1433B_RAT
ID 1433B_RAT Reviewed; 246 AA.
AC P35213;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=14-3-3 protein beta/alpha;
DE AltName: Full=Prepronerve growth factor RNH-1;
DE AltName: Full=Protein kinase C inhibitor protein 1;
DE Short=KCIP-1;
DE Contains:
DE RecName: Full=14-3-3 protein beta/alpha, N-terminally processed;
GN Name=Ywhab;
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 [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8381897; DOI=10.1016/0169-328x(93)90082-z;
RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H.;
RT "Molecular cloning of rat cDNAs for beta and gamma subtypes of 14-3-3
RT protein and developmental changes in expression of their mRNAs in the
RT nervous system.";
RL Brain Res. Mol. Brain Res. 17:135-146(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8749325; DOI=10.1093/jb/118.5.1045;
RA Takai R., Tanaka E., Miyazaki T., Suda M., Tashiro F.;
RT "Function of RNH-1/14-3-3 beta gene in cellular differentiation and
RT proliferation.";
RL J. Biochem. 118:1045-1053(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 14-57; 63-70; 86-117; 130-159; 161-189 AND 196-224, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 30-43, INTERACTION WITH AANAT, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=11427721; DOI=10.1073/pnas.141118798;
RA Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
RA Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
RA Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
RT "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-
RT binding switch in melatonin synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN [6]
RP INTERACTION WITH TESK1.
RX PubMed=11555644; DOI=10.1074/jbc.m104620200;
RA Toshima J.Y., Toshima J., Watanabe T., Mizuno K.;
RT "Binding of 14-3-3beta regulates the kinase activity and subcellular
RT localization of testicular protein kinase 1.";
RL J. Biol. Chem. 276:43471-43481(2001).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds to a
CC large number of partners, usually by recognition of a phosphoserine or
CC phosphothreonine motif. Binding generally results in the modulation of
CC the activity of the binding partner. Negative regulator of
CC osteogenesis. Blocks the nuclear translocation of the phosphorylated
CC form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on
CC cyclin D1 expression resulting in blockage of neuronal apoptosis
CC elicited by SRPK2. Negative regulator of signaling cascades that
CC mediate activation of MAP kinases via AKAP13.
CC {ECO:0000250|UniProtKB:P31946}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with SAMSN1 and PRKCE (By
CC similarity). Interacts with AKAP13. Interacts with SSH1 and
CC TORC2/CRTC2. Interacts with ABL1; the interaction results in
CC cytoplasmic location of ABL1 and inhibition of cABL-mediated apoptosis.
CC Interacts with ROR2 (dimer); the interaction results in phosphorylation
CC of YWHAB on tyrosine residues. Interacts with GAB2. Interacts with YAP1
CC (phosphorylated form). Interacts with the phosphorylated (by AKT1) form
CC of SRPK2 (By similarity). Interacts with PKA-phosphorylated AANAT
CC (PubMed:11427721). Interacts with MYO1C. Interacts with SIRT2 (By
CC similarity). Interacts with the 'Thr-369' phosphorylated form of DAPK2
CC (By similarity). Interacts with PI4KB, TBC1D22A and TBC1D22B. Interacts
CC with the 'Ser-1134' and 'Ser-1161' phosphorylated form of SOS1 (By
CC similarity). Interacts (via phosphorylated form) with YWHAB; this
CC interaction occurs in a protein kinase AKT1-dependent manner (By
CC similarity). Interacts with SLITRK1. Interacts with SYNPO2
CC (phosphorylated form); YWHAB competes with ACTN2 for interaction with
CC SYNPO2 (By similarity). Interacts with RIPOR2 (via phosphorylated
CC form); this interaction occurs in a chemokine-dependent manner and does
CC not compete for binding of RIPOR2 with RHOA nor blocks inhibition of
CC RIPOR2-mediated RHOA activity (By similarity). Interacts with MARK2 and
CC MARK3 (By similarity). Interacts with TESK1; the interaction is
CC dependent on the phosphorylation of TESK1 'Ser-439' and inhibits TESK1
CC kinase activity (PubMed:11555644). Interacts with MEFV (By similarity).
CC {ECO:0000250|UniProtKB:P31946, ECO:0000250|UniProtKB:Q9CQV8,
CC ECO:0000269|PubMed:11427721, ECO:0000269|PubMed:11555644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P31946}.
CC Melanosome {ECO:0000250|UniProtKB:P31946}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=P35213-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P35213-2; Sequence=VSP_018635;
CC -!- PTM: The alpha, brain-specific form differs from the beta form in being
CC phosphorylated. Phosphorylated on Ser-60 by protein kinase C delta type
CC catalytic subunit in a sphingosine-dependent fashion. {ECO:0000250}.
CC -!- PTM: Isoform Short contains a N-acetylmethionine at position 1.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; D17446; BAA04260.1; -; mRNA.
DR EMBL; S55223; AAA13843.1; -; mRNA.
DR EMBL; S83440; AAB50874.1; -; mRNA.
DR EMBL; BC076502; AAH76502.1; -; mRNA.
DR PIR; A49023; A49023.
DR RefSeq; NP_062250.1; NM_019377.1. [P35213-1]
DR AlphaFoldDB; P35213; -.
DR SMR; P35213; -.
DR BioGRID; 248554; 8.
DR IntAct; P35213; 6.
DR MINT; P35213; -.
DR STRING; 10116.ENSRNOP00000016981; -.
DR iPTMnet; P35213; -.
DR PhosphoSitePlus; P35213; -.
DR SwissPalm; P35213; -.
DR jPOST; P35213; -.
DR PaxDb; P35213; -.
DR PRIDE; P35213; -.
DR Ensembl; ENSRNOT00000016981; ENSRNOP00000016981; ENSRNOG00000010945. [P35213-1]
DR GeneID; 56011; -.
DR KEGG; rno:56011; -.
DR UCSC; RGD:61998; rat. [P35213-1]
DR CTD; 7529; -.
DR RGD; 61998; Ywhab.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P35213; -.
DR OMA; KGCQLAR; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P35213; -.
DR TreeFam; TF102003; -.
DR Reactome; R-RNO-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-RNO-165159; MTOR signalling.
DR Reactome; R-RNO-166208; mTORC1-mediated signalling.
DR Reactome; R-RNO-170968; Frs2-mediated activation.
DR Reactome; R-RNO-2028269; Signaling by Hippo.
DR Reactome; R-RNO-392517; Rap1 signalling.
DR Reactome; R-RNO-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-RNO-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-5673000; RAF activation.
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-RNO-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-RNO-9614399; Regulation of localization of FOXO transcription factors.
DR PRO; PR:P35213; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000010945; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; P35213; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0017053; C:transcription repressor complex; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR GO; GO:0050815; F:phosphoserine residue binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; ISO:RGD.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:RGD.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:RGD.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Nitration; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..246
FT /note="14-3-3 protein beta/alpha"
FT /id="PRO_0000000007"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT CHAIN 2..246
FT /note="14-3-3 protein beta/alpha, N-terminally processed"
FT /id="PRO_0000367904"
FT SITE 58
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 129
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT MOD_RES 2
FT /note="N-acetylthreonine; in 14-3-3 protein beta/alpha, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT MOD_RES 2
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT MOD_RES 51
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQV8"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT MOD_RES 84
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQV8"
FT MOD_RES 106
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQV8"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68251"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31946"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT VAR_SEQ 1..2
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018635"
FT MOD_RES P35213-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 28054 MW; B663D1F2182F9C43 CRC64;
MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS
WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICSDVL ELLDKYLILN ATHAESKVFY
LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY
YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD
AGEGEN
