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P20062

- TCO2_HUMAN

UniProt

P20062 - TCO2_HUMAN

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Protein

Transcobalamin-2

Gene

TCN2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. cobalamin binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cobalamin metabolic process Source: RefGenome
  2. cobalamin transport Source: ProtInc
  3. cobalt ion transport Source: UniProtKB-KW
  4. small molecule metabolic process Source: Reactome
  5. vitamin metabolic process Source: Reactome
  6. water-soluble vitamin metabolic process Source: Reactome
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: Chromosome 22

Organism-specific databases

HGNCiHGNC:11653. TCN2.

Subcellular locationi

GO - Cellular componenti

  1. endosome Source: Reactome
  2. extracellular region Source: Reactome
  3. extracellular space Source: ProtInc
  4. extracellular vesicular exosome Source: UniProt
  5. lysosomal lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Transcobalamin II deficiency (TCN2 deficiency) [MIM:275350]: Results in various forms of anemia.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi275350. phenotype.
Orphaneti859. Transcobalamin deficiency.
PharmGKBiPA36404.

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.
GenevestigatoriP20062.

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 – 3811
Helixi39 – 435
Turni47 – 493
Helixi52 – 598
Beta strandi61 – 644
Helixi67 – 8418
Helixi102 – 11413
Helixi122 – 14221
Helixi154 – 16613
Helixi173 – 18311
Helixi192 – 20716
Turni208 – 2103
Helixi213 – 2153
Helixi216 – 23217
Beta strandi240 – 2423
Turni243 – 2453
Helixi246 – 2538
Helixi262 – 27817
Turni279 – 2813
Helixi286 – 2927
Helixi295 – 2973
Helixi301 – 3044
Beta strandi329 – 3368
Beta strandi338 – 3414
Beta strandi343 – 3508
Helixi355 – 36511
Beta strandi370 – 3734
Beta strandi380 – 3845
Beta strandi391 – 3999
Turni400 – 4023
Turni409 – 4113
Beta strandi418 – 4269

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiGHKGDRL.
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. Align

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:
EMBL
GenBank
DDBJ
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. [P20062-1]
ENST00000407817; ENSP00000384914; ENSG00000185339. [P20062-2]
GeneIDi6948.
KEGGihsa:6948.
UCSCiuc003aip.2. human. [P20062-1]
uc003air.2. human. [P20062-2]

Polymorphism databases

DMDMi224471876.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

TCN2base

TCN2 mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS13881.1. [P20062-1 ]
CCDS54519.1. [P20062-2 ]
PIRi A39744.
RefSeqi NP_000346.2. NM_000355.3. [P20062-1 ]
NP_001171655.1. NM_001184726.1. [P20062-2 ]
UniGenei Hs.417948.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BB5 X-ray 3.20 A/B 19-427 [» ]
ProteinModelPortali P20062.
SMRi P20062. Positions 19-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112808. 4 interactions.
IntActi P20062. 2 interactions.
STRINGi 9606.ENSP00000215838.

Chemistry

DrugBanki DB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.

PTM databases

PhosphoSitei P20062.

Polymorphism databases

DMDMi 224471876.

Proteomic databases

PaxDbi P20062.
PRIDEi P20062.

Protocols and materials databases

DNASUi 6948.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000215838 ; ENSP00000215838 ; ENSG00000185339 . [P20062-1 ]
ENST00000407817 ; ENSP00000384914 ; ENSG00000185339 . [P20062-2 ]
GeneIDi 6948.
KEGGi hsa:6948.
UCSCi uc003aip.2. human. [P20062-1 ]
uc003air.2. human. [P20062-2 ]

Organism-specific databases

CTDi 6948.
GeneCardsi GC22P031002.
HGNCi HGNC:11653. TCN2.
HPAi HPA000837.
MIMi 275350. phenotype.
613441. gene.
neXtProti NX_P20062.
Orphaneti 859. Transcobalamin deficiency.
PharmGKBi PA36404.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG47054.
GeneTreei ENSGT00530000063370.
HOGENOMi HOG000074060.
HOVERGENi HBG001328.
InParanoidi P20062.
KOi K14619.
OMAi GHKGDRL.
OrthoDBi EOG79GT6F.
PhylomeDBi P20062.
TreeFami TF333092.

Enzyme and pathway databases

Reactomei REACT_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

EvolutionaryTracei P20062.
GenomeRNAii 6948.
NextBioi 27203.
PROi P20062.
SOURCEi Search...

Gene expression databases

Bgeei P20062.
CleanExi HS_TCN2.
ExpressionAtlasi P20062. baseline and differential.
Genevestigatori P20062.

Family and domain databases

InterProi IPR002157. Cbl-bd_transpt_euk.
IPR027954. DUF4430.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view ]
PANTHERi PTHR10559. PTHR10559. 1 hit.
Pfami PF01122. Cobalamin_bind. 1 hit.
PF14478. DUF4430. 1 hit.
[Graphical view ]
SUPFAMi SSF48239. SSF48239. 1 hit.
PROSITEi PS00468. COBALAMIN_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 153 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