1433B_SHEEP
ID 1433B_SHEEP Reviewed; 193 AA.
AC P68251; P29358;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 98.
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;
DE Flags: Fragments;
GN Name=YWHAB;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE (ISOFORM SHORT), AND ACETYLATION AT MET-1 (ISOFORM SHORT).
RC TISSUE=Brain;
RX PubMed=1317796; DOI=10.1111/j.1432-1033.1992.tb16946.x;
RA Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.;
RT "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) from
RT sheep brain. Amino acid sequence of phosphorylated forms.";
RL Eur. J. Biochem. 206:453-461(1992).
RN [2]
RP PROTEIN SEQUENCE OF 3-24 (ISOFORM LONG).
RC TISSUE=Brain;
RX PubMed=2143472; DOI=10.1111/j.1432-1033.1990.tb19138.x;
RA Toker A., Ellis C.A., Sellers L.A., Aitken A.;
RT "Protein kinase C inhibitor proteins. Purification from sheep brain and
RT sequence similarity to lipocortins and 14-3-3 protein.";
RL Eur. J. Biochem. 191:421-429(1990).
RN [3]
RP PHOSPHORYLATION AT SER-149, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=7890696; DOI=10.1074/jbc.270.11.5706;
RA Aitken A., Howell S., Jones D., Madrazo J., Patel Y.;
RT "14-3-3 alpha and delta are the phosphorylated forms of raf-activating 14-
RT 3-3 beta and zeta. In vivo stoichiometric phosphorylation in brain at a
RT Ser-Pro-Glu-Lys motif.";
RL J. Biol. Chem. 270:5706-5709(1995).
RN [4]
RP ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Aitken A., Patel Y., Martin H., Jones D., Robinson K., Madrazo J.,
RA Howell S.;
RT "Electrospray mass spectroscopy analysis with online trapping of
RT posttranslationally modified mammalian and avian brain 14-3-3 isoforms.";
RL J. Protein Chem. 13:463-465(1994).
RN [5]
RP INTERACTION WITH AANAT.
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).
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-430' and inhibits TESK1
CC kinase activity (By similarity). Interacts with MEFV (By similarity).
CC {ECO:0000250|UniProtKB:P31946, ECO:0000250|UniProtKB:Q9CQV8,
CC ECO:0000269|PubMed:11427721}.
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=P68251-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P68251-2; Sequence=VSP_018636;
CC -!- PTM: Form alpha differs from form beta in being phosphorylated.
CC Phosphorylated on Ser-60 by protein kinase C delta type catalytic
CC subunit in a sphingosine-dependent fashion (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P68251; -.
DR SMR; P68251; -.
DR iPTMnet; P68251; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
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 Gene3D; 1.20.190.20; -; 2.
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; 2.
DR Pfam; PF00244; 14-3-3; 2.
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..193
FT /note="14-3-3 protein beta/alpha"
FT /id="PRO_0000367905"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68250"
FT CHAIN 2..193
FT /note="14-3-3 protein beta/alpha, N-terminally processed"
FT /id="PRO_0000000009"
FT SITE 58
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 92
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:0000269|Ref.4"
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 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7890696"
FT MOD_RES 183
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_018636"
FT NON_CONS 84..85
FT /evidence="ECO:0000305"
FT NON_CONS 150..151
FT /evidence="ECO:0000305"
FT NON_TER 193
FT MOD_RES P68251-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:1317796"
SQ SEQUENCE 193 AA; 22054 MW; 923914FE5226E608 CRC64;
MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS
WRVISSIEQK TERNEKKQQM GKEYKMKGDY FRYLSEVASG DNKQTTVSNS QQAYQEAFEI
SKKEMQPTHP IRLGLALNFS VFYYEILNSP EAIAELDTLN EESYKDSTLI MQLLRDNLTL
WTSENQGDEG DAG
