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

8OPS

Human terminal uridylyltransferase 7 (TUT7/ZCCHC6) bound with pre-let7g miRNA and Lin28A - complex 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001556biological_processoocyte maturation
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0010586biological_processmiRNA metabolic process
A0016779molecular_functionnucleotidyltransferase activity
A0031054biological_processpre-miRNA processing
A0031123biological_processRNA 3'-end processing
A0035198molecular_functionmiRNA binding
A0046872molecular_functionmetal ion binding
A0050265molecular_functionRNA uridylyltransferase activity
A0070569molecular_functionuridylyltransferase activity
A0071044biological_processhistone mRNA catabolic process
A0071076biological_processRNA 3' uridylation
A0141008biological_processretrotransposon silencing by mRNA destabilization
A1990074biological_processpolyuridylation-dependent mRNA catabolic process
B0000932cellular_componentP-body
B0002151molecular_functionG-quadruplex RNA binding
B0003723molecular_functionRNA binding
B0003729molecular_functionmRNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005791cellular_componentrough endoplasmic reticulum
B0005829cellular_componentcytosol
B0007281biological_processgerm cell development
B0010494cellular_componentcytoplasmic stress granule
B0010586biological_processmiRNA metabolic process
B0010587biological_processmiRNA catabolic process
B0010629biological_processnegative regulation of gene expression
B0017148biological_processnegative regulation of translation
B0019827biological_processstem cell population maintenance
B0031047biological_processregulatory ncRNA-mediated gene silencing
B0031054biological_processpre-miRNA processing
B0031123biological_processRNA 3'-end processing
B0031369molecular_functiontranslation initiation factor binding
B0032008biological_processpositive regulation of TOR signaling
B0035198molecular_functionmiRNA binding
B0045666biological_processpositive regulation of neuron differentiation
B0045686biological_processnegative regulation of glial cell differentiation
B0045727biological_processpositive regulation of translation
B0046872molecular_functionmetal ion binding
B0048863biological_processstem cell differentiation
B0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B0060964biological_processregulation of miRNA-mediated gene silencing
B0070883molecular_functionpre-miRNA binding
B0071076biological_processRNA 3' uridylation
B0071333biological_processcellular response to glucose stimulus
B0140517molecular_functionprotein-RNA adaptor activity
B1901724biological_processpositive regulation of cell proliferation involved in kidney development
B1990825molecular_functionsequence-specific mRNA binding
B2000632biological_processnegative regulation of pre-miRNA processing
B2000767biological_processpositive regulation of cytoplasmic translation
Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues23
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Crl..CdvlIesiafahkHikekrH
ChainResidueDetails
ACYS246-HIS268

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsZN_FING: CCHC-type 1 => ECO:0000255|PROSITE-ProRule:PRU00047
ChainResidueDetails
BASP137-LEU154

site_idSWS_FT_FI2
Number of Residues17
DetailsZN_FING: CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047
ChainResidueDetails
BLYS159-LEU176

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylglycine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895
ChainResidueDetails
BGLY2

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
BSER3
BSER120
BSER200

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:5W0N, ECO:0007744|PDB:5W0O
ChainResidueDetails
ASER1047
ASER1057
AASN1130
ALYS1152
ASER1170
AHIS1286

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP1058
AASP1060

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR57

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR64

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5BLK4
ChainResidueDetails
ASER132
ASER893

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER172
ASER844

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER600

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER939

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon