UBR4_HUMAN
ID UBR4_HUMAN Reviewed; 5183 AA.
AC Q5T4S7; A8MPT2; A8MQ33; A8MQB1; O60646; O75050; Q4QRK5; Q5T4S8; Q5T4S9;
AC Q5TBN8; Q5TBP2; Q6DKH8; Q6P4A4; Q7L8P7; Q8IXJ4; Q8TDN5; Q8WV67; Q9HA46;
AC Q9P2N9; Q9UG82;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=E3 ubiquitin-protein ligase UBR4;
DE EC=2.3.2.27;
DE AltName: Full=600 kDa retinoblastoma protein-associated factor;
DE AltName: Full=N-recognin-4;
DE AltName: Full=RING-type E3 ubiquitin transferase UBR4;
DE AltName: Full=Retinoblastoma-associated factor of 600 kDa;
DE Short=RBAF600;
DE Short=p600;
DE AltName: Full=Zinc finger UBR1-type protein 1;
GN Name=UBR4; Synonyms=KIAA0462, KIAA1307, RBAF600, ZUBR1;
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 [MRNA] (ISOFORM 1), INTERACTION WITH RB1 AND CALM,
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16214886; DOI=10.1073/pnas.0507458102;
RA Nakatani Y., Konishi H., Vassilev A., Kurooka H., Ishiguro K., Sawada J.,
RA Ikura T., Korsmeyer S.J., Qin J., Herlitz A.M.;
RT "p600, a unique protein required for membrane morphogenesis and cell
RT survival.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15093-15098(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP PROTEIN SEQUENCE OF 166-185; 435-443; 850-857; 921-931; 1065-1079;
RP 1131-1141; 1175-1192; 1195-1208; 1286-1293; 1337-1349; 1434-1440;
RP 1464-1470; 1478-1489; 1731-1757; 1838-1850; 1875-1886; 1909-1918;
RP 1921-1931; 2048-2058; 2131-2138; 2211-2218; 2354-2381; 2527-2536;
RP 2564-2572; 2713-2721; 2981-2989; 3046-3065; 3229-3238; 3243-3252;
RP 3589-3606; 3618-3628; 3735-3745; 3809-3816; 3827-3836; 3845-3857;
RP 3889-3915; 4131-4142; 4204-4215; 4320-4334; 4414-4426; 4608-4637;
RP 4686-4696; 4717-4724; 4803-4814; 4852-4860; 5013-5022 AND 5062-5069,
RP PHOSPHORYLATION AT SER-2719, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 779-5183 (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2908-5183 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4385-5183 (ISOFORMS 1 AND 2), AND
RP VARIANT LEU-4867.
RC TISSUE=Kidney, Liver, Lung, and Spleen;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4583-5183 (ISOFORM 1), AND VARIANTS LEU-4867
RP AND ARG-4924.
RX PubMed=16247014; DOI=10.1073/pnas.0500090102;
RA Lennerz V., Fatho M., Gentilini C., Frye R.A., Lifke A., Ferel D.,
RA Woelfel C., Huber C., Woelfel T.;
RT "The response of autologous T cells to a human melanoma is dominated by
RT mutated neoantigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16013-16018(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4686-5183 (ISOFORM 1).
RC TISSUE=Brain;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4709-5183 (ISOFORM 1), AND
RP VARIANT LEU-4867.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP INTERACTION WITH HPV-16 E7; HPV-6B E7 AND HPV-11 E7 (MICROBIAL INFECTION),
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=16061792; DOI=10.1073/pnas.0505337102;
RA Huh K.-W., DeMasi J., Ogawa H., Nakatani Y., Howley P.M., Muenger K.;
RT "Association of the human papillomavirus type 16 E7 oncoprotein with the
RT 600-kDa retinoblastoma protein-associated factor, p600.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11492-11497(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181 AND THR-2715,
RP AND IDENTIFICATION BY MASS 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1084, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181 AND SER-1763,
RP AND 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2719, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181; THR-905;
RP SER-1747; SER-1878; SER-1904; THR-2715 AND SER-2719, AND IDENTIFICATION BY
RP 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 [21]
RP FUNCTION.
RX PubMed=23932781; DOI=10.1016/j.molcel.2013.07.002;
RA Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.;
RT "Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and
RT tumor growth.";
RL Mol. Cell 51:506-518(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1647; SER-1652; THR-2944 AND
RP SER-2952, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
RN [23]
RP INTERACTION WITH RIFT VALLEY FEVER VIRUS GLYCOPROTEIN N (MICROBIAL
RP INFECTION).
RX PubMed=35032865; DOI=10.1016/j.virol.2021.12.010;
RA Bracci N., de la Fuente C., Saleem S., Pinkham C., Narayanan A.,
RA Garcia-Sastre A., Balaraman V., Richt J.A., Wilson W., Kehn-Hall K.;
RT "Rift Valley fever virus Gn V5-epitope tagged virus enables identification
RT of UBR4 as a Gn interacting protein that facilitates Rift Valley fever
RT virus production.";
RL Virology 567:65-76(2022).
RN [24]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-1394.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation. Together
CC with clathrin, forms meshwork structures involved in membrane
CC morphogenesis and cytoskeletal organization. Regulates integrin-
CC mediated signaling. May play a role in activation of FAK in response to
CC cell-matrix interactions. Mediates ubiquitination of ACLY, leading to
CC its subsequent degradation. {ECO:0000269|PubMed:16214886,
CC ECO:0000269|PubMed:23932781}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with RB1 and calmodulin.
CC {ECO:0000269|PubMed:16214886}.
CC -!- SUBUNIT: (Microbial infection) Interacts with protein E7 from papilloma
CC virus HPV-16, HPV-6B and HPV-11. {ECO:0000269|PubMed:16061792}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Rift valley fever virus
CC glycoprotein N; this interaction is important for viral RNA production.
CC {ECO:0000269|PubMed:35032865}.
CC -!- INTERACTION:
CC Q5T4S7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1995940, EBI-5235340;
CC Q5T4S7; Q93009: USP7; NbExp=2; IntAct=EBI-1995940, EBI-302474;
CC Q5T4S7; P03129: E7; Xeno; NbExp=5; IntAct=EBI-1995940, EBI-866453;
CC Q5T4S7; P04020: E7; Xeno; NbExp=2; IntAct=EBI-1995940, EBI-7005254;
CC Q5T4S7; P06464: E7; Xeno; NbExp=2; IntAct=EBI-1995940, EBI-6944797;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cytoplasm. Cytoplasm, cytoskeleton. Nucleus.
CC Note=Concentrates at the leading edge of membrane structures involved
CC in actin motility.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q5T4S7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T4S7-2; Sequence=VSP_025209;
CC Name=3;
CC IsoId=Q5T4S7-3; Sequence=VSP_025203, VSP_025206;
CC Name=4;
CC IsoId=Q5T4S7-4; Sequence=VSP_025205, VSP_025206;
CC Name=5;
CC IsoId=Q5T4S7-5; Sequence=VSP_025201, VSP_025202, VSP_025204;
CC Name=6;
CC IsoId=Q5T4S7-6; Sequence=VSP_025200, VSP_025207, VSP_025208;
CC -!- SIMILARITY: Belongs to the UBR4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD43719.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF348492; AAL83880.1; -; mRNA.
DR EMBL; AK022322; BAB14011.1; -; mRNA.
DR EMBL; AL137127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB037728; BAA92545.1; -; mRNA.
DR EMBL; AB007931; BAA32307.1; -; mRNA.
DR EMBL; BC018694; AAH18694.2; -; mRNA.
DR EMBL; BC063573; AAH63573.1; -; mRNA.
DR EMBL; BC073905; AAH73905.1; -; mRNA.
DR EMBL; BC096758; AAH96758.1; -; mRNA.
DR EMBL; AJ505016; CAD43719.1; ALT_INIT; mRNA.
DR EMBL; AL049972; CAB43227.1; -; mRNA.
DR EMBL; AF055010; AAC09360.1; -; mRNA.
DR CCDS; CCDS189.1; -. [Q5T4S7-1]
DR PIR; T00076; T00076.
DR RefSeq; NP_065816.2; NM_020765.2. [Q5T4S7-1]
DR BioGRID; 116934; 251.
DR CORUM; Q5T4S7; -.
DR IntAct; Q5T4S7; 114.
DR MINT; Q5T4S7; -.
DR STRING; 9606.ENSP00000364403; -.
DR ChEMBL; CHEMBL4295851; -.
DR DrugBank; DB05483; PCL-016.
DR DrugBank; DB04959; Verpasep caltespen.
DR CarbonylDB; Q5T4S7; -.
DR GlyGen; Q5T4S7; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q5T4S7; -.
DR MetOSite; Q5T4S7; -.
DR PhosphoSitePlus; Q5T4S7; -.
DR SwissPalm; Q5T4S7; -.
DR BioMuta; UBR4; -.
DR DMDM; 74744979; -.
DR EPD; Q5T4S7; -.
DR jPOST; Q5T4S7; -.
DR MassIVE; Q5T4S7; -.
DR MaxQB; Q5T4S7; -.
DR PaxDb; Q5T4S7; -.
DR PeptideAtlas; Q5T4S7; -.
DR PRIDE; Q5T4S7; -.
DR ProteomicsDB; 64480; -. [Q5T4S7-1]
DR ProteomicsDB; 64481; -. [Q5T4S7-2]
DR ProteomicsDB; 64482; -. [Q5T4S7-3]
DR ProteomicsDB; 64483; -. [Q5T4S7-4]
DR ProteomicsDB; 64484; -. [Q5T4S7-5]
DR ProteomicsDB; 64485; -. [Q5T4S7-6]
DR Antibodypedia; 2856; 123 antibodies from 28 providers.
DR DNASU; 23352; -.
DR Ensembl; ENST00000375218.3; ENSP00000364366.3; ENSG00000127481.15. [Q5T4S7-6]
DR Ensembl; ENST00000375254.8; ENSP00000364403.3; ENSG00000127481.15. [Q5T4S7-1]
DR GeneID; 23352; -.
DR KEGG; hsa:23352; -.
DR MANE-Select; ENST00000375254.8; ENSP00000364403.3; NM_020765.3; NP_065816.2.
DR UCSC; uc001bbi.4; human. [Q5T4S7-1]
DR CTD; 23352; -.
DR DisGeNET; 23352; -.
DR GeneCards; UBR4; -.
DR HGNC; HGNC:30313; UBR4.
DR HPA; ENSG00000127481; Low tissue specificity.
DR MIM; 609890; gene.
DR neXtProt; NX_Q5T4S7; -.
DR OpenTargets; ENSG00000127481; -.
DR PharmGKB; PA162407958; -.
DR VEuPathDB; HostDB:ENSG00000127481; -.
DR eggNOG; KOG1776; Eukaryota.
DR GeneTree; ENSGT00600000084471; -.
DR HOGENOM; CLU_000069_0_0_1; -.
DR InParanoid; Q5T4S7; -.
DR OMA; NAEACMH; -.
DR OrthoDB; 717at2759; -.
DR PhylomeDB; Q5T4S7; -.
DR TreeFam; TF314406; -.
DR PathwayCommons; Q5T4S7; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q5T4S7; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23352; 647 hits in 1138 CRISPR screens.
DR ChiTaRS; UBR4; human.
DR GeneWiki; UBR4; -.
DR GenomeRNAi; 23352; -.
DR Pharos; Q5T4S7; Tbio.
DR PRO; PR:Q5T4S7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T4S7; protein.
DR Bgee; ENSG00000127481; Expressed in skin of leg and 101 other tissues.
DR ExpressionAtlas; Q5T4S7; baseline and differential.
DR Genevisible; Q5T4S7; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR025704; E3_Ub_ligase_UBR4_C.
DR InterPro; IPR045841; E3_UBR4_N.
DR InterPro; IPR045189; UBR4-like.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21725; PTHR21725; 1.
DR Pfam; PF13764; E3_UbLigase_R4; 1.
DR Pfam; PF19423; E3_UBR4_N; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calmodulin-binding; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Host-virus interaction; Membrane;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..5183
FT /note="E3 ubiquitin-protein ligase UBR4"
FT /id="PRO_0000286861"
FT TRANSMEM 850..870
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 993..1013
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 1656..1729
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1756..1778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2430..2469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2711..2764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2833..2967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3342..3385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..621
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2444..2469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2833..2891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2929..2949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2950..2967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3342..3365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3366..3385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AN08"
FT MOD_RES 370
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:A2AN08"
FT MOD_RES 905
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1084
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TL32"
FT MOD_RES 1647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1754
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TL32"
FT MOD_RES 1763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2715
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2719
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AN08"
FT MOD_RES 2724
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2AN08"
FT MOD_RES 2944
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2952
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..3585
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025200"
FT VAR_SEQ 2100
FT /note="K -> KQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_025201"
FT VAR_SEQ 2405..2486
FT /note="IGASVDPAGVTMIDAVKIYGKTKEQFGWPDEPPEEFPSASVSNICPSNLNQS
FT NGTGDSDSAAPTTTSGTVLERLVVSSLEAL -> SESPTPGADSVLIVTAKLGATGLWL
FT SNILGSLHSADFSVLSSGNFELHLMY (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_025202"
FT VAR_SEQ 2476
FT /note="E -> ESSETESLTKLD (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_025203"
FT VAR_SEQ 2487..5183
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_025204"
FT VAR_SEQ 2601
FT /note="T -> TDCFFPRCACWSLGIVGILIGAPLETPSP (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_025205"
FT VAR_SEQ 2830..2864
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_025206"
FT VAR_SEQ 3777..3797
FT /note="DDSGTAGGISSTSASVNRYIL -> VVPRCKGHLDKGLGLDQKTAS (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025207"
FT VAR_SEQ 3798..5183
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025208"
FT VAR_SEQ 5108
FT /note="K -> KKQTTPTVGGIDTGSLEPCVCE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025209"
FT VARIANT 1107
FT /note="T -> A (in dbSNP:rs16862578)"
FT /id="VAR_032193"
FT VARIANT 1394
FT /note="R -> H (in a breast cancer sample; somatic mutation;
FT dbSNP:rs756549939)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035540"
FT VARIANT 4867
FT /note="M -> L (in dbSNP:rs12584)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16247014, ECO:0000269|Ref.10"
FT /id="VAR_032194"
FT VARIANT 4924
FT /note="G -> R (in a melanoma patient)"
FT /evidence="ECO:0000269|PubMed:16247014"
FT /id="VAR_032195"
FT VARIANT 5084
FT /note="V -> M (in dbSNP:rs2274010)"
FT /id="VAR_032196"
FT CONFLICT 2016
FT /note="A -> S (in Ref. 1; AAL83880)"
FT /evidence="ECO:0000305"
FT CONFLICT 2410
FT /note="D -> E (in Ref. 1; AAL83880)"
FT /evidence="ECO:0000305"
FT CONFLICT 3957
FT /note="G -> S (in Ref. 1; AAL83880)"
FT /evidence="ECO:0000305"
FT CONFLICT 4589
FT /note="G -> V (in Ref. 7; AAH18694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5183 AA; 573841 MW; 5F6DD7B565E27609 CRC64;
MATSGGEEAA AAAPAPGTPA TGADTTPGWE VAVRPLLSAS YSAFEMKELP QLVASVIESE
SEILHHEKQY EPFYSSFVAL STHYITTVCS LIPRNQLQSV AAACKVLIEF SLLRLENPDE
ACAVSQKHLI LLIKGLCTGC SRLDRTEIIT FTAMMKSAKL PQTVKTLSDV EDQKELASPV
SPELRQKEVQ MNFLNQLTSV FNPRTVASQP ISTQTLVEGE NDEQSSTDQA SAIKTKNVFI
AQNVASLQEL GGSEKLLRVC LNLPYFLRYI NRFQDAVLAN SFFIMPATVA DATAVRNGFH
SLVIDVTMAL DTLSLPVLEP LNPSRLQDVT VLSLSCLYAG VSVATCMAIL HVGSAQQVRT
GSTSSKEDDY ESDAATIVQK CLEIYDMIGQ AISSSRRAGG EHYQNFQLLG AWCLLNSLFL
ILNLSPTALA DKGKEKDPLA ALRVRDILSR TKEGVGSPKL GPGKGHQGFG VLSVILANHA
IKLLTSLFQD LQVEALHKGW ETDGPPAALS IMAQSTSIQR IQRLIDSVPL MNLLLTLLST
SYRKACVLQR QRKGSMSSDA SASTDSNTYY EDDFSSTEED SSQDDDSEPI LGQWFEETIS
PSKEKAAPPP PPPPPPLESS PRVKSPSKQA PGEKGNILAS RKDPELFLGL ASNILNFITS
SMLNSRNNFI RNYLSVSLSE HHMATLASII KEVDKDGLKG SSDEEFAAAL YHFNHSLVTS
DLQSPNLQNT LLQQLGVAPF SEGPWPLYIH PQSLSVLSRL LLIWQHKASA QGDPDVPECL
KVWDRFLSTM KQNALQGVVP SETEDLNVEH LQMLLLIFHN FTETGRRAIL SLFVQIIQEL
SVNMDAQMRF VPLILARLLL IFDYLLHQYS KAPVYLFEQV QHNLLSPPFG WASGSQDSNS
RRATTPLYHG FKEVEENWSK HFSSDAVPHP RFYCVLSPEA SEDDLNRLDS VACDVLFSKL
VKYDELYAAL TALLAAGSQL DTVRRKENKN VTALEACALQ YYFLILWRIL GILPPSKTYI
NQLSMNSPEM SECDILHTLR WSSRLRISSY VNWIKDHLIK QGMKAEHASS LLELASTTKC
SSVKYDVEIV EEYFARQISS FCSIDCTTIL QLHEIPSLQS IYTLDAAISK VQVSLDEHFS
KMAAETDPHK SSEITKNLLP ATLQLIDTYA SFTRAYLLQN FNEEGTTEKP SKEKLQGFAA
VLAIGSSRCK ANTLGPTLVQ NLPSSVQTVC ESWNNINTNE FPNIGSWRNA FANDTIPSES
YISAVQAAHL GTLCSQSLPL AASLKHTLLS LVRLTGDLIV WSDEMNPPQV IRTLLPLLLE
SSTESVAEIS SNSLERILGP AESDEFLARV YEKLITGCYN ILANHADPNS GLDESILEEC
LQYLEKQLES SQARKAMEEF FSDSGELVQI MMATANENLS AKFCNRVLKF FTKLFQLTEK
SPNPSLLHLC GSLAQLACVE PVRLQAWLTR MTTSPPKDSD QLDVIQENRQ LLQLLTTYIV
RENSQVGEGV CAVLLGTLTP MATEMLANGD GTGFPELMVV MATLASAGQG AGHLQLHNAA
VDWLSRCKKY LSQKNVVEKL NANVMHGKHV MILECTCHIM SYLADVTNAL SQSNGQGPSH
LSVDGEERAI EVDSDWVEEL AVEEEDSQAE DSDEDSLCNK LCTFTITQKE FMNQHWYHCH
TCKMVDGVGV CTVCAKVCHK DHEISYAKYG SFFCDCGAKE DGSCLALVKR TPSSGMSSTM
KESAFQSEPR ISESLVRHAS TSSPADKAKV TISDGKVADE EKPKKSSLCR TVEGCREELQ
NQANFSFAPL VLDMLNFLMD AIQTNFQQAS AVGSSSRAQQ ALSELHTVEK AVEMTDQLMV
PTLGSQEGAF ENVRMNYSGD QGQTIRQLIS AHVLRRVAMC VLSSPHGRRQ HLAVSHEKGK
ITVLQLSALL KQADSSKRKL TLTRLASAPV PFTVLSLTGN PCKEDYLAVC GLKDCHVLTF
SSSGSVSDHL VLHPQLATGN FIIKAVWLPG SQTELAIVTA DFVKIYDLCV DALSPTFYFL
LPSSKIRDVT FLFNEEGKNI IVIMSSAGYI YTQLMEEASS AQQGPFYVTN VLEINHEDLK
DSNSQVAGGG VSVYYSHVLQ MLFFSYCQGK SFAATISRTT LEVLQLFPIN IKSSNGGSKT
SPALCQWSEV MNHPGLVCCV QQTTGVPLVV MVKPDTFLIQ EIKTLPAKAK IQDMVAIRHT
ACNEQQRTTM ILLCEDGSLR IYMANVENTS YWLQPSLQPS SVISIMKPVR KRKTATITTR
TSSQVTFPID FFEHNQQLTD VEFGGNDLLQ VYNAQQIKHR LNSTGMYVAN TKPGGFTIEI
SNNNSTMVMT GMRIQIGTQA IERAPSYIEI FGRTMQLNLS RSRWFDFPFT REEALQADKK
LNLFIGASVD PAGVTMIDAV KIYGKTKEQF GWPDEPPEEF PSASVSNICP SNLNQSNGTG
DSDSAAPTTT SGTVLERLVV SSLEALESCF AVGPIIEKER NKNAAQELAT LLLSLPAPAS
VQQQSKSLLA SLHTSRSAYH SHKDQALLSK AVQCLNTSSK EGKDLDPEVF QRLVITARSI
AIMRPNNLVH FTESKLPQME TEGMDEGKEP QKQLEGDCCS FITQLVNHFW KLHASKPKNA
FLAPACLPGL THIEATVNAL VDIIHGYCTC ELDCINTASK IYMQMLLCPD PAVSFSCKQA
LIRVLRPRNK RRHVTLPSSP RSNTPMGDKD DDDDDDADEK MQSSGIPNGG HIRQESQEQS
EVDHGDFEMV SESMVLETAE NVNNGNPSPL EALLAGAEGF PPMLDIPPDA DDETMVELAI
ALSLQQDQQG SSSSALGLQS LGLSGQAPSS SSLDAGTLSD TTASAPASDD EGSTAATDGS
TLRTSPADHG GSVGSESGGS AVDSVAGEHS VSGRSSAYGD ATAEGHPAGP GSVSSSTGAI
STTTGHQEGD GSEGEGEGET EGDVHTSNRL HMVRLMLLER LLQTLPQLRN VGGVRAIPYM
QVILMLTTDL DGEDEKDKGA LDNLLSQLIA ELGMDKKDVS KKNERSALNE VHLVVMRLLS
VFMSRTKSGS KSSICESSSL ISSATAAALL SSGAVDYCLH VLKSLLEYWK SQQNDEEPVA
TSQLLKPHTT SSPPDMSPFF LRQYVKGHAA DVFEAYTQLL TEMVLRLPYQ IKKITDTNSR
IPPPVFDHSW FYFLSEYLMI QQTPFVRRQV RKLLLFICGS KEKYRQLRDL HTLDSHVRGI
KKLLEEQGIF LRASVVTASS GSALQYDTLI SLMEHLKACA EIAAQRTINW QKFCIKDDSV
LYFLLQVSFL VDEGVSPVLL QLLSCALCGS KVLAALAASS GSSSASSSSA PVAASSGQAT
TQSKSSTKKS KKEEKEKEKD GETSGSQEDQ LCTALVNQLN KFADKETLIQ FLRCFLLESN
SSSVRWQAHC LTLHIYRNSS KSQQELLLDL MWSIWPELPA YGRKAAQFVD LLGYFSLKTP
QTEKKLKEYS QKAVEILRTQ NHILTNHPNS NIYNTLSGLV EFDGYYLESD PCLVCNNPEV
PFCYIKLSSI KVDTRYTTTQ QVVKLIGSHT ISKVTVKIGD LKRTKMVRTI NLYYNNRTVQ
AIVELKNKPA RWHKAKKVQL TPGQTEVKID LPLPIVASNL MIEFADFYEN YQASTETLQC
PRCSASVPAN PGVCGNCGEN VYQCHKCRSI NYDEKDPFLC NACGFCKYAR FDFMLYAKPC
CAVDPIENEE DRKKAVSNIN TLLDKADRVY HQLMGHRPQL ENLLCKVNEA APEKPQDDSG
TAGGISSTSA SVNRYILQLA QEYCGDCKNS FDELSKIIQK VFASRKELLE YDLQQREAAT
KSSRTSVQPT FTASQYRALS VLGCGHTSST KCYGCASAVT EHCITLLRAL ATNPALRHIL
VSQGLIRELF DYNLRRGAAA MREEVRQLMC LLTRDNPEAT QQMNDLIIGK VSTALKGHWA
NPDLASSLQY EMLLLTDSIS KEDSCWELRL RCALSLFLMA VNIKTPVVVE NITLMCLRIL
QKLIKPPAPT SKKNKDVPVE ALTTVKPYCN EIHAQAQLWL KRDPKASYDA WKKCLPIRGI
DGNGKAPSKS ELRHLYLTEK YVWRWKQFLS RRGKRTSPLD LKLGHNNWLR QVLFTPATQA
ARQAACTIVE ALATIPSRKQ QVLDLLTSYL DELSIAGECA AEYLALYQKL ITSAHWKVYL
AARGVLPYVG NLITKEIARL LALEEATLST DLQQGYALKS LTGLLSSFVE VESIKRHFKS
RLVGTVLNGY LCLRKLVVQR TKLIDETQDM LLEMLEDMTT GTESETKAFM AVCIETAKRY
NLDDYRTPVF IFERLCSIIY PEENEVTEFF VTLEKDPQQE DFLQGRMPGN PYSSNEPGIG
PLMRDIKNKI CQDCDLVALL EDDSGMELLV NNKIISLDLP VAEVYKKVWC TTNEGEPMRI
VYRMRGLLGD ATEEFIESLD STTDEEEDEE EVYKMAGVMA QCGGLECMLN RLAGIRDFKQ
GRHLLTVLLK LFSYCVKVKV NRQQLVKLEM NTLNVMLGTL NLALVAEQES KDSGGAAVAE
QVLSIMEIIL DESNAEPLSE DKGNLLLTGD KDQLVMLLDQ INSTFVRSNP SVLQGLLRII
PYLSFGEVEK MQILVERFKP YCNFDKYDED HSGDDKVFLD CFCKIAAGIK NNSNGHQLKD
LILQKGITQN ALDYMKKHIP SAKNLDADIW KKFLSRPALP FILRLLRGLA IQHPGTQVLI
GTDSIPNLHK LEQVSSDEGI GTLAENLLEA LREHPDVNKK IDAARRETRA EKKRMAMAMR
QKALGTLGMT TNEKGQVVTK TALLKQMEEL IEEPGLTCCI CREGYKFQPT KVLGIYTFTK
RVALEEMENK PRKQQGYSTV SHFNIVHYDC HLAAVRLARG REEWESAALQ NANTKCNGLL
PVWGPHVPES AFATCLARHN TYLQECTGQR EPTYQLNIHD IKLLFLRFAM EQSFSADTGG
GGRESNIHLI PYIIHTVLYV LNTTRATSRE EKNLQGFLEQ PKEKWVESAF EVDGPYYFTV
LALHILPPEQ WRATRVEILR RLLVTSQARA VAPGGATRLT DKAVKDYSAY RSSLLFWALV
DLIYNMFKKV PTSNTEGGWS CSLAEYIRHN DMPIYEAADK ALKTFQEEFM PVETFSEFLD
VAGLLSEITD PESFLKDLLN SVP
