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Protein

Transcobalamin-2

Gene

TCN2

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

Functioni

Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041Cobalamin1 Publication
Metal bindingi190 – 1901Cobalt (cobalamin axial ligand)
Binding sitei242 – 2421Cobalamin1 Publication
Binding sitei245 – 2451Cobalamin1 Publication
Binding sitei291 – 2911Cobalamin1 Publication

GO - Molecular functioni

  • cobalamin binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cobalt transport, Ion transport, Transport

Keywords - Ligandi

Cobalt, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_169120. Defective TCN2 causes hereditary megaloblastic anemia.
REACT_169178. Defective CD320 causes methylmalonic aciduria.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcobalamin-2
Short name:
TC-2
Alternative name(s):
Transcobalamin II
Short name:
TC II
Short name:
TCII
Gene namesi
Name:TCN2
Synonyms:TC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:11653. TCN2.

Subcellular locationi

GO - Cellular componenti

  • endosome Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
  • lysosomal lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Transcobalamin II deficiency (TCN2 deficiency)

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

Disease descriptionResults in various forms of anemia.

See also OMIM:275350

Organism-specific databases

MIMi275350. phenotype.
Orphaneti859. Transcobalamin deficiency.
PharmGKBiPA36404.

Chemistry

DrugBankiDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.

Polymorphism and mutation databases

BioMutaiTCN2.
DMDMi224471876.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 427409Transcobalamin-2PRO_0000005564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 2671 Publication
Disulfide bondi116 ↔ 3091 Publication
Disulfide bondi165 ↔ 2051 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP20062.
PRIDEiP20062.

PTM databases

PhosphoSiteiP20062.

Expressioni

Gene expression databases

BgeeiP20062.
CleanExiHS_TCN2.
ExpressionAtlasiP20062. baseline and differential.
GenevisibleiP20062. HS.

Organism-specific databases

HPAiHPA000837.

Interactioni

Protein-protein interaction databases

BioGridi112808. 4 interactions.
IntActiP20062. 2 interactions.
STRINGi9606.ENSP00000215838.

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 3811Combined sources
Helixi39 – 435Combined sources
Turni47 – 493Combined sources
Helixi52 – 598Combined sources
Beta strandi61 – 644Combined sources
Helixi67 – 8418Combined sources
Helixi102 – 11413Combined sources
Helixi122 – 14221Combined sources
Helixi154 – 16613Combined sources
Helixi173 – 18311Combined sources
Helixi192 – 20716Combined sources
Turni208 – 2103Combined sources
Helixi213 – 2153Combined sources
Helixi216 – 23217Combined sources
Beta strandi240 – 2423Combined sources
Turni243 – 2453Combined sources
Helixi246 – 2538Combined sources
Helixi262 – 27817Combined sources
Turni279 – 2813Combined sources
Helixi286 – 2927Combined sources
Helixi295 – 2973Combined sources
Helixi301 – 3044Combined sources
Beta strandi329 – 3368Combined sources
Beta strandi338 – 3414Combined sources
Beta strandi343 – 3508Combined sources
Helixi355 – 36511Combined sources
Beta strandi370 – 3734Combined sources
Beta strandi380 – 3845Combined sources
Beta strandi391 – 3999Combined sources
Turni400 – 4023Combined sources
Turni409 – 4113Combined sources
Beta strandi418 – 4269Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BB5X-ray3.20A/B19-427[»]
ProteinModelPortaliP20062.
SMRiP20062. Positions 19-427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20062.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni152 – 1565Cobalamin binding
Regioni190 – 1945Cobalamin binding
Regioni395 – 3973Cobalamin binding

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG47054.
GeneTreeiENSGT00530000063370.
HOGENOMiHOG000074060.
HOVERGENiHBG001328.
InParanoidiP20062.
KOiK14619.
OMAiGEREFWQ.
OrthoDBiEOG79GT6F.
PhylomeDBiP20062.
TreeFamiTF333092.

Family and domain databases

InterProiIPR002157. Cbl-bd_transpt_euk.
IPR027954. DUF4430.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR10559. PTHR10559. 1 hit.
PfamiPF01122. Cobalamin_bind. 1 hit.
PF14478. DUF4430. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
PROSITEiPS00468. COBALAMIN_BINDING. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P20062-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRHLGAFLFL LGVLGALTEM CEIPEMDSHL VEKLGQHLLP WMDRLSLEHL
60 70 80 90 100
NPSIYVGLRL SSLQAGTKED LYLHSLKLGY QQCLLGSAFS EDDGDCQGKP
110 120 130 140 150
SMGQLALYLL ALRANCEFVR GHKGDRLVSQ LKWFLEDEKR AIGHDHKGHP
160 170 180 190 200
HTSYYQYGLG ILALCLHQKR VHDSVVDKLL YAVEPFHQGH HSVDTAAMAG
210 220 230 240 250
LAFTCLKRSN FNPGRRQRIT MAIRTVREEI LKAQTPEGHF GNVYSTPLAL
260 270 280 290 300
QFLMTSPMRG AELGTACLKA RVALLASLQD GAFQNALMIS QLLPVLNHKT
310 320 330 340 350
YIDLIFPDCL APRVMLEPAA ETIPQTQEII SVTLQVLSLL PPYRQSISVL
360 370 380 390 400
AGSTVEDVLK KAHELGGFTY ETQASLSGPY LTSVMGKAAG EREFWQLLRD
410 420
PNTPLLQGIA DYRPKDGETI ELRLVSW
Length:427
Mass (Da):47,535
Last modified:March 3, 2009 - v3
Checksum:iFD04A110941989DB
GO
Isoform 2 (identifier: P20062-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     116-143: CEFVRGHKGDRLVSQLKWFLEDEKRAIG → W

Note: No experimental confirmation available.
Show »
Length:400
Mass (Da):44,421
Checksum:i38C59B8CF61DC15D
GO

Polymorphismi

Pro/Arg-259 polymorphism affects TCN2 plasma concentration and may interfere in vitamin B(12) cellular availability and homocysteine metabolism.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231I → V.
Corresponds to variant rs9606756 [ dbSNP | Ensembl ].
VAR_054539
Natural varianti89 – 891F → L.
Corresponds to variant rs35915865 [ dbSNP | Ensembl ].
VAR_054540
Natural varianti198 – 1981M → T.1 Publication
VAR_001638
Natural varianti215 – 2151R → W.
Corresponds to variant rs35838082 [ dbSNP | Ensembl ].
VAR_054541
Natural varianti219 – 2191I → L.1 Publication
VAR_001639
Natural varianti227 – 2271R → Q.1 Publication
Corresponds to variant rs17849434 [ dbSNP | Ensembl ].
VAR_054542
Natural varianti259 – 2591R → P.3 Publications
Corresponds to variant rs1801198 [ dbSNP | Ensembl ].
VAR_001640
Natural varianti348 – 3481S → F.
Corresponds to variant rs9621049 [ dbSNP | Ensembl ].
VAR_054543
Natural varianti376 – 3761L → S.1 Publication
Corresponds to variant rs1131603 [ dbSNP | Ensembl ].
VAR_001641
Natural varianti399 – 3991R → Q.
Corresponds to variant rs4820889 [ dbSNP | Ensembl ].
VAR_054544

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei116 – 14328CEFVR…KRAIG → W in isoform 2. 1 PublicationVSP_043711Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60396 mRNA. Translation: AAA61054.1.
L02647 mRNA. Translation: AAA61056.1.
L02648 mRNA. Translation: AAA61057.1.
AF047576 Genomic DNA. Translation: AAC05491.1.
CR456591 mRNA. Translation: CAG30477.1.
AC005006 Genomic DNA. No translation available.
BC001176 mRNA. Translation: AAH01176.1.
BC011239 mRNA. Translation: AAH11239.1.
CCDSiCCDS13881.1. [P20062-1]
CCDS54519.1. [P20062-2]
PIRiA39744.
RefSeqiNP_000346.2. NM_000355.3. [P20062-1]
NP_001171655.1. NM_001184726.1. [P20062-2]
UniGeneiHs.417948.

Genome annotation databases

EnsembliENST00000215838; ENSP00000215838; ENSG00000185339.
ENST00000407817; ENSP00000384914; ENSG00000185339. [P20062-2]
GeneIDi6948.
KEGGihsa:6948.
UCSCiuc003aip.2. human. [P20062-1]
uc003air.2. human. [P20062-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

TCN2base

TCN2 mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60396 mRNA. Translation: AAA61054.1.
L02647 mRNA. Translation: AAA61056.1.
L02648 mRNA. Translation: AAA61057.1.
AF047576 Genomic DNA. Translation: AAC05491.1.
CR456591 mRNA. Translation: CAG30477.1.
AC005006 Genomic DNA. No translation available.
BC001176 mRNA. Translation: AAH01176.1.
BC011239 mRNA. Translation: AAH11239.1.
CCDSiCCDS13881.1. [P20062-1]
CCDS54519.1. [P20062-2]
PIRiA39744.
RefSeqiNP_000346.2. NM_000355.3. [P20062-1]
NP_001171655.1. NM_001184726.1. [P20062-2]
UniGeneiHs.417948.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BB5X-ray3.20A/B19-427[»]
ProteinModelPortaliP20062.
SMRiP20062. Positions 19-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112808. 4 interactions.
IntActiP20062. 2 interactions.
STRINGi9606.ENSP00000215838.

Chemistry

DrugBankiDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.

PTM databases

PhosphoSiteiP20062.

Polymorphism and mutation databases

BioMutaiTCN2.
DMDMi224471876.

Proteomic databases

PaxDbiP20062.
PRIDEiP20062.

Protocols and materials databases

DNASUi6948.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215838; ENSP00000215838; ENSG00000185339.
ENST00000407817; ENSP00000384914; ENSG00000185339. [P20062-2]
GeneIDi6948.
KEGGihsa:6948.
UCSCiuc003aip.2. human. [P20062-1]
uc003air.2. human. [P20062-2]

Organism-specific databases

CTDi6948.
GeneCardsiGC22P031002.
HGNCiHGNC:11653. TCN2.
HPAiHPA000837.
MIMi275350. phenotype.
613441. gene.
neXtProtiNX_P20062.
Orphaneti859. Transcobalamin deficiency.
PharmGKBiPA36404.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47054.
GeneTreeiENSGT00530000063370.
HOGENOMiHOG000074060.
HOVERGENiHBG001328.
InParanoidiP20062.
KOiK14619.
OMAiGEREFWQ.
OrthoDBiEOG79GT6F.
PhylomeDBiP20062.
TreeFamiTF333092.

Enzyme and pathway databases

ReactomeiREACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_169120. Defective TCN2 causes hereditary megaloblastic anemia.
REACT_169178. Defective CD320 causes methylmalonic aciduria.

Miscellaneous databases

EvolutionaryTraceiP20062.
GenomeRNAii6948.
NextBioi27203.
PROiP20062.
SOURCEiSearch...

Gene expression databases

BgeeiP20062.
CleanExiHS_TCN2.
ExpressionAtlasiP20062. baseline and differential.
GenevisibleiP20062. HS.

Family and domain databases

InterProiIPR002157. Cbl-bd_transpt_euk.
IPR027954. DUF4430.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR10559. PTHR10559. 1 hit.
PfamiPF01122. Cobalamin_bind. 1 hit.
PF14478. DUF4430. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
PROSITEiPS00468. COBALAMIN_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The cDNA sequence and the deduced amino acid sequence of human transcobalamin II show homology with rat intrinsic factor and human transcobalamin I."
    Platica O., Janeczko R., Quadros E.V., Regec A., Romain R., Rothenberg S.P.
    J. Biol. Chem. 266:7860-7863(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-198; LEU-219; PRO-259 AND SER-376.
  2. "Isolation and sequence analysis of variant forms of human transcobalamin II."
    Li N., Seetharam S., Lindemans J., Alpers D.H., Arwert F., Seetharam B.
    Biochim. Biophys. Acta 1172:21-30(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The cloning and characterization of the human transcobalamin II gene."
    Regec A., Quadros E.V., Platica O., Rothenberg S.P.
    Blood 85:2711-2719(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-259.
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 2), VARIANT GLN-227.
    Tissue: Brain and Eye.
  7. "Purification and molecular characterization of human transcobalamin II."
    Quadros E.V., Rothenberg S.P., Pan Y.C.E., Stein S.
    J. Biol. Chem. 261:15455-15460(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-37.
  8. "Functional human transcobalamin II isoproteins are secreted by insect cells using the baculovirus expression system."
    Quadros E.V., Sai P., Rothenberg S.P.
    Blood 81:1239-1245(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-26.
  9. "Structural basis for mammalian vitamin B12 transport by transcobalamin."
    Wuerges J., Garau G., Geremia S., Fedosov S.N., Petersen T.E., Randaccio L.
    Proc. Natl. Acad. Sci. U.S.A. 103:4386-4391(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 19-427 IN COMPLEX WITH COBALAMIN, DISULFIDE BONDS.
  10. "Transcobalamin codon 259 polymorphism in HT-29 and Caco-2 cells and in Caucasians: relation to transcobalamin and homocysteine concentration in blood."
    Namour F., Olivier J., Abdelmouttaleb I., Adjalla C., Debard R., Salvat C., Gueant J.
    Blood 97:1092-1098(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRO-259.

Entry informationi

Entry nameiTCO2_HUMAN
AccessioniPrimary (citable) accession number: P20062
Secondary accession number(s): Q96FD4
, Q9BVI8, Q9UCI5, Q9UCI6, Q9UDM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: March 3, 2009
Last modified: July 22, 2015
This is version 160 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 22
    Human chromosome 22: 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.