Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3EBM

Crystal structure of human translationally controlled tumour associated protein (hTCTP) mutant E12V

Functional Information from GO Data
ChainGOidnamespacecontents
A0000922cellular_componentspindle pole
A0003723molecular_functionRNA binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005771cellular_componentmultivesicular body
A0005829cellular_componentcytosol
A0005881cellular_componentcytoplasmic microtubule
A0006816biological_processcalcium ion transport
A0006874biological_processintracellular calcium ion homeostasis
A0009615biological_processresponse to virus
A0042981biological_processregulation of apoptotic process
A0043066biological_processnegative regulation of apoptotic process
A0070062cellular_componentextracellular exosome
A1902230biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to DNA damage
B0000922cellular_componentspindle pole
B0003723molecular_functionRNA binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005771cellular_componentmultivesicular body
B0005829cellular_componentcytosol
B0005881cellular_componentcytoplasmic microtubule
B0006816biological_processcalcium ion transport
B0006874biological_processintracellular calcium ion homeostasis
B0009615biological_processresponse to virus
B0042981biological_processregulation of apoptotic process
B0043066biological_processnegative regulation of apoptotic process
B0070062cellular_componentextracellular exosome
B1902230biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to DNA damage
C0000922cellular_componentspindle pole
C0003723molecular_functionRNA binding
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005771cellular_componentmultivesicular body
C0005829cellular_componentcytosol
C0005881cellular_componentcytoplasmic microtubule
C0006816biological_processcalcium ion transport
C0006874biological_processintracellular calcium ion homeostasis
C0009615biological_processresponse to virus
C0042981biological_processregulation of apoptotic process
C0043066biological_processnegative regulation of apoptotic process
C0070062cellular_componentextracellular exosome
C1902230biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to DNA damage
D0000922cellular_componentspindle pole
D0003723molecular_functionRNA binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005771cellular_componentmultivesicular body
D0005829cellular_componentcytosol
D0005881cellular_componentcytoplasmic microtubule
D0006816biological_processcalcium ion transport
D0006874biological_processintracellular calcium ion homeostasis
D0009615biological_processresponse to virus
D0042981biological_processregulation of apoptotic process
D0043066biological_processnegative regulation of apoptotic process
D0070062cellular_componentextracellular exosome
D1902230biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to DNA damage
Functional Information from PROSITE/UniProt
site_idPS01002
Number of Residues11
DetailsTCTP_1 Translationally controlled tumor protein (TCTP) domain signature 1. IGGNASAEGPE
ChainResidueDetails
AILE48-GLU58

site_idPS01003
Number of Residues23
DetailsTCTP_2 Translationally controlled tumor protein (TCTP) domain signature 2. FknyqFFIGEnmnp...DGmVAlldY
ChainResidueDetails
APHE129-TYR151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PLK1 => ECO:0000269|PubMed:12167714, ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER46
BSER46
CSER46
DSER46

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER53
BSER53
CSER53
DSER53

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PLK1 => ECO:0000269|PubMed:12167714
ChainResidueDetails
ASER64
BSER64
CSER64
DSER64

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon