MAP1B_RAT
ID MAP1B_RAT Reviewed; 2461 AA.
AC P15205; B0BNK3; F1LRL9; Q62958; Q9ER21; Q9QW92;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Microtubule-associated protein 1B;
DE Short=MAP-1B;
DE AltName: Full=Neuraxin;
DE Contains:
DE RecName: Full=MAP1B heavy chain;
DE Contains:
DE RecName: Full=MAP1 light chain LC1;
GN Name=Map1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-691.
RC TISSUE=Prostate {ECO:0000312|EMBL:AAI58859.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-142.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=8666295; DOI=10.1016/0378-1119(95)00061-5;
RA Liu D., Fischer I.;
RT "Isolation and sequencing of the 5' end of the rat microtubule-associated
RT protein (MAP1B)-encoding cDNA.";
RL Gene 171:307-308(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 96-2461, DOMAIN, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Glial tumor;
RX PubMed=1639092;
RA Zauner W., Kratz J., Staunton J., Feick P., Wiche G.;
RT "Identification of two distinct microtubule binding domains on recombinant
RT rat MAP 1B.";
RL Eur. J. Cell Biol. 57:66-74(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1545-2461, AND TISSUE SPECIFICITY.
RC TISSUE=Spinal cord;
RX PubMed=2555150; DOI=10.1002/j.1460-2075.1989.tb08436.x;
RA Rienitz A., Grenningloh G., Hermans-Borgmeyer I., Kirsch J., Littauer U.Z.,
RA Prior P., Gundelfinger E.D., Schmitt B., Betz H.;
RT "Neuraxin, a novel putative structural protein of the rat central nervous
RT system that is immunologically related to microtubule-associated protein
RT 5.";
RL EMBO J. 8:2879-2888(1989).
RN [6]
RP DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RX PubMed=9260743;
RX DOI=10.1002/(sici)1097-4547(19970801)49:3<319::aid-jnr7>3.0.co;2-f;
RA Ma D., Nothias F., Boyne L.J., Fischer I.;
RT "Differential regulation of microtubule-associated protein 1B (MAP1B) in
RT rat CNS and PNS during development.";
RL J. Neurosci. Res. 49:319-332(1997).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1908, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-339; SER-341;
RP SER-343; THR-527; SER-541; SER-821; SER-824; SER-825; SER-929; SER-930;
RP THR-941; SER-956; SER-963; SER-985; SER-988; SER-1009; SER-1180; SER-1183;
RP SER-1201; SER-1239; SER-1244; SER-1248; SER-1250; SER-1252; SER-1254;
RP SER-1257; THR-1274; SER-1315; SER-1323; SER-1371; SER-1382; SER-1393;
RP SER-1420; SER-1436; SER-1494; SER-1505; SER-1513; SER-1515; THR-1518;
RP SER-1520; SER-1613; SER-1618; SER-1646; SER-1656; SER-1659; SER-1765;
RP SER-1772; SER-1778; THR-1781; SER-1812; SER-1870; SER-1874; SER-1908;
RP THR-1925; THR-1942 AND SER-2027, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Phosphorylated MAP1B may play a role in the cytoskeletal
CC changes that accompany neurite extension. Possibly MAP1B binds to at
CC least two tubulin subunits in the polymer, and this bridging of
CC subunits might be involved in nucleating microtubule polymerization and
CC in stabilizing microtubules. Acts as a positive cofactor in DAPK1-
CC mediated autophagic vesicle formation and membrane blebbing.
CC Facilitates tyrosination of alpha-tubulin in neuronal microtubules.
CC Required for synaptic maturation (By similarity). Interacts with
CC TMEM185A (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with
CC MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region
CC of MAP1B. Interacts with ANP32A and TIAM2. Interacts with the tubulin
CC tyrosine TTL (By similarity). Interacts (via C-terminus) with GAN (via
CC Kelch domains). Interacts (via N-terminus) with DAPK1. Interacts with
CC TMEM185A. Interacts with MAP1LC3B. Interacts with KIRREL3 (By
CC similarity). MAP1 light chain LC1 (via C-terminus): Interacts with
CC ELAVL4; the interaction contributes to the association of ELAVL4 with
CC microtubules (By similarity). MAP1 light chain LC1: Interacts with
CC ELAVL2 and ELAVL3 (By similarity). {ECO:0000250|UniProtKB:P14873,
CC ECO:0000250|UniProtKB:P46821}.
CC -!- INTERACTION:
CC P15205; P31388: Htr6; NbExp=2; IntAct=EBI-349666, EBI-21279242;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm
CC {ECO:0000250}. Synapse {ECO:0000250}. Cell projection, dendritic spine
CC {ECO:0000250}. Note=Colocalizes with DAPK1 in the microtubules and
CC cortical actin fibers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [MAP1 light chain LC1]: Cytoplasm
CC {ECO:0000250|UniProtKB:P14873}.
CC -!- TISSUE SPECIFICITY: Nervous system (spinal cord, brain stem, cerebellum
CC and cerebrum). Not expressed in liver, spleen, kidney, heart or muscle.
CC {ECO:0000269|PubMed:2555150}.
CC -!- DEVELOPMENTAL STAGE: In cerebral cortex, spinal cord and sciatic nerve
CC levels are high early in development but decrease during postnatal
CC development and are low in adults. In dorsal root ganglia levels remain
CC high throughout development. {ECO:0000269|PubMed:9260743}.
CC -!- INDUCTION: By nerve growth factor. {ECO:0000269|PubMed:1639092}.
CC -!- DOMAIN: Has a highly basic region with many copies of the sequence KKEE
CC and KKEI/V, repeated but not at fixed intervals, which is responsible
CC for the binding of MAP1B to microtubules. {ECO:0000269|PubMed:1639092}.
CC -!- PTM: LC1 is coexpressed with MAP1B. It is a polypeptide generated from
CC MAP1B by proteolytic processing. It is free to associate with both
CC MAP1A and MAP1B. It interacts with the N-terminal region of MAP1B (By
CC similarity). {ECO:0000250}.
CC -!- PTM: S-nitrosylation at Cys-2457 enhances interaction with
CC microtubules, and may act as an effector modification for neuronal
CC nitric oxide synthase control of growth-cone size, growth-cone collapse
CC and axon retraction. {ECO:0000250|UniProtKB:P14873}.
CC -!- SIMILARITY: Belongs to the MAP1 family. {ECO:0000305}.
CC -!- CAUTION: A C-terminal fragment of this protein (residues 1599 to 2461)
CC was originally described as neuraxin in PubMed:2555150. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI58859.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=CAA34620.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AABR07007833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07007832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC158858; AAI58859.1; ALT_SEQ; mRNA.
DR EMBL; U52950; AAB17068.1; -; mRNA.
DR EMBL; X60370; CAC16162.1; -; mRNA.
DR EMBL; X16623; CAA34620.1; ALT_INIT; mRNA.
DR PIR; A56577; A56577.
DR RefSeq; NP_062090.1; NM_019217.1.
DR AlphaFoldDB; P15205; -.
DR BMRB; P15205; -.
DR BioGRID; 248099; 12.
DR IntAct; P15205; 7.
DR MINT; P15205; -.
DR STRING; 10116.ENSRNOP00000023460; -.
DR ChEMBL; CHEMBL3217383; -.
DR iPTMnet; P15205; -.
DR PhosphoSitePlus; P15205; -.
DR jPOST; P15205; -.
DR PaxDb; P15205; -.
DR PRIDE; P15205; -.
DR Ensembl; ENSRNOT00000023460; ENSRNOP00000023460; ENSRNOG00000017428.
DR GeneID; 29456; -.
DR KEGG; rno:29456; -.
DR UCSC; RGD:3043; rat.
DR CTD; 4131; -.
DR RGD; 3043; Map1b.
DR eggNOG; KOG3592; Eukaryota.
DR GeneTree; ENSGT00940000155897; -.
DR HOGENOM; CLU_000285_0_1_1; -.
DR InParanoid; P15205; -.
DR OMA; VTKANHV; -.
DR OrthoDB; 86642at2759; -.
DR PhylomeDB; P15205; -.
DR TreeFam; TF350229; -.
DR PRO; PR:P15205; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000017428; Expressed in cerebellum and 19 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IDA:ARUK-UCL.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0097441; C:basal dendrite; IDA:ARUK-UCL.
DR GO; GO:0005856; C:cytoskeleton; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0097457; C:hippocampal mossy fiber; IDA:ARUK-UCL.
DR GO; GO:0005874; C:microtubule; IDA:ARUK-UCL.
DR GO; GO:0005875; C:microtubule associated complex; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:ARUK-UCL.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043196; C:varicosity; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:ARUK-UCL.
DR GO; GO:0005543; F:phospholipid binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0048675; P:axon extension; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0021700; P:developmental maturation; IEP:RGD.
DR GO; GO:0061162; P:establishment of monopolar cell polarity; ISO:RGD.
DR GO; GO:0051915; P:induction of synaptic plasticity by chemical substance; IEP:RGD.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; ISO:RGD.
DR GO; GO:0032387; P:negative regulation of intracellular transport; ISO:RGD.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:RGD.
DR GO; GO:0007399; P:nervous system development; IEP:RGD.
DR GO; GO:0048666; P:neuron development; IEP:RGD.
DR GO; GO:0071895; P:odontoblast differentiation; ISO:RGD.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEP:RGD.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0031114; P:regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0017085; P:response to insecticide; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007416; P:synapse assembly; IEP:RGD.
DR InterPro; IPR026074; MAP1.
DR InterPro; IPR027321; MAP1B.
DR InterPro; IPR000102; MAP1B_neuraxin.
DR PANTHER; PTHR13843; PTHR13843; 1.
DR PANTHER; PTHR13843:SF5; PTHR13843:SF5; 1.
DR Pfam; PF00414; MAP1B_neuraxin; 6.
DR PROSITE; PS00230; MAP1B_NEURAXIN; 8.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Cytoplasm; Cytoskeleton; Methylation;
KW Microtubule; Phosphoprotein; Reference proteome; Repeat; S-nitrosylation;
KW Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT CHAIN 2..2461
FT /note="Microtubule-associated protein 1B"
FT /id="PRO_0000018608"
FT CHAIN 2..2199
FT /note="MAP1B heavy chain"
FT /id="PRO_0000418381"
FT CHAIN 2200..2461
FT /note="MAP1 light chain LC1"
FT /id="PRO_0000018609"
FT REPEAT 1871..1887
FT /note="MAP1B 1"
FT /evidence="ECO:0000305"
FT REPEAT 1888..1904
FT /note="MAP1B 2"
FT /evidence="ECO:0000305"
FT REPEAT 1905..1921
FT /note="MAP1B 3"
FT /evidence="ECO:0000305"
FT REPEAT 1922..1938
FT /note="MAP1B 4"
FT /evidence="ECO:0000305"
FT REPEAT 1939..1955
FT /note="MAP1B 5"
FT /evidence="ECO:0000305"
FT REPEAT 1956..1972
FT /note="MAP1B 6"
FT /evidence="ECO:0000305"
FT REPEAT 1990..2006
FT /note="MAP1B 7"
FT /evidence="ECO:0000305"
FT REPEAT 2007..2023
FT /note="MAP1B 8"
FT /evidence="ECO:0000305"
FT REPEAT 2024..2040
FT /note="MAP1B 9"
FT /evidence="ECO:0000305"
FT REPEAT 2041..2057
FT /note="MAP1B 10"
FT /evidence="ECO:0000305"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1762..1819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1843..1884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1921..1969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2009..2029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2045..2071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2087..2343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2287..2459
FT /note="Mediates interaction with TMEM185A"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT COMPBIAS 553..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..953
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1024
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1778..1815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2131..2157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2277..2293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2301..2316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2317..2342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 527
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 892
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 901
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 941
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 956
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 963
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1274
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1321
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1403
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1518
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1781
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1789
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1790
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 1812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1870
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1874
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 1912
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1925
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 1942
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2027
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2057
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 2202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 2264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 2282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 2298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46821"
FT MOD_RES 2407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT MOD_RES 2457
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P14873"
FT CONFLICT 67
FT /note="D -> E (in Ref. 3; AAB17068)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="M -> V (in Ref. 3; AAB17068)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="T -> S (in Ref. 3; AAB17068)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="Missing (in Ref. 4; CAC16162)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="E -> K (in Ref. 4; CAC16162)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="T -> A (in Ref. 4; CAC16162)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="E -> K (in Ref. 2; AAI58859)"
FT /evidence="ECO:0000305"
FT CONFLICT 1057
FT /note="G -> D (in Ref. 4; CAC16162)"
FT /evidence="ECO:0000305"
FT CONFLICT 1138
FT /note="S -> T (in Ref. 4; CAC16162)"
FT /evidence="ECO:0000305"
FT CONFLICT 1348..1349
FT /note="KP -> NA (in Ref. 4; CAC16162)"
FT /evidence="ECO:0000305"
FT CONFLICT 1454
FT /note="S -> R (in Ref. 4; CAC16162)"
FT /evidence="ECO:0000305"
FT CONFLICT 1531
FT /note="Missing (in Ref. 4; CAC16162)"
FT /evidence="ECO:0000305"
FT CONFLICT 2114
FT /note="K -> R (in Ref. 4; CAC16162)"
FT /evidence="ECO:0000305"
FT CONFLICT 2171
FT /note="I -> L (in Ref. 4; CAC16162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2461 AA; 269643 MW; B9E2ED2B5F3742A4 CRC64;
MATVVVEATE PEPSGSIGNP AATTSPSLSH RFLDSKFYLL VVVGETVTEE HLRRAIGNIE
LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL HHRSDVLETV VLINPSDEAV
STEVRLMITD AARHKLLVLT GQCFENTGEL ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP
ANKASLTLFC PEEGDWKNSN LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP
SPFDILEPPT SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH
LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEERSQGST SNSDWMKNLI SPDLGVVFLN
VPENLKNPEP NIKMKRSTEE ACFTLQYLNK LSMKPEPLFR SVGNAIEPVI LFQKMGVGKL
EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE LILPNGQEVD IPISYLTSVS SLIVWHPANP
AEKIIRVLFP GNSTQYNILE GLEKLKHLDF LKQPLATQKD LTGQVSTPPV KQVKLKQRAD
SRESLKPATK PLSSKSVRKE SKEEAPEATK ASQVEKTPKV ESKEKVIVKK DKPGKVESKP
SVTEKEVPSK EEQSPVKAEV AEKAATESKP KVTKDKVVKK EIKTKPEEKK EEKPKKEVAK
KEDKTPLKKD EKPKKEEAKK EIKKEIKKEE KKELKKEVKK ETPLKDAKKE VKKDEKKEVK
KEEKEPKKEI KKISKDIKKS TPLSDTKKPA ALKPKVAKKE EPTKKEPIAA GKLKDKGKVK
VIKKEGKTTE AAATAVGTAA VAAAAGVAAS GPAKELEAER SLMSSPEDLT KDFEELKAEE
IDVAKDIKPQ LELIEDEEKL KETEPGEAYV IQKETEVSKG SAESPDEGIT TTEGEGECEQ
TPEELEPVEK QGVDDIEKFE DEGAGFEESS EAGDYEEKAE TEEAEEPEED GEDNVSGSAS
KHSPTEDEEI AKAEADVHIK EKRESVASGD DRAEEDMDEA LEKGEAEQSE EEGEEEEDKA
EDAREEDHEP DKTEAEDYVM AVVDKAAEAG VTEDQYGFLG TPAKQPGVQS PSREPASSIH
DETLPGGSES EATASDEENR EDQPEEFTAT SGYTQSTIEI SSEPTPMDEM STPRDVMSDE
TNNEETESPS QEFVNITKYE SSLYSQEYSK PVVASFNGLS DGSKTDATDG RDYNASASTI
SPPSSMEEDK FSKSALRDAY RPEETDVKTG AELDIKDVSD ERLSPAKSPS LSPSPPSPIE
KTPLGERSVN FSLTPNEIKA SAEGEATAVV SPGVTQAVVE EHCASPEEKT LEVVSPSQSV
TGSAGHTPYY QSPTDEKSSH LPTEVTEKPQ AVPVSFEFTE AKDENERSSI SPMDEPVPDS
ESPIEKVLSP LRSPPLIGSE SAYEDFLSAD DKALGRRSES PFEGKNGKQG FSDKESPVSD
LTSDLYQDKQ EEKSAGFIPI KEDFSPEKKA SDAEIMSSQS ALALDERKLG GDGSPTQVDV
SQFGSFKEDT KMSISEGTVS DKSATPVDEG VAEDTYSHME GVASVSTASV ATSSFPEPTT
DDVSPSLHAE VGSPHSTEVD DSLSVSVVQT PTTFQETEMS PSKEECPRPM SISPPDFSPK
TAKSRTPVQD HRSEQSSMSI EFGQESPEHS LAMDFSRQSP DHPTVGAGML HITENGPTEV
DYSPSDIQDS SLSHKIPPTE EPSYTQDNDL SELISVSQVE ASPSTSSAHT PSQIASPLQE
DTLSDVVPPR DMSLYASLAS EKVQSLEGEK LSPKSDISPL TPRESSPTYS PGFSDSTSGA
KESTAAYQTS SSPPIDAAAA EPYGFRSSML FDTMQHHLAL SRDLTTSSVE KDNGGKTPGD
FNYAYQKPES TTESPDEEDY DYESHEKTIQ AHDVGGYYYE KTERTIKSPC DSGYSYETIE
KTTKTPEDGG YSCEITEKTT RTPEEGGYSY EISEKTTRTP EVSGYTYEKT ERSRRLLDDI
SNGYDDTEDG GHTLGDCSYS YETTEKITSF PESESYSYET TTKTTRSPDT SAYCYETMEK
ITKTPQASTY SYETSDRCYT PERKSPSEAR QDVDLCLVSS CEFKHPKTEL SPSFINPNPL
EWFAGEEPTE ESEKPLTQSG GAPPPSGGKQ QGRQCDETPP TSVSESAPSQ TDSDVPPETE
ECPSITADAN IDSEDESETI PTDKTVTYKH MDPPPAPMQD RSPSPRHPDV SMVDPEALAI
EQNLGKALKK DLKEKAKTKK PGTKTKSSSP VKKGDGKSKP SAASPKPGAL KESSDKVSRV
ASPKKKESVE KAMKTTTTPE VKATRGEEKD KETKNAANAS ASKSVKTATA GPGTTKTAKS
STVPPGLPVY LDLCYIPNHS NSKNVDVEFF KRVRSSYYVV SGNDPAAEEP SRAVLDALLE
GKAQWGSNMQ VTLIPTHDSE VMREWYQETH EKQQDLNIMV LASSSTVVMQ DESFPACKIE
L
