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Protein

Serotransferrin

Gene

TF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi82 – 821Iron 1
Metal bindingi114 – 1141Iron 1
Binding sitei139 – 1391Carbonate 1
Binding sitei143 – 1431Carbonate 1
Binding sitei145 – 1451Carbonate 1; via amide nitrogen
Binding sitei146 – 1461Carbonate 1; via amide nitrogen
Metal bindingi207 – 2071Iron 1
Metal bindingi268 – 2681Iron 1
Metal bindingi411 – 4111Iron 2PROSITE-ProRule annotation
Metal bindingi445 – 4451Iron 2PROSITE-ProRule annotation
Binding sitei471 – 4711Carbonate 2PROSITE-ProRule annotation
Binding sitei475 – 4751Carbonate 2PROSITE-ProRule annotation
Binding sitei477 – 4771Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
Binding sitei478 – 4781Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi536 – 5361Iron 2PROSITE-ProRule annotation
Metal bindingi604 – 6041Iron 2PROSITE-ProRule annotation

GO - Molecular functioni

  • ferric iron binding Source: InterPro
  • ferric iron transmembrane transporter activity Source: InterPro
  • receptor binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_25060. Iron uptake and transport.
REACT_25283. Transferrin endocytosis and recycling.
REACT_318. Platelet degranulation.

Protein family/group databases

MEROPSiS60.972.

Names & Taxonomyi

Protein namesi
Recommended name:
Serotransferrin
Short name:
Transferrin
Alternative name(s):
Beta-1 metal-binding globulin
Siderophilin
Gene namesi
Name:TF
ORF Names:PRO1400
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11740. TF.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • basal part of cell Source: UniProtKB
  • basal plasma membrane Source: UniProtKB
  • blood microparticle Source: UniProtKB
  • cell surface Source: UniProtKB
  • coated pit Source: UniProtKB
  • cytoplasmic membrane-bounded vesicle Source: UniProtKB
  • early endosome Source: UniProtKB
  • endocytic vesicle Source: MGI
  • endosome membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • late endosome Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • recycling endosome Source: UniProtKB
  • secretory granule lumen Source: Reactome
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Atransferrinemia (ATRAF)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare autosomal recessive disorder characterized by abnormal synthesis of transferrin leading to iron overload and microcytic hypochromic anemia.

See also OMIM:209300
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771D → N in ATRAF. 1 Publication
VAR_038810
Natural varianti477 – 4771A → P in ATRAF. 1 Publication
VAR_012997

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi209300. phenotype.
Orphaneti1195. Congenital atransferrinemia.
PharmGKBiPA36457.

Chemistry

DrugBankiDB01370. Aluminium.
DB01294. Bismuth Subsalicylate.
DB05260. Gallium nitrate.
DB00893. Iron Dextran.

Polymorphism and mutation databases

BioMutaiTF.
DMDMi313104271.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 698679SerotransferrinPRO_0000035715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 67PROSITE-ProRule annotation1 Publication
Disulfide bondi38 ↔ 58PROSITE-ProRule annotation1 Publication
Modified residuei42 – 421Dimethylated arginine; alternateBy similarity
Modified residuei42 – 421Omega-N-methylated arginine; alternateBy similarity
Glycosylationi51 – 511O-linked (GalNAc...)CAR_000073
Disulfide bondi137 ↔ 213PROSITE-ProRule annotation1 Publication
Disulfide bondi156 ↔ 350PROSITE-ProRule annotation1 Publication
Disulfide bondi177 ↔ 193PROSITE-ProRule annotation1 Publication
Disulfide bondi180 ↔ 196PROSITE-ProRule annotation1 Publication
Disulfide bondi190 ↔ 198PROSITE-ProRule annotation1 Publication
Disulfide bondi246 ↔ 260PROSITE-ProRule annotation1 Publication
Disulfide bondi358 ↔ 615PROSITE-ProRule annotation1 Publication
Disulfide bondi364 ↔ 396PROSITE-ProRule annotation1 Publication
Disulfide bondi374 ↔ 387PROSITE-ProRule annotation1 Publication
Disulfide bondi421 ↔ 693PROSITE-ProRule annotation1 Publication
Glycosylationi432 – 4321N-linked (GlcNAc...) (complex)6 PublicationsCAR_000074
Disulfide bondi437 ↔ 656PROSITE-ProRule annotation1 Publication
Disulfide bondi469 ↔ 542PROSITE-ProRule annotation1 Publication
Glycosylationi491 – 4911N-linked (GlcNAc...); partial; atypical1 Publication
Disulfide bondi493 ↔ 684PROSITE-ProRule annotation1 Publication
Disulfide bondi503 ↔ 517PROSITE-ProRule annotation1 Publication
Disulfide bondi514 ↔ 525PROSITE-ProRule annotation1 Publication
Disulfide bondi582 ↔ 596PROSITE-ProRule annotation1 Publication
Glycosylationi630 – 6301N-linked (GlcNAc...) (complex)8 PublicationsCAR_000075
Disulfide bondi634 ↔ 639PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation

Proteomic databases

MaxQBiP02787.
PaxDbiP02787.
PRIDEiP02787.

2D gel databases

DOSAC-COBS-2DPAGEP02787.
REPRODUCTION-2DPAGEIPI00022463.
P02787.
SWISS-2DPAGEP02787.
UCD-2DPAGEP02787.

PTM databases

PhosphoSiteiP02787.
UniCarbKBiP02787.

Miscellaneous databases

PMAP-CutDBP02787.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiP02787.
CleanExiHS_TF.
ExpressionAtlasiP02787. baseline and differential.
GenevisibleiP02787. HS.

Organism-specific databases

HPAiCAB009538.
HPA001527.
HPA005692.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
GASTP013505EBI-714319,EBI-3436637

Protein-protein interaction databases

BioGridi112876. 32 interactions.
DIPiDIP-2738N.
IntActiP02787. 33 interactions.
MINTiMINT-1400694.
STRINGi9606.ENSP00000385834.

Structurei

Secondary structure

1
698
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 307Combined sources
Helixi31 – 4818Combined sources
Beta strandi51 – 544Combined sources
Beta strandi55 – 639Combined sources
Helixi64 – 729Combined sources
Beta strandi78 – 814Combined sources
Helixi83 – 908Combined sources
Turni92 – 943Combined sources
Beta strandi97 – 1059Combined sources
Beta strandi107 – 12115Combined sources
Helixi128 – 1303Combined sources
Beta strandi136 – 1394Combined sources
Turni144 – 1474Combined sources
Helixi148 – 1547Combined sources
Helixi155 – 1573Combined sources
Beta strandi158 – 1603Combined sources
Helixi165 – 1728Combined sources
Beta strandi173 – 1775Combined sources
Turni183 – 1853Combined sources
Helixi187 – 1904Combined sources
Beta strandi191 – 1933Combined sources
Helixi194 – 1963Combined sources
Beta strandi198 – 2025Combined sources
Helixi206 – 21510Combined sources
Beta strandi220 – 2256Combined sources
Helixi228 – 2325Combined sources
Helixi236 – 2394Combined sources
Beta strandi242 – 2454Combined sources
Turni247 – 2493Combined sources
Beta strandi251 – 2533Combined sources
Helixi254 – 2596Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi269 – 2724Combined sources
Beta strandi274 – 2763Combined sources
Helixi279 – 29315Combined sources
Turni295 – 2973Combined sources
Beta strandi298 – 3003Combined sources
Beta strandi310 – 3145Combined sources
Beta strandi318 – 3236Combined sources
Helixi330 – 3345Combined sources
Helixi336 – 34510Combined sources
Turni346 – 3483Combined sources
Helixi354 – 3574Combined sources
Beta strandi360 – 3656Combined sources
Helixi368 – 38013Combined sources
Turni381 – 3833Combined sources
Beta strandi384 – 3896Combined sources
Helixi393 – 4019Combined sources
Beta strandi407 – 4104Combined sources
Helixi412 – 4209Combined sources
Beta strandi424 – 4307Combined sources
Helixi437 – 4393Combined sources
Beta strandi445 – 4528Combined sources
Beta strandi455 – 4573Combined sources
Helixi460 – 4623Combined sources
Beta strandi466 – 4716Combined sources
Turni476 – 4794Combined sources
Helixi480 – 4856Combined sources
Helixi487 – 4893Combined sources
Helixi495 – 4973Combined sources
Beta strandi498 – 5036Combined sources
Beta strandi509 – 5113Combined sources
Helixi512 – 5143Combined sources
Helixi521 – 5233Combined sources
Beta strandi531 – 5333Combined sources
Helixi535 – 54511Combined sources
Beta strandi548 – 5536Combined sources
Helixi556 – 5594Combined sources
Turni568 – 5725Combined sources
Helixi575 – 5773Combined sources
Beta strandi578 – 5814Combined sources
Beta strandi587 – 5893Combined sources
Helixi590 – 5956Combined sources
Beta strandi598 – 6014Combined sources
Beta strandi605 – 6084Combined sources
Helixi610 – 6123Combined sources
Helixi613 – 62715Combined sources
Beta strandi628 – 6303Combined sources
Beta strandi635 – 6373Combined sources
Beta strandi644 – 6463Combined sources
Beta strandi648 – 6503Combined sources
Beta strandi656 – 6594Combined sources
Helixi661 – 6633Combined sources
Helixi666 – 6694Combined sources
Helixi672 – 68413Combined sources
Helixi688 – 6947Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8EX-ray1.60A22-350[»]
1A8FX-ray1.80A22-350[»]
1B3EX-ray2.50A23-352[»]
1BP5X-ray2.20A/B/C/D20-356[»]
1BTJX-ray3.20A/B20-356[»]
1D3KX-ray1.80A22-350[»]
1D4NX-ray2.00A22-350[»]
1DTGX-ray2.40A20-353[»]
1FQEX-ray1.80A20-350[»]
1FQFX-ray2.10A20-350[»]
1JQFX-ray1.85A20-353[»]
1N7WX-ray2.20A22-350[»]
1N7XX-ray2.10A20-350[»]
1N84X-ray2.05A20-350[»]
1OQGX-ray1.90A20-354[»]
1OQHX-ray2.40A20-354[»]
1RYOX-ray1.20A20-346[»]
1SUVelectron microscopy7.50C/D22-350[»]
2HAUX-ray2.70A/B23-698[»]
2HAVX-ray2.70A/B23-698[»]
2O7UX-ray2.80A/B/C/D/E/F/G/H/I20-356[»]
2O84X-ray2.60X20-356[»]
3FGSX-ray1.80A20-356[»]
3QYTX-ray2.80A20-698[»]
3S9LX-ray3.22C/D20-698[»]
3S9MX-ray3.32C/D20-698[»]
3S9NX-ray3.25C/D20-698[»]
3SKPX-ray1.70A358-698[»]
3V83X-ray2.10A/B/C/D/E/F1-698[»]
3V89X-ray3.10B356-698[»]
3V8XX-ray2.60B1-698[»]
3VE1X-ray2.96B/D20-698[»]
4H0WX-ray2.40A20-698[»]
4X1BX-ray2.45A20-698[»]
4X1DX-ray2.80A/B20-698[»]
ProteinModelPortaliP02787.
SMRiP02787. Positions 20-698.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02787.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 347323Transferrin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini361 – 683323Transferrin-like 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the transferrin family.PROSITE-ProRule annotation
Contains 2 transferrin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG87503.
GeneTreeiENSGT00390000001619.
HOGENOMiHOG000252723.
HOVERGENiHBG000055.
InParanoidiP02787.
KOiK14736.
OMAiIGLLYCD.
OrthoDBiEOG7D59N7.
PhylomeDBiP02787.
TreeFamiTF324013.

Family and domain databases

InterProiIPR030685. Serotransferrin_mammal.
IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF500682. Serotransferrin. 1 hit.
PIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 1 hit.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLAVGALLV CAVLGLCLAV PDKTVRWCAV SEHEATKCQS FRDHMKSVIP
60 70 80 90 100
SDGPSVACVK KASYLDCIRA IAANEADAVT LDAGLVYDAY LAPNNLKPVV
110 120 130 140 150
AEFYGSKEDP QTFYYAVAVV KKDSGFQMNQ LRGKKSCHTG LGRSAGWNIP
160 170 180 190 200
IGLLYCDLPE PRKPLEKAVA NFFSGSCAPC ADGTDFPQLC QLCPGCGCST
210 220 230 240 250
LNQYFGYSGA FKCLKDGAGD VAFVKHSTIF ENLANKADRD QYELLCLDNT
260 270 280 290 300
RKPVDEYKDC HLAQVPSHTV VARSMGGKED LIWELLNQAQ EHFGKDKSKE
310 320 330 340 350
FQLFSSPHGK DLLFKDSAHG FLKVPPRMDA KMYLGYEYVT AIRNLREGTC
360 370 380 390 400
PEAPTDECKP VKWCALSHHE RLKCDEWSVN SVGKIECVSA ETTEDCIAKI
410 420 430 440 450
MNGEADAMSL DGGFVYIAGK CGLVPVLAEN YNKSDNCEDT PEAGYFAIAV
460 470 480 490 500
VKKSASDLTW DNLKGKKSCH TAVGRTAGWN IPMGLLYNKI NHCRFDEFFS
510 520 530 540 550
EGCAPGSKKD SSLCKLCMGS GLNLCEPNNK EGYYGYTGAF RCLVEKGDVA
560 570 580 590 600
FVKHQTVPQN TGGKNPDPWA KNLNEKDYEL LCLDGTRKPV EEYANCHLAR
610 620 630 640 650
APNHAVVTRK DKEACVHKIL RQQQHLFGSN VTDCSGNFCL FRSETKDLLF
660 670 680 690
RDDTVCLAKL HDRNTYEKYL GEEYVKAVGN LRKCSTSSLL EACTFRRP
Length:698
Mass (Da):77,064
Last modified:November 30, 2010 - v3
Checksum:i9A73B90D8C5671E9
GO

Sequence cautioni

The sequence AAF22007.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161D → N in AAH59367 (PubMed:15489334).Curated
Sequence conflicti264 – 2641Q → E AA sequence (PubMed:6833213).Curated
Sequence conflicti329 – 3291D → N AA sequence (PubMed:6833213).Curated
Sequence conflicti329 – 3291D → N in AAA61141 (PubMed:3858812).Curated
Sequence conflicti351 – 3511P → Q in AAH59367 (PubMed:15489334).Curated
Sequence conflicti380 – 3812NS → SD AA sequence (PubMed:6833213).Curated
Sequence conflicti436 – 4361N → D AA sequence (PubMed:6833213).Curated
Sequence conflicti558 – 5614PQNT → TQNP AA sequence (PubMed:6833213).Curated
Sequence conflicti591 – 5911E → Q AA sequence (PubMed:6833213).Curated
Sequence conflicti672 – 6721E → Q AA sequence (PubMed:6833213).Curated
Sequence conflicti691 – 6911E → G in AAA61142 (PubMed:6322780).Curated

Polymorphismi

Different polymorphic variants of transferrin are known. The sequence shown is the predominant electrophoretic variant (C1 or TF*C1).

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421R → L.
Corresponds to variant rs41298293 [ dbSNP | Ensembl ].
VAR_034569
Natural varianti55 – 551S → R.1 Publication
Corresponds to variant rs8177318 [ dbSNP | Ensembl ].
VAR_029280
Natural varianti76 – 761A → V.
Corresponds to variant rs41298977 [ dbSNP | Ensembl ].
VAR_034570
Natural varianti77 – 771D → N in ATRAF. 1 Publication
VAR_038810
Natural varianti142 – 1421G → S.1 Publication
Corresponds to variant rs1799830 [ dbSNP | Ensembl ].
VAR_011997
Natural varianti277 – 2771G → S in allele TF*C3; associated with a reduction in total iron binding capacity; risk factor for iron deficiency anemia in menstruating white women. 3 Publications
Corresponds to variant rs1799899 [ dbSNP | Ensembl ].
VAR_011998
Natural varianti296 – 2961D → G in allele TF*D1. 1 Publication
Corresponds to variant rs8177238 [ dbSNP | Ensembl ].
VAR_007544
Natural varianti319 – 3191H → R in allele TF*CHI.
Corresponds to variant rs41295774 [ dbSNP | Ensembl ].
VAR_007545
Natural varianti377 – 3771W → C.
Corresponds to variant rs1804498 [ dbSNP | Ensembl ].
VAR_011999
Natural varianti448 – 4481I → V.13 Publications
Corresponds to variant rs2692696 [ dbSNP | Ensembl ].
VAR_058199
Natural varianti477 – 4771A → P in ATRAF. 1 Publication
VAR_012997
Natural varianti562 – 5621G → V.
Corresponds to variant rs41296590 [ dbSNP | Ensembl ].
VAR_034571
Natural varianti589 – 5891P → S in allele TF*C2. 4 Publications
Corresponds to variant rs1049296 [ dbSNP | Ensembl ].
VAR_012000
Natural varianti645 – 6451T → P.
Corresponds to variant rs1130537 [ dbSNP | Ensembl ].
VAR_012001
Natural varianti646 – 6461K → E in allele TF*BV. 1 Publication
VAR_012998
Natural varianti671 – 6711G → E in allele TF*B2. 1 Publication
Corresponds to variant rs121918677 [ dbSNP | Ensembl ].
VAR_012999

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12530 mRNA. Translation: AAA61140.1.
M17611, M17610 Genomic DNA. Translation: AAA61147.1.
M17614, M17612, M17613 Genomic DNA. Translation: AAA61148.1.
S95936 mRNA. Translation: AAB22049.1.
AF288144
, AF294270, AF294271, AF288139, AF288140, AF288141, AF288142, AF288143 Genomic DNA. Translation: AAK77664.1.
AY308797 Genomic DNA. Translation: AAP45055.1.
DQ525716 Genomic DNA. Translation: ABF47110.1.
AC080128 mRNA. No translation available.
AC083905 mRNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79167.1.
BC059367 mRNA. Translation: AAH59367.1.
M21569, M15673 Genomic DNA. Translation: AAA61143.2.
M21570 Genomic DNA. Translation: AAA61145.1.
X04600 Genomic DNA. Translation: CAA28265.1.
AJ252279 mRNA. Translation: CAB96907.1.
M11372
, M11361, M11362, M11363, M11364, M11365, M11366, M11367, M11368, M11369, M11370, M11371 Genomic DNA. Translation: AAA61141.1.
AF118063 mRNA. Translation: AAF22007.1. Different initiation.
M12525 mRNA. Translation: AAA61142.1.
U88581 mRNA. Translation: AAB97880.1.
AF058327 Genomic DNA. Translation: AAC63506.1.
M26641 mRNA. Translation: AAA61233.1.
CCDSiCCDS3080.1.
PIRiA20981. TFHUP.
RefSeqiNP_001054.1. NM_001063.3.
UniGeneiHs.518267.

Genome annotation databases

EnsembliENST00000402696; ENSP00000385834; ENSG00000091513.
GeneIDi7018.
KEGGihsa:7018.
UCSCiuc003epu.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Transferrin entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12530 mRNA. Translation: AAA61140.1.
M17611, M17610 Genomic DNA. Translation: AAA61147.1.
M17614, M17612, M17613 Genomic DNA. Translation: AAA61148.1.
S95936 mRNA. Translation: AAB22049.1.
AF288144
, AF294270, AF294271, AF288139, AF288140, AF288141, AF288142, AF288143 Genomic DNA. Translation: AAK77664.1.
AY308797 Genomic DNA. Translation: AAP45055.1.
DQ525716 Genomic DNA. Translation: ABF47110.1.
AC080128 mRNA. No translation available.
AC083905 mRNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79167.1.
BC059367 mRNA. Translation: AAH59367.1.
M21569, M15673 Genomic DNA. Translation: AAA61143.2.
M21570 Genomic DNA. Translation: AAA61145.1.
X04600 Genomic DNA. Translation: CAA28265.1.
AJ252279 mRNA. Translation: CAB96907.1.
M11372
, M11361, M11362, M11363, M11364, M11365, M11366, M11367, M11368, M11369, M11370, M11371 Genomic DNA. Translation: AAA61141.1.
AF118063 mRNA. Translation: AAF22007.1. Different initiation.
M12525 mRNA. Translation: AAA61142.1.
U88581 mRNA. Translation: AAB97880.1.
AF058327 Genomic DNA. Translation: AAC63506.1.
M26641 mRNA. Translation: AAA61233.1.
CCDSiCCDS3080.1.
PIRiA20981. TFHUP.
RefSeqiNP_001054.1. NM_001063.3.
UniGeneiHs.518267.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8EX-ray1.60A22-350[»]
1A8FX-ray1.80A22-350[»]
1B3EX-ray2.50A23-352[»]
1BP5X-ray2.20A/B/C/D20-356[»]
1BTJX-ray3.20A/B20-356[»]
1D3KX-ray1.80A22-350[»]
1D4NX-ray2.00A22-350[»]
1DTGX-ray2.40A20-353[»]
1FQEX-ray1.80A20-350[»]
1FQFX-ray2.10A20-350[»]
1JQFX-ray1.85A20-353[»]
1N7WX-ray2.20A22-350[»]
1N7XX-ray2.10A20-350[»]
1N84X-ray2.05A20-350[»]
1OQGX-ray1.90A20-354[»]
1OQHX-ray2.40A20-354[»]
1RYOX-ray1.20A20-346[»]
1SUVelectron microscopy7.50C/D22-350[»]
2HAUX-ray2.70A/B23-698[»]
2HAVX-ray2.70A/B23-698[»]
2O7UX-ray2.80A/B/C/D/E/F/G/H/I20-356[»]
2O84X-ray2.60X20-356[»]
3FGSX-ray1.80A20-356[»]
3QYTX-ray2.80A20-698[»]
3S9LX-ray3.22C/D20-698[»]
3S9MX-ray3.32C/D20-698[»]
3S9NX-ray3.25C/D20-698[»]
3SKPX-ray1.70A358-698[»]
3V83X-ray2.10A/B/C/D/E/F1-698[»]
3V89X-ray3.10B356-698[»]
3V8XX-ray2.60B1-698[»]
3VE1X-ray2.96B/D20-698[»]
4H0WX-ray2.40A20-698[»]
4X1BX-ray2.45A20-698[»]
4X1DX-ray2.80A/B20-698[»]
ProteinModelPortaliP02787.
SMRiP02787. Positions 20-698.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112876. 32 interactions.
DIPiDIP-2738N.
IntActiP02787. 33 interactions.
MINTiMINT-1400694.
STRINGi9606.ENSP00000385834.

Chemistry

ChEMBLiCHEMBL4865.
DrugBankiDB01370. Aluminium.
DB01294. Bismuth Subsalicylate.
DB05260. Gallium nitrate.
DB00893. Iron Dextran.

Protein family/group databases

MEROPSiS60.972.

PTM databases

PhosphoSiteiP02787.
UniCarbKBiP02787.

Polymorphism and mutation databases

BioMutaiTF.
DMDMi313104271.

2D gel databases

DOSAC-COBS-2DPAGEP02787.
REPRODUCTION-2DPAGEIPI00022463.
P02787.
SWISS-2DPAGEP02787.
UCD-2DPAGEP02787.

Proteomic databases

MaxQBiP02787.
PaxDbiP02787.
PRIDEiP02787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000402696; ENSP00000385834; ENSG00000091513.
GeneIDi7018.
KEGGihsa:7018.
UCSCiuc003epu.2. human.

Organism-specific databases

CTDi7018.
GeneCardsiGC03P133464.
HGNCiHGNC:11740. TF.
HPAiCAB009538.
HPA001527.
HPA005692.
MIMi190000. gene.
209300. phenotype.
neXtProtiNX_P02787.
Orphaneti1195. Congenital atransferrinemia.
PharmGKBiPA36457.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG87503.
GeneTreeiENSGT00390000001619.
HOGENOMiHOG000252723.
HOVERGENiHBG000055.
InParanoidiP02787.
KOiK14736.
OMAiIGLLYCD.
OrthoDBiEOG7D59N7.
PhylomeDBiP02787.
TreeFamiTF324013.

Enzyme and pathway databases

ReactomeiREACT_25060. Iron uptake and transport.
REACT_25283. Transferrin endocytosis and recycling.
REACT_318. Platelet degranulation.

Miscellaneous databases

ChiTaRSiTF. human.
EvolutionaryTraceiP02787.
GeneWikiiTransferrin.
GenomeRNAii7018.
NextBioi27415.
PMAP-CutDBP02787.
PROiP02787.
SOURCEiSearch...

Gene expression databases

BgeeiP02787.
CleanExiHS_TF.
ExpressionAtlasiP02787. baseline and differential.
GenevisibleiP02787. HS.

Family and domain databases

InterProiIPR030685. Serotransferrin_mammal.
IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF500682. Serotransferrin. 1 hit.
PIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 1 hit.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS TF*B2; TF*CHI; TF*D1 AND VAL-448.
  2. "Complete structure of the human transferrin gene. Comparison with analogous chicken gene and human pseudogene."
    Schaeffer E., Lucero M.A., Jeltsch J.-M., Py M.-C., Levin M.J., Chambon P., Cohen G.N., Zakin M.M.
    Gene 56:109-116(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-448.
    Tissue: Liver.
  4. "Molecular characterization of a case of atransferrinemia."
    Beutler E., Gelbart T., Lee P.L., Trevino R., Fernandez M.A., Fairbanks V.F.
    Blood 96:4071-4074(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-448 AND ATRAF PRO-477.
  5. SeattleSNPs variation discovery resource
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-55; SER-277; GLY-296; VAL-448 AND SER-589.
  6. NHLBI resequencing and genotyping service (RS&G)
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-448.
  7. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-448.
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-448.
    Tissue: Brain.
  10. "The human transferrin gene: 5' region contains conserved sequences which match the control elements regulated by heavy metals, glucocorticoids and acute phase reaction."
    Adrian G.S., Korinek B.W., Bowman B.H., Yang F.
    Gene 49:167-175(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 AND 291-300.
  11. "The 5' region of the human transferrin gene: structure and potential regulatory sites."
    Lucero M.A., Schaeffer E., Cohen G.N., Zakin M.M.
    Nucleic Acids Res. 14:8692-8692(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
  12. "The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure."
    McGillivray R.T.A., Mendez E., Shewale J.G., Sinha S.K., Lineback-Zins J., Brew K.
    J. Biol. Chem. 258:3543-3553(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-698, VARIANT VAL-448.
  13. "Alternative splicing prevents transferrin secretion during differentiation of a human oligodendrocyte cell line."
    de Arriba Zerpa G.A., Saleh M.-C., Fernandez P.M., Guillou F., Espinosa de los Monteros A., de Vellis J., Zakin M.M., Baron B.
    J. Neurosci. Res. 61:388-395(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-72.
  14. "Organization of the human transferrin gene: direct evidence that it originated by gene duplication."
    Park I., Schaeffer E., Sidoli A., Baralle F.E., Cohen G.N., Zakin M.M.
    Proc. Natl. Acad. Sci. U.S.A. 82:3149-3153(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-698, VARIANT VAL-448.
  15. "Functional prediction of the coding sequences of 33 new genes deduced by analysis of cDNA clones from human fetal liver."
    Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Bi J., Zhang Y., Liu M., He F.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-698, VARIANT VAL-448.
    Tissue: Fetal liver.
  16. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 108-121; 259-273; 332-343; 374-384; 434-452; 454-464; 495-508; 531-541; 577-600 AND 684-696, IDENTIFICATION BY MASS SPECTROMETRY, VARIANT VAL-448.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  17. "The major protein expression profile and two-dimensional protein database of human heart."
    Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.
    Electrophoresis 16:1160-1169(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 263-266; 454-458; 531-538 AND 589-595.
    Tissue: Heart.
  18. "Molecular cloning and sequence analysis of cDNA for human transferrin."
    Uzan G., Frain M., Park I., Besmond C., Maessen G., Trepat J.S., Zakin M.M., Kahn A.
    Biochem. Biophys. Res. Commun. 119:273-281(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 422-698, VARIANT VAL-448.
  19. "Human transferrin (Tf): a single mutation at codon 570 determines Tf C1 or Tf C2 variant."
    Namekata K., Oyama F., Imagawa M., Ihara Y.
    Hum. Genet. 100:457-458(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 564-624, VARIANTS TF*C2 AND SER-589.
    Tissue: Brain.
  20. Tsuchida S., Ikemoto S., Kajii E.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 564-624.
  21. "Changes in brain gene expression shared by scrapie and Alzheimer disease."
    Duguid J.R., Bohmont C.W., Liu N.G., Tourtellotte W.W.
    Proc. Natl. Acad. Sci. U.S.A. 86:7260-7264(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 636-696.
  22. Cited for: DISULFIDE BONDS.
  23. "Expression and initial characterization of five site-directed mutants of the N-terminal half-molecule of human transferrin."
    Woodworth R.C., Mason A.B., Funk W.D., McGillivray R.T.A.
    Biochemistry 30:10824-10829(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  24. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
    Tissue: Bile.
  25. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
    Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
    Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
    Tissue: Plasma.
  26. "Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry."
    Satomi Y., Shimonishi Y., Hase T., Takao T.
    Rapid Commun. Mass Spectrom. 18:2983-2988(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-432; ASN-491 AND ASN-630.
  27. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
    Tissue: Plasma.
  28. "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
    Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
    J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-630.
    Tissue: Saliva.
  29. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
    Tissue: Liver.
  30. Cited for: GLYCOSYLATION AT ASN-630.
  31. "Enrichment of glycopeptides for glycan structure and attachment site identification."
    Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
    Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630, STRUCTURE OF CARBOHYDRATES.
    Tissue: Cerebrospinal fluid.
  32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  34. "Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release."
    Macgillivray R.T.A., Moore S.A., Chen J., Anderson B.F., Baker H., Luo Y., Bewley M.C., Smith C.A., Murphy M.E.P., Wang Y., Mason A.B., Woodworth R.C., Brayer G.D., Baker E.N.
    Biochemistry 37:7919-7928(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 22-350.
  35. "Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin."
    Jeffrey P.D., Bewley M.C., Macgillivray R.T.A., Mason A.B., Woodworth R.C., Baker E.N.
    Biochemistry 37:13978-13986(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-350.
  36. "X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32."
    Bewley M.C., Tam B.M., Grewal J., He S., Shewry S., Murphy M.E.P., Mason A.B., Woodworth R.C., Baker E.N., Macgillivray R.T.A.
    Biochemistry 38:2535-2541(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-352.
  37. "Exon/intron structure of the human transferrin receptor gene."
    Evans P., Kemp J.
    Gene 199:123-131(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-142.
  38. "Identification of a mutation (A1879G) of transferrin from cDNA prepared from peripheral blood cells."
    Pang H., Koda Y., Soejima M., Kimura H.
    Ann. Hum. Genet. 62:271-274(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLU-646.
  39. "Human transferrin G277S mutation: a risk factor for iron deficiency anaemia."
    Lee P.L., Halloran C., Trevino R., Felitti V., Beutler E.
    Br. J. Haematol. 115:329-333(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SER-277; SER-589 AND GLU-671, CHARACTERIZATION OF VARIANT SER-277.
  40. "Identification of 96 single nucleotide polymorphisms in eight genes involved in iron metabolism: efficiency of bioinformatic extraction compared with a systematic sequencing approach."
    Douabin-Gicquel V., Soriano N., Ferran H., Wojcik F., Palierne E., Tamim S., Jovelin T., McKie A.T., Le Gall J.-Y., David V., Mosser J.
    Hum. Genet. 109:393-401(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SER-277 AND SER-589.
  41. "Molecular characterization of a third case of human atransferrinemia."
    Knisely A.S., Gelbart T., Beutler E.
    Blood 104:2607-2607(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ATRAF ASN-77.
  42. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRFE_HUMAN
AccessioniPrimary (citable) accession number: P02787
Secondary accession number(s): O43890
, Q1HBA5, Q9NQB8, Q9UHV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 30, 2010
Last modified: June 24, 2015
This is version 196 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.