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O95639

- CPSF4_HUMAN

UniProt

O95639 - CPSF4_HUMAN

Protein

Cleavage and polyadenylation specificity factor subunit 4

Gene

CPSF4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U).2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri35 – 6127C3H1-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri62 – 8928C3H1-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri90 – 11728C3H1-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri118 – 14225C3H1-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri143 – 16927C3H1-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri243 – 26018CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. modification by virus of host mRNA processing Source: Reactome
    2. modulation by virus of host morphology or physiology Source: Reactome
    3. modulation by virus of host process Source: Reactome
    4. mRNA processing Source: UniProtKB-KW
    5. viral life cycle Source: Reactome

    Keywords - Biological processi

    Host-virus interaction, mRNA processing

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_6173. Inhibition of Host mRNA Processing and RNA Silencing.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cleavage and polyadenylation specificity factor subunit 4
    Alternative name(s):
    Cleavage and polyadenylation specificity factor 30 kDa subunit
    Short name:
    CPSF 30 kDa subunit
    NS1 effector domain-binding protein 1
    Short name:
    Neb-1
    No arches homolog
    Gene namesi
    Name:CPSF4
    Synonyms:CPSF30, NAR, NEB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:2327. CPSF4.

    Subcellular locationi

    GO - Cellular componenti

    1. mRNA cleavage and polyadenylation specificity factor complex Source: UniProtKB
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26844.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 269269Cleavage and polyadenylation specificity factor subunit 4PRO_0000074402Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021Phosphoserine2 Publications
    Modified residuei212 – 2121Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO95639.
    PaxDbiO95639.
    PRIDEiO95639.

    PTM databases

    PhosphoSiteiO95639.

    Expressioni

    Gene expression databases

    ArrayExpressiO95639.
    BgeeiO95639.
    CleanExiHS_CPSF4.
    GenevestigatoriO95639.

    Organism-specific databases

    HPAiHPA049094.

    Interactioni

    Subunit structurei

    Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with FIP1L1. Association with influenza A virus NS1 blocks processing of pre-mRNAs, thereby preventing nuclear export of host cell mRNAs.3 Publications

    Protein-protein interaction databases

    BioGridi116104. 9 interactions.
    DIPiDIP-48675N.
    IntActiO95639. 7 interactions.
    MINTiMINT-1429837.
    STRINGi9606.ENSP00000292476.

    Structurei

    Secondary structure

    1
    269
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi69 – 724
    Helixi79 – 813
    Beta strandi82 – 854
    Turni90 – 923
    Helixi97 – 1026
    Beta strandi111 – 1133
    Beta strandi122 – 1254

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D9NNMR-A61-126[»]
    2RHKX-ray1.95C/D61-121[»]
    ProteinModelPortaliO95639.
    SMRiO95639. Positions 61-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95639.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CPSF4/YTH1 family.Curated
    Contains 5 C3H1-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri35 – 6127C3H1-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri62 – 8928C3H1-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri90 – 11728C3H1-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri118 – 14225C3H1-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri143 – 16927C3H1-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri243 – 26018CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5084.
    HOGENOMiHOG000212457.
    HOVERGENiHBG051108.
    InParanoidiO95639.
    KOiK14404.
    OMAiPLDQVTC.
    OrthoDBiEOG7XH6QD.
    PhylomeDBiO95639.
    TreeFamiTF314871.

    Family and domain databases

    Gene3Di4.10.1000.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProiIPR000571. Znf_CCCH.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF00642. zf-CCCH. 2 hits.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view]
    SMARTiSM00343. ZnF_C2HC. 1 hit.
    SM00356. ZnF_C3H1. 5 hits.
    [Graphical view]
    SUPFAMiSSF57756. SSF57756. 1 hit.
    PROSITEiPS50103. ZF_C3H1. 5 hits.
    PS50158. ZF_CCHC. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95639-1) [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

    MQEIIASVDH IKFDLEIAVE QQLGAQPLPF PGMDKSGAAV CEFFLKAACG    50
    KGGMCPFRHI SGEKTVVCKH WLRGLCKKGD QCEFLHEYDM TKMPECYFYS 100
    KFGECSNKEC PFLHIDPESK IKDCPWYDRG FCKHGPLCRH RHTRRVICVN 150
    YLVGFCPEGP SCKFMHPRFE LPMGTTEQPP LPQQTQPPAK QSNNPPLQRS 200
    SSLIQLTSQN SSPNQQRTPQ VIGVMQSQNS SAGNRGPRPL EQVTCYKCGE 250
    KGHYANRCTK GHLAFLSGQ 269
    Length:269
    Mass (Da):30,255
    Last modified:May 1, 1999 - v1
    Checksum:i49444E3EB840464A
    GO
    Isoform 2 (identifier: O95639-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         191-215: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:244
    Mass (Da):27,547
    Checksum:i0DF72BE36CF97106
    GO
    Isoform 3 (identifier: O95639-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         191-216: Missing.

    Note: May be due to a competing acceptor splice site. No experimental confirmation available.

    Show »
    Length:243
    Mass (Da):27,419
    Checksum:i3535FE5A0D525C8F
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei191 – 21626Missing in isoform 3. 1 PublicationVSP_008602Add
    BLAST
    Alternative sequencei191 – 21525Missing in isoform 2. 1 PublicationVSP_008601Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U79569 mRNA. Translation: AAD00321.1.
    CR542161 mRNA. Translation: CAG46958.1.
    EF191081 Genomic DNA. Translation: ABN05292.1.
    CH236956 Genomic DNA. Translation: EAL23878.1.
    CH471091 Genomic DNA. Translation: EAW76667.1.
    CH471091 Genomic DNA. Translation: EAW76668.1.
    BC003101 mRNA. Translation: AAH03101.1.
    BC050738 mRNA. Translation: AAH50738.1.
    CCDSiCCDS47652.1. [O95639-2]
    CCDS5664.1. [O95639-1]
    RefSeqiNP_001075028.1. NM_001081559.1. [O95639-2]
    NP_006684.1. NM_006693.2. [O95639-1]
    UniGeneiHs.489287.

    Genome annotation databases

    EnsembliENST00000292476; ENSP00000292476; ENSG00000160917. [O95639-1]
    ENST00000436336; ENSP00000395311; ENSG00000160917. [O95639-2]
    GeneIDi10898.
    KEGGihsa:10898.
    UCSCiuc003uqi.3. human. [O95639-2]
    uc003uqj.3. human. [O95639-1]
    uc003uqk.3. human. [O95639-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U79569 mRNA. Translation: AAD00321.1 .
    CR542161 mRNA. Translation: CAG46958.1 .
    EF191081 Genomic DNA. Translation: ABN05292.1 .
    CH236956 Genomic DNA. Translation: EAL23878.1 .
    CH471091 Genomic DNA. Translation: EAW76667.1 .
    CH471091 Genomic DNA. Translation: EAW76668.1 .
    BC003101 mRNA. Translation: AAH03101.1 .
    BC050738 mRNA. Translation: AAH50738.1 .
    CCDSi CCDS47652.1. [O95639-2 ]
    CCDS5664.1. [O95639-1 ]
    RefSeqi NP_001075028.1. NM_001081559.1. [O95639-2 ]
    NP_006684.1. NM_006693.2. [O95639-1 ]
    UniGenei Hs.489287.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D9N NMR - A 61-126 [» ]
    2RHK X-ray 1.95 C/D 61-121 [» ]
    ProteinModelPortali O95639.
    SMRi O95639. Positions 61-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116104. 9 interactions.
    DIPi DIP-48675N.
    IntActi O95639. 7 interactions.
    MINTi MINT-1429837.
    STRINGi 9606.ENSP00000292476.

    PTM databases

    PhosphoSitei O95639.

    Proteomic databases

    MaxQBi O95639.
    PaxDbi O95639.
    PRIDEi O95639.

    Protocols and materials databases

    DNASUi 10898.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000292476 ; ENSP00000292476 ; ENSG00000160917 . [O95639-1 ]
    ENST00000436336 ; ENSP00000395311 ; ENSG00000160917 . [O95639-2 ]
    GeneIDi 10898.
    KEGGi hsa:10898.
    UCSCi uc003uqi.3. human. [O95639-2 ]
    uc003uqj.3. human. [O95639-1 ]
    uc003uqk.3. human. [O95639-3 ]

    Organism-specific databases

    CTDi 10898.
    GeneCardsi GC07P099036.
    HGNCi HGNC:2327. CPSF4.
    HPAi HPA049094.
    MIMi 603052. gene.
    neXtProti NX_O95639.
    PharmGKBi PA26844.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5084.
    HOGENOMi HOG000212457.
    HOVERGENi HBG051108.
    InParanoidi O95639.
    KOi K14404.
    OMAi PLDQVTC.
    OrthoDBi EOG7XH6QD.
    PhylomeDBi O95639.
    TreeFami TF314871.

    Enzyme and pathway databases

    Reactomei REACT_6173. Inhibition of Host mRNA Processing and RNA Silencing.

    Miscellaneous databases

    EvolutionaryTracei O95639.
    GeneWikii CPSF4.
    GenomeRNAii 10898.
    NextBioi 41385.
    PROi O95639.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95639.
    Bgeei O95639.
    CleanExi HS_CPSF4.
    Genevestigatori O95639.

    Family and domain databases

    Gene3Di 4.10.1000.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProi IPR000571. Znf_CCCH.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF00642. zf-CCCH. 2 hits.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view ]
    SMARTi SM00343. ZnF_C2HC. 1 hit.
    SM00356. ZnF_C3H1. 5 hits.
    [Graphical view ]
    SUPFAMi SSF57756. SSF57756. 1 hit.
    PROSITEi PS50103. ZF_C3H1. 5 hits.
    PS50158. ZF_CCHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Assignment of the human homolog of the zebrafish essential gene no arches to 7q22.1."
      Kawakami K., Gaiano N., Grosshans D., Scherer S., Tsui L.-C., Hopkins N.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. SeattleSNPs variation discovery resource
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [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] (ISOFORMS 2 AND 3).
      Tissue: Eye and PNS.
    7. "The 30-kD subunit of mammalian cleavage and polyadenylation specificity factor and its yeast homolog are RNA-binding zinc finger proteins."
      Barabino S.M.L., Huebner W., Jenny A., Minvielle-Sebastia L., Keller W.
      Genes Dev. 11:1703-1716(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs."
      Nemeroff M.E., Barabino S.M.L., Li Y., Keller W., Krug R.M.
      Mol. Cell 1:991-1000(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INFLUENZA A VIRUS NS1 PROTEIN.
    9. "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase."
      Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.
      EMBO J. 23:616-626(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRE-MRNA 3'-END PROCESSING, IDENTIFICATION IN THE CPSF COMPLEX, INTERACTION WITH FIP1L1.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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].
    12. "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 SER-202 AND SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA."
      Laishram R.S., Anderson R.A.
      EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CPSF COMPLEX.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Solution structure of CCCH-type zinc-finger domain 2 in cleavage and polyadenylation specificity factor."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 61-126.

    Entry informationi

    Entry nameiCPSF4_HUMAN
    AccessioniPrimary (citable) accession number: O95639
    Secondary accession number(s): D6W5S8
    , Q6FGE6, Q86TF8, Q9BTW6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2003
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 124 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3