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P20062

- TCO2_HUMAN

UniProt

P20062 - TCO2_HUMAN

Protein

Transcobalamin-2

Gene

TCN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (03 Mar 2009)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiP20062.
    BgeeiP20062.
    CleanExiHS_TCN2.
    GenevestigatoriP20062.

    Organism-specific databases

    HPAiHPA000837.

    Interactioni

    Protein-protein interaction databases

    BioGridi112808. 3 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.
    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

    MRHLGAFLFL LGVLGALTEM CEIPEMDSHL VEKLGQHLLP WMDRLSLEHL    50
    NPSIYVGLRL SSLQAGTKED LYLHSLKLGY QQCLLGSAFS EDDGDCQGKP 100
    SMGQLALYLL ALRANCEFVR GHKGDRLVSQ LKWFLEDEKR AIGHDHKGHP 150
    HTSYYQYGLG ILALCLHQKR VHDSVVDKLL YAVEPFHQGH HSVDTAAMAG 200
    LAFTCLKRSN FNPGRRQRIT MAIRTVREEI LKAQTPEGHF GNVYSTPLAL 250
    QFLMTSPMRG AELGTACLKA RVALLASLQD GAFQNALMIS QLLPVLNHKT 300
    YIDLIFPDCL APRVMLEPAA ETIPQTQEII SVTLQVLSLL PPYRQSISVL 350
    AGSTVEDVLK KAHELGGFTY ETQASLSGPY LTSVMGKAAG EREFWQLLRD 400
    PNTPLLQGIA DYRPKDGETI ELRLVSW 427
    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. 3 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.
    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

    ArrayExpressi P20062.
    Bgeei P20062.
    CleanExi HS_TCN2.
    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

    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 1, 2014
    This is version 152 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