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4X1D

Ytterbium-bound human serum transferrin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005770cellular_componentlate endosome
A0005788cellular_componentendoplasmic reticulum lumen
A0005886cellular_componentplasma membrane
A0005905cellular_componentclathrin-coated pit
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0007015biological_processactin filament organization
A0008198molecular_functionferrous iron binding
A0008199molecular_functionferric iron binding
A0009617biological_processresponse to bacterium
A0009925cellular_componentbasal plasma membrane
A0009986cellular_componentcell surface
A0010008cellular_componentendosome membrane
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0019731biological_processantibacterial humoral response
A0019899molecular_functionenzyme binding
A0030139cellular_componentendocytic vesicle
A0030316biological_processosteoclast differentiation
A0030669cellular_componentclathrin-coated endocytic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0031647biological_processregulation of protein stability
A0031982cellular_componentvesicle
A0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
A0034756biological_processregulation of iron ion transport
A0034774cellular_componentsecretory granule lumen
A0034986molecular_functioniron chaperone activity
A0042327biological_processpositive regulation of phosphorylation
A0044325molecular_functiontransmembrane transporter binding
A0045178cellular_componentbasal part of cell
A0045780biological_processpositive regulation of bone resorption
A0045893biological_processpositive regulation of DNA-templated transcription
A0046872molecular_functionmetal ion binding
A0048260biological_processpositive regulation of receptor-mediated endocytosis
A0048471cellular_componentperinuclear region of cytoplasm
A0055037cellular_componentrecycling endosome
A0060586biological_processmulticellular organismal-level iron ion homeostasis
A0070062cellular_componentextracellular exosome
A0070371biological_processERK1 and ERK2 cascade
A0071281biological_processcellular response to iron ion
A0072562cellular_componentblood microparticle
A1990459molecular_functiontransferrin receptor binding
A1990712cellular_componentHFE-transferrin receptor complex
A2000147biological_processpositive regulation of cell motility
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005768cellular_componentendosome
B0005769cellular_componentearly endosome
B0005770cellular_componentlate endosome
B0005788cellular_componentendoplasmic reticulum lumen
B0005886cellular_componentplasma membrane
B0005905cellular_componentclathrin-coated pit
B0006826biological_processiron ion transport
B0006879biological_processintracellular iron ion homeostasis
B0007015biological_processactin filament organization
B0008198molecular_functionferrous iron binding
B0008199molecular_functionferric iron binding
B0009617biological_processresponse to bacterium
B0009925cellular_componentbasal plasma membrane
B0009986cellular_componentcell surface
B0010008cellular_componentendosome membrane
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0019731biological_processantibacterial humoral response
B0019899molecular_functionenzyme binding
B0030139cellular_componentendocytic vesicle
B0030316biological_processosteoclast differentiation
B0030669cellular_componentclathrin-coated endocytic vesicle membrane
B0031410cellular_componentcytoplasmic vesicle
B0031647biological_processregulation of protein stability
B0031982cellular_componentvesicle
B0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
B0034756biological_processregulation of iron ion transport
B0034774cellular_componentsecretory granule lumen
B0034986molecular_functioniron chaperone activity
B0042327biological_processpositive regulation of phosphorylation
B0044325molecular_functiontransmembrane transporter binding
B0045178cellular_componentbasal part of cell
B0045780biological_processpositive regulation of bone resorption
B0045893biological_processpositive regulation of DNA-templated transcription
B0046872molecular_functionmetal ion binding
B0048260biological_processpositive regulation of receptor-mediated endocytosis
B0048471cellular_componentperinuclear region of cytoplasm
B0055037cellular_componentrecycling endosome
B0060586biological_processmulticellular organismal-level iron ion homeostasis
B0070062cellular_componentextracellular exosome
B0070371biological_processERK1 and ERK2 cascade
B0071281biological_processcellular response to iron ion
B0072562cellular_componentblood microparticle
B1990459molecular_functiontransferrin receptor binding
B1990712cellular_componentHFE-transferrin receptor complex
B2000147biological_processpositive regulation of cell motility
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue YB A 701
ChainResidue
AASP392
ATYR426
ATYR517
AHIS585
AMLI702

site_idAC2
Number of Residues10
Detailsbinding site for residue MLI A 702
ChainResidue
ATHR457
AALA458
AGLY459
ATYR517
AHIS585
AYB701
AASP392
ATYR426
ATHR452
AARG456

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 703
ChainResidue
ACYS227
ALEU228
AASP229
AASP240
AHIS242
AHOH836

site_idAC4
Number of Residues5
Detailsbinding site for residue YB B 701
ChainResidue
BASP392
BTYR426
BTYR517
BHIS585
BMLI702

site_idAC5
Number of Residues10
Detailsbinding site for residue MLI B 702
ChainResidue
BASP392
BTYR426
BTHR452
BARG456
BTHR457
BALA458
BGLY459
BTYR517
BHIS585
BYB701

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL B 703
ChainResidue
BLEU228
BASP229
BASP240
BHIS242
BHOH835

Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD
ChainResidueDetails
ATYR95-ASP104
ATYR426-SER435

site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF
ChainResidueDetails
ATYR188-PHE204
ATYR517-PHE532

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV
ChainResidueDetails
AGLN222-VAL252
AASP558-VAL588

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
ChainResidueDetails
AASP63
ATYR95
ATYR188
AHIS249
BASP63
BTYR95
BTYR188
BHIS249

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ATHR120
AARG124
AALA126
AGLY127
BTHR120
BARG124
BALA126
BGLY127

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719, ECO:0000269|PubMed:31636418, ECO:0007744|PDB:3V83, ECO:0007744|PDB:3VE1, ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ
ChainResidueDetails
AASP392
ATYR426
ATYR517
AHIS585
BASP392
BTYR426
BTYR517
BHIS585

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
ChainResidueDetails
ATHR452
AARG456
AALA458
AGLY459
BTHR452
BARG456
BALA458
BGLY459

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:P12346
ChainResidueDetails
AARG23
BARG23

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER370
ASER666
BSER370
BSER666

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: O-linked (GalNAc...) serine
ChainResidueDetails
ASER32
BSER32

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:31636418, ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ
ChainResidueDetails
AASN413
BASN413

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269|PubMed:15536627
ChainResidueDetails
AASN472
BASN472

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295
ChainResidueDetails
AASN611
BASN611

226707

PDB entries from 2024-10-30

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