UBR4_MOUSE
ID UBR4_MOUSE Reviewed; 5180 AA.
AC A2AN08; A2AN07; A2AN09; A2AN10; A2AN11; Q52KI4; Q6PB49; Q6PFC7; Q80Y11;
AC Q8BGB9; Q8C3E8; Q8C4W5; Q8C8X7; Q8CGE0; Q8CHF3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=E3 ubiquitin-protein ligase UBR4;
DE EC=2.3.2.27;
DE AltName: Full=N-recognin-4;
DE AltName: Full=RING-type E3 ubiquitin transferase UBR4;
DE AltName: Full=Zinc finger UBR1-type protein 1;
DE AltName: Full=p600;
GN Name=Ubr4; Synonyms=Kiaa0462, Zubr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-4461 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 2599-5180 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Head, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1290-3369 (ISOFORM 3).
RC TISSUE=Brain;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4020-5180.
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, Eye, and Mammary tumor;
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 FUNCTION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16055722; DOI=10.1128/mcb.25.16.7120-7136.2005;
RA Tasaki T., Mulder L.C.F., Iwamatsu A., Lee M.J., Davydov I.V.,
RA Varshavsky A., Muesing M., Kwon Y.T.;
RT "A family of mammalian E3 ubiquitin ligases that contain the UBR box motif
RT and recognize N-degrons.";
RL Mol. Cell. Biol. 25:7120-7136(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16081543; DOI=10.1073/pnas.0505322102;
RA DeMasi J., Huh K.-W., Nakatani Y., Muenger K., Howley P.M.;
RT "Bovine papillomavirus E7 transformation function correlates with cellular
RT p600 protein binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11486-11491(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181; SER-212;
RP TYR-370; SER-2719 AND THR-2721, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-2603 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:16055722}.
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. {ECO:0000250}.
CC -!- INTERACTION:
CC A2AN08; P06933: E7; Xeno; NbExp=2; IntAct=EBI-4285947, EBI-7730971;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Nucleus {ECO:0000250}. Note=Concentrates at the leading
CC edge of membrane structures involved in actin motility. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=A2AN08-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AN08-2; Sequence=VSP_025210;
CC Name=3;
CC IsoId=A2AN08-3; Sequence=VSP_025213, VSP_025215;
CC Name=4;
CC IsoId=A2AN08-4; Sequence=VSP_025211, VSP_025212;
CC Name=5;
CC IsoId=A2AN08-5; Sequence=VSP_025214;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult and embryonic stages with
CC highest levels in testis and brain. {ECO:0000269|PubMed:16055722}.
CC -!- SIMILARITY: Belongs to the UBR4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39609.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK044277; BAC31850.1; -; mRNA.
DR EMBL; AK080556; BAC37944.1; -; mRNA.
DR EMBL; AK082231; BAC38442.2; ALT_SEQ; mRNA.
DR EMBL; AK083644; BAC38980.2; ALT_SEQ; mRNA.
DR EMBL; AK086097; BAC39609.1; ALT_INIT; mRNA.
DR EMBL; AL807833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB093242; BAC41426.2; -; mRNA.
DR EMBL; BC040468; AAH40468.1; -; mRNA.
DR EMBL; BC051096; AAH51096.1; -; mRNA.
DR EMBL; BC057625; AAH57625.1; -; mRNA.
DR EMBL; BC059890; AAH59890.1; -; mRNA.
DR EMBL; BC094329; AAH94329.1; -; mRNA.
DR CCDS; CCDS51340.1; -. [A2AN08-1]
DR RefSeq; NP_001153791.1; NM_001160319.1. [A2AN08-1]
DR BioGRID; 213238; 33.
DR DIP; DIP-61499N; -.
DR IntAct; A2AN08; 13.
DR MINT; A2AN08; -.
DR STRING; 10090.ENSMUSP00000095433; -.
DR iPTMnet; A2AN08; -.
DR PhosphoSitePlus; A2AN08; -.
DR SwissPalm; A2AN08; -.
DR EPD; A2AN08; -.
DR jPOST; A2AN08; -.
DR MaxQB; A2AN08; -.
DR PaxDb; A2AN08; -.
DR PeptideAtlas; A2AN08; -.
DR PRIDE; A2AN08; -.
DR ProteomicsDB; 298371; -. [A2AN08-1]
DR ProteomicsDB; 298372; -. [A2AN08-2]
DR ProteomicsDB; 298373; -. [A2AN08-3]
DR ProteomicsDB; 298374; -. [A2AN08-4]
DR ProteomicsDB; 298375; -. [A2AN08-5]
DR Antibodypedia; 2856; 123 antibodies from 28 providers.
DR Ensembl; ENSMUST00000097822; ENSMUSP00000095433; ENSMUSG00000066036. [A2AN08-1]
DR Ensembl; ENSMUST00000165860; ENSMUSP00000125800; ENSMUSG00000066036. [A2AN08-3]
DR GeneID; 69116; -.
DR KEGG; mmu:69116; -.
DR UCSC; uc008vmj.2; mouse. [A2AN08-4]
DR UCSC; uc008vmm.2; mouse. [A2AN08-1]
DR CTD; 23352; -.
DR MGI; MGI:1916366; Ubr4.
DR VEuPathDB; HostDB:ENSMUSG00000066036; -.
DR eggNOG; KOG1776; Eukaryota.
DR GeneTree; ENSGT00600000084471; -.
DR HOGENOM; CLU_000069_0_0_1; -.
DR InParanoid; A2AN08; -.
DR OMA; NAEACMH; -.
DR OrthoDB; 717at2759; -.
DR PhylomeDB; A2AN08; -.
DR TreeFam; TF314406; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 69116; 24 hits in 76 CRISPR screens.
DR ChiTaRS; Ubr4; mouse.
DR PRO; PR:A2AN08; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AN08; protein.
DR Bgee; ENSMUSG00000066036; Expressed in entorhinal cortex and 270 other tissues.
DR ExpressionAtlas; A2AN08; baseline and differential.
DR Genevisible; A2AN08; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS: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; ISS: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; 1.
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; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..5180
FT /note="E3 ubiquitin-protein ligase UBR4"
FT /id="PRO_0000286862"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 1655..1728
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 205..228
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..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2429..2466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2708..2761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2830..2963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3344..3383
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 2443..2466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2830..2888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2926..2945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2947..2963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3344..3362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3363..3382
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:21183079"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 370
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 905
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 1083
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 1401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TL32"
FT MOD_RES 1646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 1651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 1746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 1753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TL32"
FT MOD_RES 1876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 1902
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 2712
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 2716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 2719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2721
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2941
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 2949
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT VAR_SEQ 1..3159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025210"
FT VAR_SEQ 466..474
FT /note="HQGFGVLSV -> CVSACKLHF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025211"
FT VAR_SEQ 475..5180
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025212"
FT VAR_SEQ 2474
FT /note="E -> ESSETESLTKLD (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_025213"
FT VAR_SEQ 2599
FT /note="T -> TDCFSPRCACWNLGIVGILIGAPLETPSA (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_025214"
FT VAR_SEQ 2827..2861
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_025215"
FT CONFLICT 445
FT /note="R -> K (in Ref. 1; BAC39609)"
FT /evidence="ECO:0000305"
FT MOD_RES A2AN08-5:2603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 5180 AA; 572290 MW; 5F4238194DF88EE0 CRC64;
MATSGGEEAA AAAPAPGAPA TGQDTTPGWE VAVRPLLSAS YSAFEMKELP QLVASVIESE
SEILHHEKQY EPFYSSFVAL STHYITTVCS LIPRNQLQSV AAACKVLIEF SLLRLENPDE
ACAVSQKHLI LLIKGLCTGC SRLDRTEIIT FTAMMKSAKL PQTVKTLSDV EDQKELASPV
SPELRQKEVQ MNFLNQLTSV FNPRTVPSPP ISPQALVEGE NDEQSSPDQV SAAKTKSVFI
AQNVASLQEL GGSEKLLRVC LNLPYFLRYI NRFQDAVVAN SFFIMPATVA DATAVRNGFH
SLVIDVTMAL DTLSLPVLEP LNPSRLQDVT VLSLSCLYAG VSVATCMAIL HVGSAQQVRT
GSTSSKEDDY ESDAATIVQK CLEIYDMIGQ AISSSRRAGG EHFQNFQLLG AWCLLNSLFL
ILNLSPTALA DKGKEKDPLA ALRVRDILSR TKEGVGSPKL GPGKGHQGFG VLSVILANHA
IKLLASLFQD LQVEALHKGW ETDGPPAVLS IMAQSTSTQR IQRLIDSVPL TNLLLTLLST
SYRKACVLQR QRKGSMSSDA SASTDSNTYY EDDFSSTEED SSQDDDSEPI LGQWFEETIS
PSKEKAAPPP PPPPPPLESS PRVKSPNKQA SGEKGNILAS RKDPELFSGL ASNILNFITT
SMLNSRNSFI RSYLSASLSE HHMATLASII KEVDKDGLKG SSDEDFAAAL YHFNHSLVTS
DLQSPNLQNT LLQQLGVAPF SEGPWPLYIH PQGLSVLSRL LLIWQHKAGA QGDPDVPECL
KVWDRFLTTM KQNALQGVVP SETEDLNVEH LQLLLLIFHS FSEKGRRAIL TMLVQSIQEL
SVNMEVQMRT APLILARLLL IFDYLLHQYS KAPVYLFEQV QHNLLSPPFG WASGSQDSSS
RRANTPLYHG FKEVEENWSK HFSSDAAPQP RFYCVLSTEA SEEDLNRLDS EACEVLFSKP
VKYDELYSSL TTLLAAGSQL DTTRRKEKKN VTALEACALQ YYFLILWRIL GILPPSKTYM
NQLAMNSPEM SECDILHTLR WSSRLRISSY VSWIKDHLIK QGMKPEHAGS LIELAASKCS
SVKYDVEIVE EYFARQISSF CSIDCTAVLQ LHEIPSLQSI YTLDAAVSKV QVSLDEHFSK
MAAETDPHKS SEITKNLLPA TLQLIDTYAS FTRAYLLQNL NEEGSTEKPS QEKLHGFAAV
LAIGSSRCKA NTLGPTLVQN LPSSVQSVCE SWNNINTNEF PNIGSWRNAF ANDTIPSESY
ISAVQAAHLG TLCGQSLPLA ASLKHTLLSL VRLTGDLIVW SDEMNPAQVI RTLLPLLLES
STESAAEISS NSLERILGPA ESDEFLARVY EKLITGCYNI LANHADPNSG LDESILEECL
QYLEKQLESS QARKAMEEFF SDGGELVQIM MATANEDLSA KFCNRVLKFF TKLFQLTEKS
PNPSLLHLCG SLAQLACVEP VRLQAWLTRM TTSPPKDSDQ LEVIQENRQL LQLLTTYIVR
ENSQVGEGVC AVLLGTLTPM ATDMLANGDG TGFPELMVVM ATLASAGQGA GHLQLHNAAV
DWLGRCKKYL SQKNVVEKLN ANVMHGKHVM VLECTCHIMS YLADVTNALS QSNGQGPSHL
SVDGEERAIE VDSDWVEELA VEEEDSQAED SDEDSLCNKL CTFTITQKEF MNQHWYHCHT
CKMVDGVGVC TVCAKVCHKD HEISYAKYGS FFCDCGAKED GSCLALVKRT PSSGMSSTMK
ESAFQSEPRV SESLVRHAST SPADKAKVTI SDGKVTDEEK PKKSSLCRTV EGCREELQNQ
ANFSFAPLVL DMLSFLMDAI QTNFQQASAV GSSSRAQQAL SELHTVDKGV EMTDQLMVPT
LGSQEGAFEN VRMNYSGDQG QTIRQLISAH VLRRVAMCVL SSPHGRRQHL AVSHEKGKIT
VLQLSALLKQ ADSSKRKLTL TRLASAPVPF TVLSLTGNPC KEDYLAVCGL KDCHVLTFSS
SGSVSDHLVL HPQLATGNFI IKAVWLPGSQ TELAIVTADF VKIYDLSIDA LSPTFYFLLP
SSKIRDVTFL FNEEGKNIIV IMSSAGYMYT QLMEEASSAQ QGPFYVTNVL EINHEDLKDS
NSQVAGGGVS VYYSHVLQML FFSYSQGRSF AATVSRSTLE VLQLFPINIK SSNGGSKTSP
ALCQWSEVMN HPGLVCCVQQ TTGVPLVVMV KPGTFLIQEI KTLPAKAKIQ DMVAIRHTAC
NEQQRTTMIL LCEDGSLRIY MANVENTSYW LQPSLQPSSV ISIMKPVRKR KTATITARTS
SQVTFPIDFF EHNQQLTDVE FGGNDLLQVY NAQQIKHRLN STGMYVANTK PGGFTIEISN
NSSTMVMTGM RIQIGTQAIE RAPSYIEIFG RTMQLNLSRS RWFDFPFTRE EALQADRKLS
LFIGASVDPA GVTMIDAVKI YGKTKEQFGW PDEPPEDFPS ASVSNICPPN LNQSNGTGES
DSAAPATTSG TVLERLVVSS LEALESCFAV GPIIEKERNK HAAQELATLL LSLPAPASVQ
QQSKSLLASL HSSRSAYHSH KDQALLSKAV QCLNTSSKEG KDLDPEVFQR LVITARSIAV
TRPNNLVHFT ESKLPQMETE GADEGKEPQK QEGDGCSFIT QLVNHFWKLH ASKPKNAFLA
PACLPGLTHI EATVNALVDI IHGYCTCELD CINTASKIYM QMLLCPDPAV SFSCKQALIR
VLRPRNKRRH VTLPSSPRSN TPMGDKDDDD DDDADEKMQS SGIPDGGHIR QESQEQSEVD
HGDFEMVSES MVLETAENVN NGNPSPLEAL LAGAEGFPPM LDIPPDADDE TMVELAIALS
LQQDQQGSSS SALGLQSLGL SGQAPSSSSL DAGTLSDTTA SAPASDDEGS TAATDGSTLR
TSPADHGGSV GSESGGSAVD SVAGEHSVSG RSSAYGDATA EGHPAGPGSV SSSTGAISTA
TGHQEGDGSE GEGEGEAEGD VHTSNRLHMV RLMLLERLLQ TLPQLRNVGG VRAIPYMQVI
LMLTTDLDGE DEKDKGALDN LLAQLIAELG MDKKDVSKKN ERSALNEVHL VVMRLLSVFM
SRTKSGSKSS ICESSSLISS ATAAALLSSG AVDYCLHVLK SLLEYWKSQQ SDEEPVAASQ
LLKPHTTSSP PDMSPFFLRQ YVKGHAADVF EAYTQLLTEM VLRLPYQIKK IADTSSRIPP
PVFDHSWFYF LSEYLMIQQT PFVRRQVRKL LLFICGSKEK YRQLRDLHTL DSHVRGIKKL
LEEQGIFLRA SVVTASSGSA LQYDTLISLM EHLKACAEIA AQRTINWQKF CIKDDSVLYF
LLQVSFLVDE GVSPVLLQLL SCALCGSKVL AALAASTGSS SVASSSAPPA ASSGQATTQS
KSSTKKSKKE EKEKEKEGES SGSQEDQLCT ALVNQLNRFA DKETLIQFLR CFLLESNSSS
VRWQAHCLTL HIYRNSNKAQ QELLLDLMWS IWPELPAYGR KAAQFVDLLG YFSLKTAQTE
KKLKEYSQKA VEILRTQNHI LTNHPNSNIY NTLSGLVEFD GYYLESDPCL VCNNPEVPFC
YIKLSSIKVD TRYTTTQQVV KLIGSHTISK VTVKIGDLKR TKMVRTINLY YNNRTVQAIV
ELKNKPARWH KAKKVQLTPG QTEVKIDLPL PIVASNLMIE FADFYENYQA STETLQCPRC
SASVPANPGV CGNCGENVYQ CHKCRSINYD EKDPFLCNAC GFCKYARFDF MLYAKPCCAV
DPIENEEDRK KAVSNINTLL DKADRVYHQL MGHRPQLENL LCKVNEAAPE KPQEDSGTAG
GISSTSASVN RYILQLAQEY CGDCKNSFDE LSKIIQKVFA SRKELLEYDL QQREAATKSS
RTSVQPTFTA SQYRALSVLG CGHTSSTKCY GCASAVTEHC ITLLRALATN PALRHILVSQ
GLIRELFDYN LRRGAAAIRE EVRQLMCLLT RDNPEATQQM NDLIIGKVST ALKGHWANPD
LASSLQYEML LLTDSISKED SCWELRLRCA LSLFLMAVNI KTPVVVENIT LMCLRILQKL
IKPPAPTSKK NKDVPVEALT TVKPYCNEIH AQAQLWLKRD PKASYEAWKK CLPIRGVDGN
GKSPSKSELH RLYLTEKYVW RWKQFLSRRG KRTTPLDLKL GHNNWLRQVL FTPATQAARQ
AACTIVEALA TVPSRKQQVL DLLTSYLDEL SVAGECAAEY LALYQKLIAS CHWKVYLAAR
GVLPYVGNLI TKEIARLLAL EEATLSTDLQ QGYALKSLTG LLSSFVEVES IKRHFKSRLV
GTVLNGYLCL RKLVLQRTKL IDETQDMLLE MLEDMTTGTE SETKAFMAVC IETAKRYNLD
DYRTPVFIFE RLCSIIYPEE NEVTEFFVTL EKDPQQEDFL QGRMPGNPYS SNEPGIGPLM
RDIKNKICQD CDLVALLEDD SGMELLVNNK IISLDLPVAE VYKKVWCATN EGEPMRIVYR
MRGLLGDATE EFIESLDSTT DEEEDEEEVY RMAGVMAQCG GLQCMLNRLA GVKDFKQGRH
LLTVLLKLFS YCVKVKVNRQ QLVKLETNTL NVMLGTLNLA LVAEQESKDS GGAAVAEQVL
SIMEIILDES NAEPLSEDKG NLLLTGDKDQ LVMLLDQINS TFVRSNPSVL QGLLRIIPYL
SFGEVEKMQI LVERFKPYCS FEKYDEDHSG DDKVFLDCFC KIAAGIKNNS NGHQLKDLIL
QKGITQNALD YMKKHIPSAK NLDADIWKKF LSRPALPFIL RLLRGLAMQH PATQVLIGTD
SITSLHKLEQ VSSDEGIGTL AENLLEALRE HPDVNKKIDA ARRETRAEKK RMAMAMRQKA
LGTLGMTTNE KGQVVTKTAL LKQMEELIEE PGLTCCICRE GYKFQPTKVL GIYTFTKRVA
LEEMENKPRK QQGYSTVSHF NIVHYDCHLA AVRLARGREE WESAALQNAN TKCNGLLPVW
GPHVPESAFA TCLARHNTYL QECTGQREPT YQLNIHDIKL LFLRFAMEQS FSADTGGGGR
ESNIHLIPYI IHTVLYVLNT TRATSREEKN LQGFLEQPKE KWTESAFDVD GPHYFTILAL
HVLPPEQWKA IRVEILRRLL VASHARAVAP GGATRLTDKA VKDYSAYRSS LLFWALVDLI
YNMFKKVPTS NTEGGWSCSL AEYIRHNDMP IYEAADKALK TFQEEFMPVE TFSEFLDAAG
LLSEITDPES FLKDLLNSVP
