1433B_BOVIN
ID 1433B_BOVIN Reviewed; 246 AA.
AC P68250; P29358; Q0VCL1;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=14-3-3 protein beta/alpha;
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-246.
RX PubMed=1671102; DOI=10.1016/0022-2836(91)90616-e;
RA Isobe T., Ichimura T., Sunaya T., Okuyama T., Takahashi N., Kuwano R.,
RA Takahashi Y.;
RT "Distinct forms of the protein kinase-dependent activator of tyrosine and
RT tryptophan hydroxylases.";
RL J. Mol. Biol. 217:125-132(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RA Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J.,
RA McConnell D.G.;
RT "Expression of 14-3-3 proteins in bovine retinal photoreceptors.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=7931346; DOI=10.1046/j.1471-4159.1994.63051908.x;
RA Tanji M., Horwitz R., Rosenfeld G., Waymire J.C.;
RT "Activation of protein kinase C by purified bovine brain 14-3-3: comparison
RT with tyrosine hydroxylase activation.";
RL J. Neurochem. 63:1908-1916(1994).
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, ECO:0000269|PubMed:7931346}.
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. Interacts with PKA-phosphorylated AANAT. Interacts with
CC MYO1C. Interacts with SIRT2 (By similarity). Interacts with the 'Thr-
CC 369' phosphorylated form of DAPK2 (By similarity). Interacts with
CC PI4KB, TBC1D22A and TBC1D22B. Interacts with the 'Ser-1134' and 'Ser-
CC 1161' phosphorylated form of SOS1 (By similarity). Interacts (via
CC phosphorylated form) with YWHAB; this interaction occurs in a protein
CC kinase AKT1-dependent manner (By similarity). Interacts with SLITRK1.
CC Interacts with SYNPO2 (phosphorylated form); YWHAB competes with ACTN2
CC for interaction with SYNPO2 (By similarity). Interacts with RIPOR2 (via
CC phosphorylated form); this interaction occurs in a chemokine-dependent
CC manner and does not compete for binding of RIPOR2 with RHOA nor blocks
CC inhibition of RIPOR2-mediated RHOA activity (By similarity). Interacts
CC with MARK2 and MARK3 (By similarity). Interacts with TESK1; the
CC interaction is dependent on the phosphorylation of TESK1 'Ser-439' and
CC inhibits TESK1 kinase activity (By similarity). Interacts with MEFV (By
CC similarity). {ECO:0000250|UniProtKB:P31946,
CC ECO:0000250|UniProtKB:Q9CQV8}.
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 Comment=It is uncertain whether isoform Short is produced by
CC alternative initiation or another biological event.;
CC Name=Long;
CC IsoId=P68250-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P68250-2; Sequence=VSP_018631;
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 -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; BC120112; AAI20113.1; -; mRNA.
DR EMBL; AF043736; AAC02090.1; -; mRNA.
DR PIR; S13467; S13467.
DR RefSeq; NP_777219.2; NM_174794.2.
DR AlphaFoldDB; P68250; -.
DR SMR; P68250; -.
DR STRING; 9913.ENSBTAP00000022411; -.
DR iPTMnet; P68250; -.
DR PaxDb; P68250; -.
DR PeptideAtlas; P68250; -.
DR PRIDE; P68250; -.
DR GeneID; 286863; -.
DR KEGG; bta:286863; -.
DR CTD; 7529; -.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P68250; -.
DR OrthoDB; 1176818at2759; -.
DR TreeFam; TF102003; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
DR GO; GO:0019904; F:protein domain specific binding; ISS:AgBase.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; ISS:AgBase.
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_0000367899"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31946,
FT ECO:0000269|PubMed:1671102"
FT CHAIN 2..246
FT /note="14-3-3 protein beta/alpha, N-terminally processed"
FT /id="PRO_0000000001"
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:0000303|Ref.3"
FT /id="VSP_018631"
FT CONFLICT 101
FT /note="Q -> E (in Ref. 1; AAI20113)"
FT /evidence="ECO:0000305"
FT MOD_RES P68250-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 246 AA; 28081 MW; CABA32314D86800D CRC64;
MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS
WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL QLLDKYLIPN ATQPESKVFY
LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY
YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD
AGEGEN
