STMN1_BOVIN
ID STMN1_BOVIN Reviewed; 149 AA.
AC Q3T0C7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Stathmin;
GN Name=STMN1;
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].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the regulation of the microtubule (MT) filament
CC system by destabilizing microtubules. Prevents assembly and promotes
CC disassembly of microtubules (By similarity). Its phosphorylation at
CC Ser-16 may be required for axon formation during neurogenesis. Involved
CC in the control of the learned and innate fear (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds to two alpha/beta-tubulin heterodimers. Interacts with
CC KIST (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- PTM: Many different phosphorylated forms are observed depending on
CC specific combinations among the sites which can be phosphorylated. MAPK
CC is responsible for the phosphorylation of stathmin in response to NGF.
CC Phosphorylation at Ser-16 seems to be required for neuron polarization
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the stathmin 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 EMBL; BC102453; AAI02454.1; -; mRNA.
DR RefSeq; NP_001029962.1; NM_001034790.2.
DR RefSeq; XP_005203304.1; XM_005203247.2.
DR RefSeq; XP_015316021.1; XM_015460535.1.
DR RefSeq; XP_015316025.1; XM_015460539.1.
DR AlphaFoldDB; Q3T0C7; -.
DR SMR; Q3T0C7; -.
DR CORUM; Q3T0C7; -.
DR STRING; 9913.ENSBTAP00000018284; -.
DR iPTMnet; Q3T0C7; -.
DR PaxDb; Q3T0C7; -.
DR PeptideAtlas; Q3T0C7; -.
DR PRIDE; Q3T0C7; -.
DR Ensembl; ENSBTAT00000018284; ENSBTAP00000018284; ENSBTAG00000013761.
DR GeneID; 616317; -.
DR KEGG; bta:616317; -.
DR CTD; 3925; -.
DR VEuPathDB; HostDB:ENSBTAG00000013761; -.
DR eggNOG; KOG1280; Eukaryota.
DR GeneTree; ENSGT01030000234597; -.
DR HOGENOM; CLU_102026_1_1_1; -.
DR InParanoid; Q3T0C7; -.
DR OMA; MAFELVF; -.
DR OrthoDB; 1381987at2759; -.
DR TreeFam; TF326935; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000013761; Expressed in floor plate of diencephalon and 104 other tissues.
DR ExpressionAtlas; Q3T0C7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR InterPro; IPR030514; Stathmin_CS.
DR InterPro; IPR000956; Stathmin_fam.
DR InterPro; IPR036002; Stathmin_sf.
DR PANTHER; PTHR10104; PTHR10104; 1.
DR Pfam; PF00836; Stathmin; 1.
DR PIRSF; PIRSF002285; Stathmin; 1.
DR PRINTS; PR00345; STATHMIN.
DR SUPFAM; SSF101494; SSF101494; 1.
DR PROSITE; PS00563; STATHMIN_1; 1.
DR PROSITE; PS01041; STATHMIN_2; 1.
DR PROSITE; PS51663; STATHMIN_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Methylation; Microtubule; Neurogenesis; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P16949"
FT CHAIN 2..149
FT /note="Stathmin"
FT /id="PRO_0000182388"
FT DOMAIN 4..145
FT /note="SLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT REGION 121..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..140
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P16949"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16949"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16949"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54227"
FT MOD_RES 25
FT /note="Phosphoserine; by CDK1, MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P16949"
FT MOD_RES 29
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16949"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16949"
FT MOD_RES 38
FT /note="Phosphoserine; by CDK1, MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P16949"
FT MOD_RES 63
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P16949"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16949"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16949"
SQ SEQUENCE 149 AA; 17303 MW; 316426F60DABCD01 CRC64;
MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER
RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL
ERLREKDKHI EEVRKNKESK DPADETEAD
