NEB1_HUMAN
ID NEB1_HUMAN Reviewed; 1098 AA.
AC Q9ULJ8; A1L494; B2RWQ1; E9PCA0; E9PCK6; E9PDX1; F8W7J9; O76059; Q9NXT2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Neurabin-1;
DE AltName: Full=Neurabin-I;
DE AltName: Full=Neural tissue-specific F-actin-binding protein I;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 9A;
GN Name=PPP1R9A; Synonyms=KIAA1222;
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] (ISOFORM 2).
RC TISSUE=Colon;
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP VAL-331.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 357-1098 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION BY
RP 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-840, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-840, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [9]
RP STRUCTURE BY NMR OF 500-593.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domain of spinophilin/neurabinII protein.";
RL Submitted (JUN-2005) to the PDB data bank.
CC -!- FUNCTION: Binds to actin filaments (F-actin) and shows cross-linking
CC activity. Binds along the sides of the F-actin. May be involved in
CC neurite formation. Inhibits protein phosphatase 1-alpha activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Possibly exists as a homodimer, homotrimer or a homotetramer.
CC Interacts with F-actin, protein phosphatase 1 (PP1), neurabin-2 and
CC p70-S6K (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9ULJ8; P41220: RGS2; NbExp=3; IntAct=EBI-2515561, EBI-712388;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Synapse,
CC synaptosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Long;
CC IsoId=Q9ULJ8-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q9ULJ8-2; Sequence=VSP_011139, VSP_005121;
CC Name=3;
CC IsoId=Q9ULJ8-3; Sequence=VSP_044469, VSP_044470, VSP_005121;
CC Name=4;
CC IsoId=Q9ULJ8-4; Sequence=VSP_044471;
CC Name=5;
CC IsoId=Q9ULJ8-5; Sequence=VSP_053808, VSP_005121;
CC -!- DOMAIN: Interacts with p70-S6K via its PDZ domain. {ECO:0000250}.
CC -!- DOMAIN: The PP1 binding region is natively unstructured, upon PP1
CC binding, it acquires structure, blocks a substrate-binding site, and
CC restricts PP1 phosphatase specificity to a subset of substrates.
CC {ECO:0000250}.
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DR EMBL; AK000075; BAA90928.1; -; mRNA.
DR EMBL; AC002429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004022; AAC35294.2; -; Genomic_DNA.
DR EMBL; AC073886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130449; AAI30450.1; -; mRNA.
DR EMBL; BC150636; AAI50637.1; -; mRNA.
DR EMBL; AB033048; BAA86536.1; -; mRNA.
DR CCDS; CCDS34683.1; -. [Q9ULJ8-1]
DR CCDS; CCDS55127.1; -. [Q9ULJ8-3]
DR CCDS; CCDS55128.1; -. [Q9ULJ8-4]
DR CCDS; CCDS55129.1; -. [Q9ULJ8-5]
DR RefSeq; NP_001159632.1; NM_001166160.1. [Q9ULJ8-3]
DR RefSeq; NP_001159633.1; NM_001166161.1. [Q9ULJ8-5]
DR RefSeq; NP_001159634.1; NM_001166162.1. [Q9ULJ8-4]
DR RefSeq; NP_001159635.1; NM_001166163.1.
DR RefSeq; NP_060120.2; NM_017650.2. [Q9ULJ8-1]
DR RefSeq; XP_016867892.1; XM_017012403.1. [Q9ULJ8-5]
DR RefSeq; XP_016867894.1; XM_017012405.1. [Q9ULJ8-1]
DR RefSeq; XP_016867895.1; XM_017012406.1. [Q9ULJ8-1]
DR PDB; 1WF8; NMR; -; A=500-593.
DR PDBsum; 1WF8; -.
DR AlphaFoldDB; Q9ULJ8; -.
DR BMRB; Q9ULJ8; -.
DR SMR; Q9ULJ8; -.
DR BioGRID; 120747; 112.
DR IntAct; Q9ULJ8; 40.
DR MINT; Q9ULJ8; -.
DR iPTMnet; Q9ULJ8; -.
DR PhosphoSitePlus; Q9ULJ8; -.
DR BioMuta; PPP1R9A; -.
DR DMDM; 50403806; -.
DR EPD; Q9ULJ8; -.
DR jPOST; Q9ULJ8; -.
DR MassIVE; Q9ULJ8; -.
DR MaxQB; Q9ULJ8; -.
DR PaxDb; Q9ULJ8; -.
DR PeptideAtlas; Q9ULJ8; -.
DR PRIDE; Q9ULJ8; -.
DR ProteomicsDB; 19462; -.
DR ProteomicsDB; 19765; -.
DR ProteomicsDB; 29959; -.
DR ProteomicsDB; 85051; -. [Q9ULJ8-1]
DR ProteomicsDB; 85052; -. [Q9ULJ8-2]
DR Antibodypedia; 4361; 149 antibodies from 27 providers.
DR DNASU; 55607; -.
DR Ensembl; ENST00000289495.7; ENSP00000289495.7; ENSG00000158528.12. [Q9ULJ8-5]
DR Ensembl; ENST00000340694.8; ENSP00000344524.4; ENSG00000158528.12. [Q9ULJ8-1]
DR Ensembl; ENST00000424654.5; ENSP00000411342.1; ENSG00000158528.12. [Q9ULJ8-4]
DR Ensembl; ENST00000433360.6; ENSP00000405514.1; ENSG00000158528.12. [Q9ULJ8-3]
DR Ensembl; ENST00000433881.5; ENSP00000398870.1; ENSG00000158528.12. [Q9ULJ8-1]
DR Ensembl; ENST00000456331.6; ENSP00000402893.2; ENSG00000158528.12. [Q9ULJ8-4]
DR GeneID; 55607; -.
DR KEGG; hsa:55607; -.
DR MANE-Select; ENST00000433360.6; ENSP00000405514.1; NM_001166160.2; NP_001159632.1. [Q9ULJ8-3]
DR UCSC; uc003unp.5; human. [Q9ULJ8-1]
DR CTD; 55607; -.
DR DisGeNET; 55607; -.
DR GeneCards; PPP1R9A; -.
DR HGNC; HGNC:14946; PPP1R9A.
DR HPA; ENSG00000158528; Tissue enhanced (brain).
DR MIM; 602468; gene.
DR neXtProt; NX_Q9ULJ8; -.
DR OpenTargets; ENSG00000158528; -.
DR PharmGKB; PA33661; -.
DR VEuPathDB; HostDB:ENSG00000158528; -.
DR eggNOG; KOG1945; Eukaryota.
DR GeneTree; ENSGT00940000155538; -.
DR HOGENOM; CLU_007401_0_0_1; -.
DR InParanoid; Q9ULJ8; -.
DR OMA; XLNEAVP; -.
DR OrthoDB; 128743at2759; -.
DR PhylomeDB; Q9ULJ8; -.
DR TreeFam; TF105540; -.
DR PathwayCommons; Q9ULJ8; -.
DR SignaLink; Q9ULJ8; -.
DR BioGRID-ORCS; 55607; 8 hits in 1068 CRISPR screens.
DR ChiTaRS; PPP1R9A; human.
DR EvolutionaryTrace; Q9ULJ8; -.
DR GeneWiki; PPP1R9A; -.
DR GenomeRNAi; 55607; -.
DR Pharos; Q9ULJ8; Tbio.
DR PRO; PR:Q9ULJ8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9ULJ8; protein.
DR Bgee; ENSG00000158528; Expressed in Brodmann (1909) area 23 and 186 other tissues.
DR ExpressionAtlas; Q9ULJ8; baseline and differential.
DR Genevisible; Q9ULJ8; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR029994; Neurabin-1.
DR InterPro; IPR040645; Neurabin-1/2_PDZ.
DR InterPro; IPR043446; Neurabin-like.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR16154; PTHR16154; 1.
DR PANTHER; PTHR16154:SF22; PTHR16154:SF22; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17817; PDZ_5; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Neurogenesis;
KW Phosphoprotein; Reference proteome; Synapse; Synaptosome.
FT CHAIN 1..1098
FT /note="Neurabin-1"
FT /id="PRO_0000071507"
FT DOMAIN 504..592
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 988..1051
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..144
FT /note="Actin-binding"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..502
FT /note="Interaction with protein phosphatase 1"
FT /evidence="ECO:0000250"
FT REGION 597..1090
FT /note="Interaction with TGN38"
FT /evidence="ECO:0000250"
FT REGION 627..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 597..627
FT /evidence="ECO:0000255"
FT COILED 670..824
FT /evidence="ECO:0000255"
FT COILED 1033..1090
FT /evidence="ECO:0000255"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..645
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35867"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35867"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35867"
FT MOD_RES 460
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O35867"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35867"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35867"
FT MOD_RES 956
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35867"
FT MOD_RES 957
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35867"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35867"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35867"
FT VAR_SEQ 1..918
FT /note="MLKTESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKSDGEQKTKEGEGSQ
FT QSRGRKYGSNVNRIKNLFMQMGMEPNENAAVIAKTRGKGGHSSPQRRMKPKEFLEKTDG
FT SVVKLESSVSERISRFDTMYDGPSYSKFTETRKMFERSVHESGQNNRYSPKKEKAGGSE
FT PQDEWGGSKSNRGSTDSLDSLSSRTEAVSPTVSQLSAVFENTDSPSAIISEKAENNEYS
FT VTGHYPLNLPSVTVTNLDTFGHLKDSNSWPPSNKRGVDTEDAHKSNATPVPEVASKSTS
FT LASIPGEEIQQSKEPEDSTSNQQTPDSIDKDGPEEPCAESKAMPKSEIPSPQSQLLEDA
FT EANLVGREAAKQQRKELAGGDFTSPDASASSCGKEVPEDSNNFDGSHVYMHSDYNVYRV
FT RSRYNSDWGETGTEQDEEEDSDENSYYQPDMEYSEIVGLPEEEEIPANRKIKFSSAPIK
FT VFNTYSNEDYDRRNDEVDPVAASAEYELEKRVEKLELFPVELEKDEDGLGISIIGMGVG
FT ADAGLEKLGIFVKTVTEGGAAQRDGRIQVNDQIVEVDGISLVGVTQNFAATVLRNTKGN
FT VRFVIGREKPGQVSEVAQLISQTLEQERRQRELLEQHYAQYDADDDETGEYATDEEEDE
FT VGPVLPGSDMAIEVFELPENEDMFSPSELDTSKLSHKFKELQIKHAVTEAEIQKLKTKL
FT QAAENEKVRWELEKTQLQQNIEENKERMLKLESYWIEAQTLCHTVNEHLKETQSQYQAL
FT EKKYNKAKKLIKDFQQKELDFIKRQEAERKKIEDLEKAHLVEVQGLQVRIRDLEAEVFR
FT LLKQNGTQVNNNNNIFERRTSLGEVSKGDTMENLDGKQTSCQDGLSQDLNEAVPETERL
FT DSKALKTRAQLSVKNRRQRPSRTRLYDSVSSTDGEDSLER -> MHITKLLPPKGLRTS
FT SPESDSGVPPLTPVDSNVPFSSDHIAEFQEEPLDPEMGPLSSMWGDTSLFSTSKSDHDV
FT EESPCHHQTTNKKILREKDDAKDPKSLRASSSLAVQGGKIKRKFVDLGAPLRRNSSKGK
FT KWKEKEKEASRFSAGSRIFRGRLENWTPKPCSTAQTSTRSPCMPFSWFNDSRKGSYSFR
FT NLPAPTSSLQPSPETLISDKKGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011139"
FT VAR_SEQ 630
FT /note="E -> ENTVAELQGMSGNCNNNNNYFLK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044469"
FT VAR_SEQ 919
FT /note="K -> KPSNSFYNHMHITKLLPPKGLRTSSPESDSGVPPLTPVDSNVPFSSD
FT HIAEFQEEPLDPEMGPLSSMWGDTSLFSTSKSDHDVEESPCHHQTTNKKILREKDDAKD
FT PKSLRASSSLAVQGGKIKRKFVDLGAPLRRNSSKGKKWKEKEKEASRFSAGSRIFRGRL
FT ENWTPKPCSTAQTSTRSPCMPFSWFNDSRKGSYSFRNLPAPTSSLQPSPETLISDKKGS
FT KVENTWITKANKRNPNPSSSSIFGRHSQLMSVVWIQETN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044470"
FT VAR_SEQ 919
FT /note="K -> KGLRTSSPESDSGVPPLTPVDSNVPFSSDHIAEFQEEPLDPEMGPLS
FT SMWGDTSLFSTSKSDHDVEESPCHHQTTNKKILREKDDAKDPKSLRASSSLAVQGGKIK
FT RKFVDLGAPLRRNSSKGKKWKEKEKEASRFSAGSRIFRGRLENWTPKPCSTAQTSTRSP
FT CMPFSWFNDSRKGSYSFRNLPAPTSSLQPSPETLISDKKGSK (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_053808"
FT VAR_SEQ 920..1028
FT /note="NFTFNDDFSPSSTSSADLSGLGAEPKTPGLSQSLALSSDESLDMIDDEILDD
FT GQSPKHSQCQNRAVQEWSVQQVSHWLMSLNLEQYVSEFSAQNITGEQLLQLDGNKLK
FT -> PSNSFYNHMHITKLLPPKGLRTSSPESDSGVPPLTPVDSNVPFSSDHIAEFQEEPL
FT DPEMGPLSSMWGDTSLFSTSKSDHDVEESPCHHQTTNKKILREKDDAKDPKSLRASSSL
FT AVQGGKIKRKFVDLGAPLRRNSSKGKKWKEKEKEASRFSAGSRIFRGRLENWTPKPCST
FT AQTSTRSPCMPFSWFNDSRKGSYSFRNLPAPTSSLQPSPETLISDKKGSKNFTFNDDFS
FT PSSTSSADLSGLGAEPKTPGLSQSLALSSDE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044471"
FT VAR_SEQ 960..967
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_005121"
FT VARIANT 331
FT /note="M -> V (in dbSNP:rs10230714)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051746"
FT CONFLICT 379
FT /note="C -> S (in Ref. 3; AAI50637)"
FT /evidence="ECO:0000305"
FT CONFLICT 952
FT /note="S -> P (in Ref. 1; BAA90928)"
FT /evidence="ECO:0000305"
FT STRAND 500..508
FT /evidence="ECO:0007829|PDB:1WF8"
FT STRAND 516..524
FT /evidence="ECO:0007829|PDB:1WF8"
FT STRAND 531..539
FT /evidence="ECO:0007829|PDB:1WF8"
FT HELIX 544..548
FT /evidence="ECO:0007829|PDB:1WF8"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:1WF8"
FT HELIX 570..579
FT /evidence="ECO:0007829|PDB:1WF8"
FT STRAND 582..591
FT /evidence="ECO:0007829|PDB:1WF8"
FT CONFLICT Q9ULJ8-3:1039
FT /note="R -> Q (in Ref. 3; AAI50637)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9ULJ8-4:1017
FT /note="R -> Q (in Ref. 3; AAI30450)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9ULJ8-4:1057
FT /note="S -> N (in Ref. 3; AAI30450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1098 AA; 123342 MW; 998FD9821C422891 CRC64;
MLKTESSGER TTLRSASPHR NAYRTEFQAL KSTFDKPKSD GEQKTKEGEG SQQSRGRKYG
SNVNRIKNLF MQMGMEPNEN AAVIAKTRGK GGHSSPQRRM KPKEFLEKTD GSVVKLESSV
SERISRFDTM YDGPSYSKFT ETRKMFERSV HESGQNNRYS PKKEKAGGSE PQDEWGGSKS
NRGSTDSLDS LSSRTEAVSP TVSQLSAVFE NTDSPSAIIS EKAENNEYSV TGHYPLNLPS
VTVTNLDTFG HLKDSNSWPP SNKRGVDTED AHKSNATPVP EVASKSTSLA SIPGEEIQQS
KEPEDSTSNQ QTPDSIDKDG PEEPCAESKA MPKSEIPSPQ SQLLEDAEAN LVGREAAKQQ
RKELAGGDFT SPDASASSCG KEVPEDSNNF DGSHVYMHSD YNVYRVRSRY NSDWGETGTE
QDEEEDSDEN SYYQPDMEYS EIVGLPEEEE IPANRKIKFS SAPIKVFNTY SNEDYDRRND
EVDPVAASAE YELEKRVEKL ELFPVELEKD EDGLGISIIG MGVGADAGLE KLGIFVKTVT
EGGAAQRDGR IQVNDQIVEV DGISLVGVTQ NFAATVLRNT KGNVRFVIGR EKPGQVSEVA
QLISQTLEQE RRQRELLEQH YAQYDADDDE TGEYATDEEE DEVGPVLPGS DMAIEVFELP
ENEDMFSPSE LDTSKLSHKF KELQIKHAVT EAEIQKLKTK LQAAENEKVR WELEKTQLQQ
NIEENKERML KLESYWIEAQ TLCHTVNEHL KETQSQYQAL EKKYNKAKKL IKDFQQKELD
FIKRQEAERK KIEDLEKAHL VEVQGLQVRI RDLEAEVFRL LKQNGTQVNN NNNIFERRTS
LGEVSKGDTM ENLDGKQTSC QDGLSQDLNE AVPETERLDS KALKTRAQLS VKNRRQRPSR
TRLYDSVSST DGEDSLERKN FTFNDDFSPS STSSADLSGL GAEPKTPGLS QSLALSSDES
LDMIDDEILD DGQSPKHSQC QNRAVQEWSV QQVSHWLMSL NLEQYVSEFS AQNITGEQLL
QLDGNKLKAL GMTASQDRAV VKKKLKEMKM SLEKARKAQE KMEKQREKLR RKEQEQMQRK
SKKTEKMTST TAEGAGEQ
