEEYGERA INKVKSVRDE VFHTDQDDPS SSDDEGMPYT
RPVKFKAAHG FKGPYDFDQI KVVQDLSGEH MGAVWTMKFS HCGRLLASAG QDNVVRIWAL
KNAFDYFNNM RMKYNTEGRV SPSPSQESLS SSKSDTDTGV CSGTDEDPDD KNAPFRQRPF
CKYKGHTADL LDLSWSKNYF LLSSSMDKTV RLWHISRREC LCCFQHIDFV TAIAFHPRDD
RYFLSGSLDG KLRLWNIPDK KVALWNEVDG QTKLITAANF CQNGKYAVIG TYDGRCIFYD
TEHLKYHTQI HVRSTRGRNK VGRKITGIEP LPGENKILVT SNDSRIRLYD LRDLSLSMKY
KGYVNSSSQI KASFSHDFTY LVSGSEDKYV YIWSTYHDLS KFTSVRRDRN DFWEGIKAHN
AVVTSAIFAP NPSLMLSLDV QSEKSEGNEK SEDAEVLDAT PSGIMKTDNT EVLLSADFTG
AIKVFVNKRK NVS
