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

7B51

Crystal structure of human CRM1 covalently modified by 2-mercaptoethanol at Cys528

Functional Information from GO Data
ChainGOidnamespacecontents
A0000054biological_processribosomal subunit export from nucleus
A0000055biological_processribosomal large subunit export from nucleus
A0000056biological_processribosomal small subunit export from nucleus
A0000776cellular_componentkinetochore
A0003723molecular_functionRNA binding
A0005049molecular_functionnuclear export signal receptor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005642cellular_componentannulate lamellae
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006406biological_processmRNA export from nucleus
A0006611biological_processprotein export from nucleus
A0006886biological_processintracellular protein transport
A0006913biological_processnucleocytoplasmic transport
A0010824biological_processregulation of centrosome duplication
A0015030cellular_componentCajal body
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0031267molecular_functionsmall GTPase binding
A0031965cellular_componentnuclear membrane
A0032434biological_processregulation of proteasomal ubiquitin-dependent protein catabolic process
A0032991cellular_componentprotein-containing complex
A0034504biological_processprotein localization to nucleus
A0042176biological_processregulation of protein catabolic process
A0042254biological_processribosome biogenesis
A0043231cellular_componentintracellular membrane-bounded organelle
A0046825biological_processregulation of protein export from nucleus
A0051028biological_processmRNA transport
A1990904cellular_componentribonucleoprotein complex
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0006913biological_processnucleocytoplasmic transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER391

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS446
ALYS693

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q80U96
ChainResidueDetails
ATHR448

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q80U96
ChainResidueDetails
ASER450

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q80U96
ChainResidueDetails
ATYR454

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1031

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
BALA2

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR24

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:31075303
ChainResidueDetails
BLYS37

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS60
BLYS99

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS71

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:29040603
ChainResidueDetails
BLYS134

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62827
ChainResidueDetails
BLYS159

site_idSWS_FT_FI14
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
ChainResidueDetails
BLYS71

site_idSWS_FT_FI15
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS152

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon