RBCC

Full text data of WDR44

WDR44 [Confidence: low (only semi-automatic identification from reviews)]
WD repeat-containing protein 44 (Rabphilin-11)

UniProt Q5JSH3
ID WDR44_HUMAN Reviewed; 913 AA.
AC Q5JSH3; B4DSE9; F8W913; Q0JS52; Q0JTF3; Q5JSH2; Q6ZSC1; Q7Z365;
read moreAC Q7Z3P6; Q8NAU8; Q8NHU5; Q9NUV4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=WD repeat-containing protein 44;
DE AltName: Full=Rabphilin-11;
GN Name=WDR44;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
RP NUCLEOTIDE 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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
RP 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
RT project: 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-96, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation 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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient 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 MASS SPECTROMETRY.
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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS
RP SPECTROMETRY.
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
RP SCALE ANALYSIS] AT SER-3; SER-27; SER-50; SER-96; THR-219; SER-262;
RP SER-342 AND SER-403, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Downstream effector for RAB11. May be involved in
CC vesicle recycling (By similarity).
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
CC (By similarity).
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 (By similarity).
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q5JSH3-3; Sequence=VSP_021807, VSP_021808, VSP_021810;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q5JSH3-4; Sequence=VSP_046637, VSP_046638;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92015.1; Type=Frameshift; Positions=792;
CC Sequence=BAC03799.1; Type=Erroneous initiation;
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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; CAI41402.1; -; Genomic_DNA.
DR EMBL; AL391803; CAI41402.1; JOINED; Genomic_DNA.
DR EMBL; AL391830; CAI41402.1; JOINED; Genomic_DNA.
DR EMBL; AL391474; CAI41403.1; -; Genomic_DNA.
DR EMBL; AL391803; CAI41403.1; JOINED; Genomic_DNA.
DR EMBL; AL391830; CAI41403.1; JOINED; Genomic_DNA.
DR EMBL; AL391803; CAI41482.1; -; Genomic_DNA.
DR EMBL; AL391474; CAI41482.1; JOINED; Genomic_DNA.
DR EMBL; AL391830; CAI41482.1; JOINED; Genomic_DNA.
DR EMBL; AL391803; CAI41483.1; -; Genomic_DNA.
DR EMBL; AL391474; CAI41483.1; JOINED; Genomic_DNA.
DR EMBL; AL391830; CAI41483.1; JOINED; Genomic_DNA.
DR EMBL; AL391830; CAI41512.1; -; Genomic_DNA.
DR EMBL; AL391474; CAI41512.1; JOINED; Genomic_DNA.
DR EMBL; AL391803; CAI41512.1; JOINED; Genomic_DNA.
DR EMBL; AL391830; CAI41513.1; -; Genomic_DNA.
DR EMBL; AL391474; CAI41513.1; JOINED; Genomic_DNA.
DR EMBL; AL391803; CAI41513.1; JOINED; Genomic_DNA.
DR EMBL; BC028697; AAH28697.3; -; mRNA.
DR RefSeq; NP_001171894.1; NM_001184965.1.
DR RefSeq; NP_001171895.1; NM_001184966.1.
DR RefSeq; NP_061918.3; NM_019045.4.
DR UniGene; Hs.98510; -.
DR ProteinModelPortal; Q5JSH3; -.
DR SMR; Q5JSH3; 501-865.
DR IntAct; Q5JSH3; 2.
DR MINT; MINT-4650026; -.
DR PhosphoSite; Q5JSH3; -.
DR DMDM; 74762196; -.
DR PaxDb; Q5JSH3; -.
DR PRIDE; Q5JSH3; -.
DR DNASU; 54521; -.
DR Ensembl; ENST00000254029; ENSP00000254029; ENSG00000131725.
DR Ensembl; ENST00000371822; ENSP00000360887; ENSG00000131725.
DR Ensembl; ENST00000371825; ENSP00000360890; ENSG00000131725.
DR GeneID; 54521; -.
DR KEGG; hsa:54521; -.
DR UCSC; uc011mtr.2; human.
DR CTD; 54521; -.
DR GeneCards; GC0XP117480; -.
DR H-InvDB; HIX0017006; -.
DR HGNC; HGNC:30512; WDR44.
DR HPA; HPA038084; -.
DR neXtProt; NX_Q5JSH3; -.
DR PharmGKB; PA128394668; -.
DR eggNOG; COG2319; -.
DR HOVERGEN; HBG080376; -.
DR InParanoid; Q5JSH3; -.
DR OMA; HDFSYLV; -.
DR OrthoDB; EOG7W6WK0; -.
DR PhylomeDB; Q5JSH3; -.
DR SignaLink; Q5JSH3; -.
DR GeneWiki; WDR44; -.
DR GenomeRNAi; 54521; -.
DR NextBio; 56920; -.
DR PRO; PR:Q5JSH3; -.
DR ArrayExpress; Q5JSH3; -.
DR Bgee; Q5JSH3; -.
DR CleanEx; HS_WDR44; -.
DR Genevestigator; Q5JSH3; -.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
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; Complete proteome;
KW Cytoplasm; Endosome; Golgi apparatus; Membrane; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 913 WD repeat-containing protein 44.
FT /FTId=PRO_0000262769.
FT REPEAT 509 548 WD 1.
FT REPEAT 605 643 WD 2.
FT REPEAT 645 685 WD 3.
FT REPEAT 690 729 WD 4.
FT REPEAT 740 779 WD 5.
FT REPEAT 784 823 WD 6.
FT REPEAT 876 913 WD 7.
FT REGION 2 170 Binding activity.
FT COILED 119 184 Potential.
FT COMPBIAS 211 257 Pro-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 3 3 Phosphoserine.
FT MOD_RES 11 11 Phosphotyrosine.
FT MOD_RES 27 27 Phosphoserine.
FT MOD_RES 50 50 Phosphoserine.
FT MOD_RES 96 96 Phosphoserine.
FT MOD_RES 219 219 Phosphothreonine.
FT MOD_RES 262 262 Phosphoserine.
FT MOD_RES 271 271 Phosphothreonine.
FT MOD_RES 342 342 Phosphoserine.
FT MOD_RES 403 403 Phosphoserine.
FT MOD_RES 470 470 Phosphoserine.
FT MOD_RES 471 471 Phosphoserine.
FT MOD_RES 472 472 Phosphoserine.
FT MOD_RES 561 561 Phosphoserine.
FT MOD_RES 565 565 Phosphoserine.
FT VAR_SEQ 1 473 Missing (in isoform 3).
FT /FTId=VSP_021807.
FT VAR_SEQ 37 61 Missing (in isoform 4).
FT /FTId=VSP_046637.
FT VAR_SEQ 474 477 DEGM -> MVNV (in isoform 3).
FT /FTId=VSP_021808.
FT VAR_SEQ 659 722 Missing (in isoform 4).
FT /FTId=VSP_046638.
FT VAR_SEQ 796 803 Missing (in isoform 2).
FT /FTId=VSP_021809.
FT VAR_SEQ 884 913 IMKTDNTEVLLSADFTGAIKVFVNKRKNVS -> AVAHACN
FT PSTLGGRGRRIT (in isoform 3).
FT /FTId=VSP_021810.
FT VARIANT 289 289 A -> T (in dbSNP:rs17271416).
FT /FTId=VAR_029538.
FT VARIANT 296 296 T -> A (in dbSNP:rs17855531).
FT /FTId=VAR_029539.
FT CONFLICT 89 89 L -> P (in Ref. 2; CAD97788).
FT CONFLICT 96 96 S -> G (in Ref. 2; CAL38210).
FT CONFLICT 194 194 S -> P (in Ref. 4; AAH28697).
FT CONFLICT 206 206 V -> A (in Ref. 2; CAL38662).
FT CONFLICT 250 250 P -> L (in Ref. 2; CAL38662).
FT CONFLICT 276 276 V -> A (in Ref. 1; BAG61611).
FT CONFLICT 331 331 A -> P (in Ref. 2; CAD98010).
FT CONFLICT 380 380 G -> D (in Ref. 2; CAL38210).
FT CONFLICT 473 473 D -> N (in Ref. 2; CAL38662).
FT CONFLICT 534 534 V -> A (in Ref. 2; CAD97788).
FT CONFLICT 539 539 A -> L (in Ref. 2; CAD97788).
FT CONFLICT 547 547 F -> L (in Ref. 1; BAG61611).
FT CONFLICT 586 586 E -> G (in Ref. 2; CAD97788).
FT CONFLICT 613 613 L -> P (in Ref. 2; CAL38662).
FT CONFLICT 649 650 Missing (in Ref. 1; BAA92015).
FT CONFLICT 740 740 K -> R (in Ref. 2; CAL38210/CAL38662).
FT CONFLICT 858 858 L -> S (in Ref. 2; CAL38662).
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
//

RBCC Red Blood Cell Collection

Full text data of WDR44