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P78396

- CCNA1_HUMAN

UniProt

P78396 - CCNA1_HUMAN

Protein

Cyclin-A1

Gene

CCNA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    May be involved in the control of the cell cycle at the G1/S (start) and G2/M (mitosis) transitions. May primarily function in the control of the germline meiotic cell cycle and additionally in the control of mitotic cell cycle in some somatic cells.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. G1/S transition of mitotic cell cycle Source: Reactome
    2. G2/M transition of mitotic cell cycle Source: Reactome
    3. male meiosis I Source: ProtInc
    4. mitotic cell cycle Source: Reactome
    5. mitotic nuclear division Source: UniProtKB-KW
    6. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
    7. regulation of G2/M transition of mitotic cell cycle Source: InterPro
    8. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
    9. spermatogenesis Source: ProtInc

    Keywords - Molecular functioni

    Cyclin

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_111214. G0 and Early G1.
    REACT_1156. Orc1 removal from chromatin.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_1915. G2 Phase.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_6362. Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
    REACT_683. G1/S-Specific Transcription.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
    SignaLinkiP78396.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-A1
    Gene namesi
    Name:CCNA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:1577. CCNA1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: ProtInc
    2. microtubule cytoskeleton Source: LIFEdb
    3. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26147.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465Cyclin-A1PRO_0000080333Add
    BLAST

    Post-translational modificationi

    Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. Deubiquitinated and stabilized by USP37 enables entry into S phase.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiP78396.
    PaxDbiP78396.
    PRIDEiP78396.

    Expressioni

    Tissue specificityi

    Very high levels in testis and very low levels in brain. Also found in myeloid leukemia cell lines.

    Developmental stagei

    Expression increases in early G1 phase and reaches highest levels during the S and G2/M phases.

    Gene expression databases

    ArrayExpressiP78396.
    BgeeiP78396.
    CleanExiHS_CCNA1.
    GenevestigatoriP78396.

    Interactioni

    Subunit structurei

    Interacts with the CDK2 and the CDC2 protein kinases to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex. Does not bind CDK4 and CDK5 (in vitro). The cyclin A1-CDK2 complex interacts with transcription factor E2F-1 and RB proteins. Found in a complex with CDK2, CABLES1 and CCNE1 By similarity. Interacts with INCA1 and KLHDC9.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDKN1AP389363EBI-375065,EBI-375077

    Protein-protein interaction databases

    BioGridi114417. 54 interactions.
    IntActiP78396. 10 interactions.
    MINTiMINT-104479.
    STRINGi9606.ENSP00000255465.

    Structurei

    3D structure databases

    ProteinModelPortaliP78396.
    SMRiP78396. Positions 210-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi388 – 3914Poly-Ala

    Sequence similaritiesi

    Belongs to the cyclin family. Cyclin AB subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG5024.
    HOGENOMiHOG000167672.
    HOVERGENiHBG106244.
    InParanoidiP78396.
    KOiK06627.
    OMAiAEIRHRP.
    OrthoDBiEOG7G7KQ0.
    PhylomeDBiP78396.
    TreeFamiTF101002.

    Family and domain databases

    Gene3Di1.10.472.10. 2 hits.
    InterProiIPR013763. Cyclin-like.
    IPR014400. Cyclin_A/B/D/E/F.
    IPR015453. Cyclin_A_chordates.
    IPR004367. Cyclin_C-dom.
    IPR006671. Cyclin_N.
    [Graphical view]
    PANTHERiPTHR10177:SF68. PTHR10177:SF68. 1 hit.
    PfamiPF02984. Cyclin_C. 1 hit.
    PF00134. Cyclin_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001771. Cyclin_A_B_D_E. 1 hit.
    SMARTiSM00385. CYCLIN. 2 hits.
    [Graphical view]
    SUPFAMiSSF47954. SSF47954. 2 hits.
    PROSITEiPS00292. CYCLINS. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P78396-1) [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

    METGFPAIMY PGSFIGGWGE EYLSWEGPGL PDFVFQQQPV ESEAMHCSNP    50
    KSGVVLATVA RGPDACQILT RAPLGQDPPQ RTVLGLLTAN GQYRRTCGQG 100
    ITRIRCYSGS ENAFPPAGKK ALPDCGVQEP PKQGFDIYMD ELEQGDRDSC 150
    SVREGMAFED VYEVDTGTLK SDLHFLLDFN TVSPMLVDSS LLSQSEDISS 200
    LGTDVINVTE YAEEIYQYLR EAEIRHRPKA HYMKKQPDIT EGMRTILVDW 250
    LVEVGEEYKL RAETLYLAVN FLDRFLSCMS VLRGKLQLVG TAAMLLASKY 300
    EEIYPPEVDE FVYITDDTYT KRQLLKMEHL LLKVLAFDLT VPTTNQFLLQ 350
    YLRRQGVCVR TENLAKYVAE LSLLEADPFL KYLPSLIAAA AFCLANYTVN 400
    KHFWPETLAA FTGYSLSEIV PCLSELHKAY LDIPHRPQQA IREKYKASKY 450
    LCVSLMEPPA VLLLQ 465
    Length:465
    Mass (Da):52,358
    Last modified:May 1, 1997 - v1
    Checksum:iC9C023EEA1CF036D
    GO
    Isoform 2 (identifier: P78396-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         38-38: Missing.

    Show »
    Length:464
    Mass (Da):52,230
    Checksum:iE67C6E6D741B7D73
    GO
    Isoform 3 (identifier: P78396-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-44: Missing.

    Show »
    Length:421
    Mass (Da):47,494
    Checksum:i33F2BA565699105C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 475EAMHC → SS in AAV38384. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4444Missing in isoform 3. 1 PublicationVSP_044257Add
    BLAST
    Alternative sequencei38 – 381Missing in isoform 2. 1 PublicationVSP_034392

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66838 mRNA. Translation: AAB49754.1.
    BT019577 mRNA. Translation: AAV38384.1.
    AK301897 mRNA. Translation: BAH13579.1.
    AK316392 mRNA. Translation: BAH14763.1.
    AL359767 Genomic DNA. Translation: CAI12728.1.
    CH471075 Genomic DNA. Translation: EAX08565.1.
    CH471075 Genomic DNA. Translation: EAX08566.1.
    BC036346 mRNA. Translation: AAH36346.1.
    U97680 mRNA. Translation: AAB60863.1.
    CCDSiCCDS45030.1. [P78396-2]
    CCDS45031.1. [P78396-3]
    CCDS9357.1. [P78396-1]
    RefSeqiNP_001104515.1. NM_001111045.1. [P78396-2]
    NP_001104516.1. NM_001111046.1. [P78396-3]
    NP_001104517.1. NM_001111047.1. [P78396-3]
    NP_003905.1. NM_003914.3. [P78396-1]
    UniGeneiHs.417050.

    Genome annotation databases

    EnsembliENST00000255465; ENSP00000255465; ENSG00000133101. [P78396-1]
    ENST00000440264; ENSP00000400666; ENSG00000133101. [P78396-3]
    GeneIDi8900.
    KEGGihsa:8900.
    UCSCiuc001uvr.4. human. [P78396-1]
    uc001uvs.4. human. [P78396-2]

    Polymorphism databases

    DMDMi8134359.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66838 mRNA. Translation: AAB49754.1 .
    BT019577 mRNA. Translation: AAV38384.1 .
    AK301897 mRNA. Translation: BAH13579.1 .
    AK316392 mRNA. Translation: BAH14763.1 .
    AL359767 Genomic DNA. Translation: CAI12728.1 .
    CH471075 Genomic DNA. Translation: EAX08565.1 .
    CH471075 Genomic DNA. Translation: EAX08566.1 .
    BC036346 mRNA. Translation: AAH36346.1 .
    U97680 mRNA. Translation: AAB60863.1 .
    CCDSi CCDS45030.1. [P78396-2 ]
    CCDS45031.1. [P78396-3 ]
    CCDS9357.1. [P78396-1 ]
    RefSeqi NP_001104515.1. NM_001111045.1. [P78396-2 ]
    NP_001104516.1. NM_001111046.1. [P78396-3 ]
    NP_001104517.1. NM_001111047.1. [P78396-3 ]
    NP_003905.1. NM_003914.3. [P78396-1 ]
    UniGenei Hs.417050.

    3D structure databases

    ProteinModelPortali P78396.
    SMRi P78396. Positions 210-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114417. 54 interactions.
    IntActi P78396. 10 interactions.
    MINTi MINT-104479.
    STRINGi 9606.ENSP00000255465.

    Chemistry

    BindingDBi P78396.
    ChEMBLi CHEMBL2094128.

    Polymorphism databases

    DMDMi 8134359.

    Proteomic databases

    MaxQBi P78396.
    PaxDbi P78396.
    PRIDEi P78396.

    Protocols and materials databases

    DNASUi 8900.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000255465 ; ENSP00000255465 ; ENSG00000133101 . [P78396-1 ]
    ENST00000440264 ; ENSP00000400666 ; ENSG00000133101 . [P78396-3 ]
    GeneIDi 8900.
    KEGGi hsa:8900.
    UCSCi uc001uvr.4. human. [P78396-1 ]
    uc001uvs.4. human. [P78396-2 ]

    Organism-specific databases

    CTDi 8900.
    GeneCardsi GC13P037005.
    HGNCi HGNC:1577. CCNA1.
    MIMi 604036. gene.
    neXtProti NX_P78396.
    PharmGKBi PA26147.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5024.
    HOGENOMi HOG000167672.
    HOVERGENi HBG106244.
    InParanoidi P78396.
    KOi K06627.
    OMAi AEIRHRP.
    OrthoDBi EOG7G7KQ0.
    PhylomeDBi P78396.
    TreeFami TF101002.

    Enzyme and pathway databases

    Reactomei REACT_111214. G0 and Early G1.
    REACT_1156. Orc1 removal from chromatin.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_1915. G2 Phase.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_6362. Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
    REACT_683. G1/S-Specific Transcription.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
    SignaLinki P78396.

    Miscellaneous databases

    GeneWikii Cyclin_A1.
    GenomeRNAii 8900.
    NextBioi 33435.
    PROi P78396.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78396.
    Bgeei P78396.
    CleanExi HS_CCNA1.
    Genevestigatori P78396.

    Family and domain databases

    Gene3Di 1.10.472.10. 2 hits.
    InterProi IPR013763. Cyclin-like.
    IPR014400. Cyclin_A/B/D/E/F.
    IPR015453. Cyclin_A_chordates.
    IPR004367. Cyclin_C-dom.
    IPR006671. Cyclin_N.
    [Graphical view ]
    PANTHERi PTHR10177:SF68. PTHR10177:SF68. 1 hit.
    Pfami PF02984. Cyclin_C. 1 hit.
    PF00134. Cyclin_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001771. Cyclin_A_B_D_E. 1 hit.
    SMARTi SM00385. CYCLIN. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 2 hits.
    PROSITEi PS00292. CYCLINS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a second human cyclin A that is highly expressed in testis and in several leukemic cell lines."
      Yang R., Morosetti R., Koeffler H.P.
      Cancer Res. 57:913-920(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Myeloid.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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] (ISOFORM 2).
      Tissue: Brain.
    7. "The human testes cyclin A1 disrupts growth and DNA damage response of a yeast replication mutant."
      Perkins E.L., Wood V.J., Sterling J.F., Hashem V.I., Resnick M.A.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 55-465.
      Tissue: Testis.
    8. "Functions of cyclin A1 in the cell cycle and its interactions with transcription factor E2F-1 and the Rb family of proteins."
      Yang R., Mueller C., Huynh V., Fung Y.K., Yee A.S., Koeffler H.P.
      Mol. Cell. Biol. 19:2400-2407(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. Cited for: INTERACTION WITH INCA1 AND KLHDC9.
    10. "Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry."
      Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G., Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.
      Mol. Cell 42:511-523(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP37.

    Entry informationi

    Entry nameiCCNA1_HUMAN
    AccessioniPrimary (citable) accession number: P78396
    Secondary accession number(s): B7Z7E3
    , Q5T3V0, Q5U0G2, Q8IY91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 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 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3