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Q15361

- TTF1_HUMAN

UniProt

Q15361 - TTF1_HUMAN

Protein

Transcription termination factor 1

Gene

TTF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity.1 Publication

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. chromatin remodeling Source: Ensembl
    2. DNA-templated transcription, termination Source: UniProtKB
    3. gene expression Source: Reactome
    4. negative regulation of DNA replication Source: UniProtKB-KW
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. termination of RNA polymerase I transcription Source: Reactome
    7. transcription from RNA polymerase I promoter Source: Reactome
    8. transcription initiation from RNA polymerase I promoter Source: Ensembl

    Keywords - Molecular functioni

    DNA replication inhibitor

    Keywords - Biological processi

    Transcription, Transcription regulation, Transcription termination

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_953. RNA Polymerase I Transcription Initiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription termination factor 1
    Short name:
    TTF-1
    Alternative name(s):
    RNA polymerase I termination factor
    Transcription termination factor I
    Short name:
    TTF-I
    Gene namesi
    Name:TTF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:12397. TTF1.

    Subcellular locationi

    Nucleus. Nucleusnucleolus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleolus Source: HPA
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37062.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 905905Transcription termination factor 1PRO_0000250472Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei65 – 651Phosphoserine2 Publications
    Modified residuei240 – 2401Phosphoserine1 Publication
    Modified residuei403 – 4031Phosphoserine1 Publication
    Modified residuei476 – 4761Phosphotyrosine1 Publication
    Modified residuei478 – 4781Phosphoserine1 Publication
    Modified residuei481 – 4811Phosphoserine3 Publications
    Modified residuei487 – 4871Phosphoserine4 Publications
    Modified residuei872 – 8721Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15361.
    PaxDbiQ15361.
    PRIDEiQ15361.

    PTM databases

    PhosphoSiteiQ15361.

    Expressioni

    Gene expression databases

    BgeeiQ15361.
    CleanExiHS_TTF1.
    GenevestigatoriQ15361.

    Organism-specific databases

    HPAiCAB053633.
    HPA051105.
    HPA054837.

    Interactioni

    Subunit structurei

    Oligomer. The oligomeric structure enables to interact simultaneously with two separate DNA fragments. Interacts with BAZ2A/TIP5.

    Protein-protein interaction databases

    BioGridi113121. 9 interactions.
    IntActiQ15361. 2 interactions.
    MINTiMINT-1181965.
    STRINGi9606.ENSP00000333920.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15361.
    SMRiQ15361. Positions 613-667.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini612 – 66150Myb-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini661 – 74585Myb-like 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 223223N-terminal region (NRD)By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi17 – 215Poly-Lys
    Compositional biasi216 – 22510Poly-Lys
    Compositional biasi272 – 28211Poly-LysAdd
    BLAST
    Compositional biasi329 – 33810Poly-Lys

    Domaini

    The N-terminal region (NRD) inhibits DNA-binding via its interaction with the C-terminal region.By similarity

    Sequence similaritiesi

    Contains 2 Myb-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG262979.
    HOGENOMiHOG000231811.
    HOVERGENiHBG104803.
    InParanoidiQ15361.
    KOiK15225.
    OMAiDYLYETT.
    OrthoDBiEOG7ZKS9N.
    PhylomeDBiQ15361.
    TreeFamiTF333537.

    Family and domain databases

    Gene3Di1.10.10.60. 2 hits.
    InterProiIPR009057. Homeodomain-like.
    IPR017877. Myb-like_dom.
    IPR001005. SANT/Myb.
    [Graphical view]
    SMARTiSM00717. SANT. 2 hits.
    [Graphical view]
    PROSITEiPS50090. MYB_LIKE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q15361-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGESSRFEI HTPVSDKKKK KCSIHKERPQ KHSHEIFRDS SLVNEQSQIT    50
    RRKKRKKDFQ HLISSPLKKS RICDETANAT STLKKRKKRR YSALEVDEEA 100
    GVTVVLVDKE NINNTPKHFR KDVDVVCVDM SIEQKLPRKP KTDKFQVLAK 150
    SHAHKSEALH SKVREKKNKK HQRKAASWES QRARDTLPQS ESHQEESWLS 200
    VGPGGEITEL PASAHKNKSK KKKKKSSNRE YETLAMPEGS QAGREAGTDM 250
    QESQPTVGLD DETPQLLGPT HKKKSKKKKK KKSNHQEFEA LAMPEGSQVG 300
    SEVGADMQES RPAVGLHGET AGIPAPAYKN KSKKKKKKSN HQEFEAVAMP 350
    ESLESAYPEG SQVGSEVGTV EGSTALKGFK ESNSTKKKSK KRKLTSVKRA 400
    RVSGDDFSVP SKNSESTLFD SVEGDGAMME EGVKSRPRQK KTQACLASKH 450
    VQEAPRLEPA NEEHNVETAE DSEIRYLSAD SGDADDSDAD LGSAVKQLQE 500
    FIPNIKDRAT STIKRMYRDD LERFKEFKAQ GVAIKFGKFS VKENKQLEKN 550
    VEDFLALTGI ESADKLLYTD RYPEEKSVIT NLKRRYSFRL HIGRNIARPW 600
    KLIYYRAKKM FDVNNYKGRY SEGDTEKLKM YHSLLGNDWK TIGEMVARSS 650
    LSVALKFSQI SSQRNRGAWS KSETRKLIKA VEEVILKKMS PQELKEVDSK 700
    LQENPESCLS IVREKLYKGI SWVEVEAKVQ TRNWMQCKSK WTEILTKRMT 750
    NGRRIYYGMN ALRAKVSLIE RLYEINVEDT NEIDWEDLAS AIGDVPPSYV 800
    QTKFSRLKAV YVPFWQKKTF PEIIDYLYET TLPLLKEKLE KMMEKKGTKI 850
    QTPAAPKQVF PFRDIFYYED DSEGEDIEKE SEGQAPCMAH ACNSSTLGGQ 900
    GRWII 905
    Length:905
    Mass (Da):103,051
    Last modified:September 11, 2007 - v3
    Checksum:i12F829CEFDDF96E8
    GO

    Sequence cautioni

    The sequence AAH62692.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAI04640.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAI27670.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
    The sequence AAI27671.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
    The sequence AAI43049.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
    The sequence AAI43050.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
    The sequence CAA58807.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.
    The sequence CAA58807.1 differs from that shown. Reason: Frameshift at position 875.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti281 – 2811K → T in AAH50734. (PubMed:15489334)Curated
    Sequence conflicti649 – 6491S → R in CAA58807. (PubMed:7597036)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351E → K.1 Publication
    Corresponds to variant rs11550314 [ dbSNP | Ensembl ].
    VAR_027563
    Natural varianti290 – 2901A → S.
    Corresponds to variant rs8999 [ dbSNP | Ensembl ].
    VAR_027564
    Natural varianti303 – 3031V → A.
    Corresponds to variant rs3739914 [ dbSNP | Ensembl ].
    VAR_027565
    Natural varianti360 – 3601G → V.
    Corresponds to variant rs3739915 [ dbSNP | Ensembl ].
    VAR_027566
    Natural varianti401 – 4011R → Q.
    Corresponds to variant rs3739916 [ dbSNP | Ensembl ].
    VAR_027567
    Natural varianti473 – 4731E → K.
    Corresponds to variant rs12336746 [ dbSNP | Ensembl ].
    VAR_050201
    Natural varianti885 – 8851A → V.
    Corresponds to variant rs1752676 [ dbSNP | Ensembl ].
    VAR_061363

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83973 mRNA. Translation: CAA58807.1. Sequence problems.
    AL353701 Genomic DNA. Translation: CAI94997.2.
    BC050734 mRNA. Translation: AAH50734.1.
    BC062692 mRNA. Translation: AAH62692.1. Sequence problems.
    BC104639 mRNA. Translation: AAI04640.1. Sequence problems.
    BC127669 mRNA. Translation: AAI27670.1. Sequence problems.
    BC127670 mRNA. Translation: AAI27671.1. Sequence problems.
    BC143048 mRNA. Translation: AAI43049.1. Sequence problems.
    BC143049 mRNA. Translation: AAI43050.1. Sequence problems.
    CCDSiCCDS6948.1.
    PIRiI38182.
    RefSeqiNP_001192225.1. NM_001205296.1.
    NP_031370.2. NM_007344.3.
    UniGeneiHs.54780.
    Hs.732733.

    Genome annotation databases

    EnsembliENST00000334270; ENSP00000333920; ENSG00000125482.
    GeneIDi7270.
    KEGGihsa:7270.
    UCSCiuc004cbl.3. human.

    Polymorphism databases

    DMDMi158518534.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83973 mRNA. Translation: CAA58807.1 . Sequence problems.
    AL353701 Genomic DNA. Translation: CAI94997.2 .
    BC050734 mRNA. Translation: AAH50734.1 .
    BC062692 mRNA. Translation: AAH62692.1 . Sequence problems.
    BC104639 mRNA. Translation: AAI04640.1 . Sequence problems.
    BC127669 mRNA. Translation: AAI27670.1 . Sequence problems.
    BC127670 mRNA. Translation: AAI27671.1 . Sequence problems.
    BC143048 mRNA. Translation: AAI43049.1 . Sequence problems.
    BC143049 mRNA. Translation: AAI43050.1 . Sequence problems.
    CCDSi CCDS6948.1.
    PIRi I38182.
    RefSeqi NP_001192225.1. NM_001205296.1.
    NP_031370.2. NM_007344.3.
    UniGenei Hs.54780.
    Hs.732733.

    3D structure databases

    ProteinModelPortali Q15361.
    SMRi Q15361. Positions 613-667.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113121. 9 interactions.
    IntActi Q15361. 2 interactions.
    MINTi MINT-1181965.
    STRINGi 9606.ENSP00000333920.

    PTM databases

    PhosphoSitei Q15361.

    Polymorphism databases

    DMDMi 158518534.

    Proteomic databases

    MaxQBi Q15361.
    PaxDbi Q15361.
    PRIDEi Q15361.

    Protocols and materials databases

    DNASUi 7270.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334270 ; ENSP00000333920 ; ENSG00000125482 .
    GeneIDi 7270.
    KEGGi hsa:7270.
    UCSCi uc004cbl.3. human.

    Organism-specific databases

    CTDi 7270.
    GeneCardsi GC09M135250.
    H-InvDB HIX0201412.
    HGNCi HGNC:12397. TTF1.
    HPAi CAB053633.
    HPA051105.
    HPA054837.
    MIMi 600777. gene.
    neXtProti NX_Q15361.
    PharmGKBi PA37062.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262979.
    HOGENOMi HOG000231811.
    HOVERGENi HBG104803.
    InParanoidi Q15361.
    KOi K15225.
    OMAi DYLYETT.
    OrthoDBi EOG7ZKS9N.
    PhylomeDBi Q15361.
    TreeFami TF333537.

    Enzyme and pathway databases

    Reactomei REACT_1074. RNA Polymerase I Transcription Termination.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_953. RNA Polymerase I Transcription Initiation.

    Miscellaneous databases

    GeneWikii Transcription_termination_factor,_RNA_polymerase_I.
    GenomeRNAii 7270.
    NextBioi 28421.
    PROi Q15361.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15361.
    CleanExi HS_TTF1.
    Genevestigatori Q15361.

    Family and domain databases

    Gene3Di 1.10.10.60. 2 hits.
    InterProi IPR009057. Homeodomain-like.
    IPR017877. Myb-like_dom.
    IPR001005. SANT/Myb.
    [Graphical view ]
    SMARTi SM00717. SANT. 2 hits.
    [Graphical view ]
    PROSITEi PS50090. MYB_LIKE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular evolution of mammalian ribosomal gene terminator sequences and the transcription termination factor TTF-1."
      Evers R., Grummt I.
      Proc. Natl. Acad. Sci. U.S.A. 92:5827-5831(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] OF 1-338 AND 457-905, VARIANT LYS-35.
      Tissue: Uterus.
    4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-403; SER-481 AND SER-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-476; SER-481 AND SER-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-487 AND SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-481; SER-487 AND SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTTF1_HUMAN
    AccessioniPrimary (citable) accession number: Q15361
    Secondary accession number(s): A1L160
    , Q4VXF3, Q58EY2, Q6P5T5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 120 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3