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Q9UQR1

- ZN148_HUMAN

UniProt

Q9UQR1 - ZN148_HUMAN

Protein

Zinc finger protein 148

Gene

ZNF148

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (24 Jan 2001)
      Previous versions | rss
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    Functioni

    Involved in transcriptional regulation. Represses the transcription of a number of genes including gastrin, stromelysin and enolase. Binds to the G-rich box in the enhancer region of these genes.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri171 – 19323C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri199 – 22123C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri227 – 24923C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri255 – 27824C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. double-stranded DNA binding Source: Ensembl
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. sequence-specific DNA binding Source: UniProtKB
    5. sequence-specific DNA binding transcription factor activity Source: Ensembl
    6. transcription regulatory region sequence-specific DNA binding Source: Ensembl

    GO - Biological processi

    1. cellular defense response Source: ProtInc
    2. gamete generation Source: Ensembl
    3. negative regulation of gene expression Source: UniProtKB
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
    6. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    7. protein complex assembly Source: Ensembl
    8. substantia nigra development Source: UniProt
    9. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ9UQR1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger protein 148
    Alternative name(s):
    Transcription factor ZBP-89
    Zinc finger DNA-binding protein 89
    Gene namesi
    Name:ZNF148
    Synonyms:ZBP89
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:12933. ZNF148.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37520.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 794794Zinc finger protein 148PRO_0000047427Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941Phosphothreonine1 Publication
    Modified residuei250 – 2501Phosphoserine1 Publication
    Modified residuei306 – 3061Phosphoserine4 Publications
    Modified residuei412 – 4121Phosphoserine1 Publication
    Modified residuei607 – 6071N6-acetyllysine1 Publication
    Modified residuei665 – 6651Phosphoserine1 Publication
    Modified residuei784 – 7841Phosphoserine3 Publications

    Post-translational modificationi

    Sumoylated with SUMO2. Desumoylated by SENP3, resulting in the stimulation of transcription of its target genes By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UQR1.
    PaxDbiQ9UQR1.
    PRIDEiQ9UQR1.

    PTM databases

    PhosphoSiteiQ9UQR1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UQR1.
    BgeeiQ9UQR1.
    CleanExiHS_ZNF148.
    GenevestigatoriQ9UQR1.

    Organism-specific databases

    HPAiCAB017486.
    HPA001656.

    Interactioni

    Subunit structurei

    Interacts with HNRNPDL. Interacts with the 5FMC complex; the interaction requires association with CHTOP.1 Publication

    Protein-protein interaction databases

    BioGridi113501. 13 interactions.
    IntActiQ9UQR1. 4 interactions.
    STRINGi9606.ENSP00000353863.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UQR1.
    SMRiQ9UQR1. Positions 138-324, 350-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Contains 4 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri171 – 19323C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri199 – 22123C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri227 – 24923C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri255 – 27824C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOGENOMiHOG000293204.
    HOVERGENiHBG054247.
    InParanoidiQ9UQR1.
    OMAiNDAYLNN.
    OrthoDBiEOG76QFGM.
    PhylomeDBiQ9UQR1.
    TreeFamiTF331779.

    Family and domain databases

    Gene3Di3.30.160.60. 4 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 4 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UQR1-1) [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

    MNIDDKLEGL FLKCGGIDEM QSSRTMVVMG GVSGQSTVSG ELQDSVLQDR    50
    SMPHQEILAA DEVLQESEMR QQDMISHDEL MVHEETVKND EEQMETHERL 100
    PQGLQYALNV PISVKQEITF TDVSEQLMRD KKQIREPVDL QKKKKRKQRS 150
    PAKILTINED GSLGLKTPKS HVCEHCNAAF RTNYHLQRHV FIHTGEKPFQ 200
    CSQCDMRFIQ KYLLQRHEKI HTGEKPFRCD ECGMRFIQKY HMERHKRTHS 250
    GEKPYQCEYC LQYFSRTDRV LKHKRMCHEN HDKKLNRCAI KGGLLTSEED 300
    SGFSTSPKDN SLPKKKRQKT EKKSSGMDKE SALDKSDLKK DKNDYLPLYS 350
    SSTKVKDEYM VAEYAVEMPH SSVGGSHLED ASGEIHPPKL VLKKINSKRS 400
    LKQPLEQNQT ISPLSTYEES KVSKYAFELV DKQALLDSEG NADIDQVDNL 450
    QEGPSKPVHS STNYDDAMQF LKKKRYLQAA SNNSREYALN VGTIASQPSV 500
    TQAAVASVID ESTTASILES QALNVEIKSN HDKNVIPDEV LQTLLDHYSH 550
    KANGQHEISF SVADTEVTSS ISINSSEVPE VTPSENVGSS SQASSSDKAN 600
    MLQEYSKFLQ QALDRTSQND AYLNSPSLNF VTDNQTLPNQ PAFSSIDKQV 650
    YATMPINSFR SGMNSPLRTT PDKSHFGLIV GDSQHSFPFS GDETNHASAT 700
    STQDFLDQVT SQKKAEAQPV HQAYQMSSFE QPFRAPYHGS RAGIATQFST 750
    ANGQVNLRGP GTSAEFSEFP LVNVNDNRAG MTSSPDATTG QTFG 794
    Length:794
    Mass (Da):88,976
    Last modified:January 24, 2001 - v2
    Checksum:i50413723459EBD1F
    GO
    Isoform 2 (identifier: Q9UQR1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-205: Missing.
         233-690: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:131
    Mass (Da):14,473
    Checksum:iCD38D10B58EE1E1E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti287 – 2871R → T in CAA15422. (PubMed:10359087)Curated
    Sequence conflicti348 – 3481L → V in CAA15422. (PubMed:10359087)Curated
    Sequence conflicti379 – 3791E → K in AAB57692. 1 PublicationCurated
    Sequence conflicti495 – 4951A → R in CAA15422. (PubMed:10359087)Curated
    Sequence conflicti616 – 6161T → N in AAB57692. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 205205Missing in isoform 2. 1 PublicationVSP_055938Add
    BLAST
    Alternative sequencei233 – 690458Missing in isoform 2. 1 PublicationVSP_055939Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039019 mRNA. Translation: AAC39926.1.
    AJ236885 mRNA. Translation: CAA15422.1.
    AC108688 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79394.1.
    CH471052 Genomic DNA. Translation: EAW79395.1.
    CH471052 Genomic DNA. Translation: EAW79396.1.
    CH471052 Genomic DNA. Translation: EAW79398.1.
    BC018971 mRNA. Translation: AAH18971.1.
    BC050260 mRNA. Translation: AAH50260.1.
    U96633 Genomic DNA. Translation: AAB57692.1.
    CCDSiCCDS3031.1.
    RefSeqiNP_068799.2. NM_021964.2.
    UniGeneiHs.592591.

    Genome annotation databases

    EnsembliENST00000360647; ENSP00000353863; ENSG00000163848.
    ENST00000484491; ENSP00000420335; ENSG00000163848.
    ENST00000485866; ENSP00000420448; ENSG00000163848.
    ENST00000492394; ENSP00000419322; ENSG00000163848.
    ENST00000544464; ENSP00000437916; ENSG00000163848.
    GeneIDi7707.
    KEGGihsa:7707.
    UCSCiuc003ehx.4. human.

    Polymorphism databases

    DMDMi12643385.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039019 mRNA. Translation: AAC39926.1 .
    AJ236885 mRNA. Translation: CAA15422.1 .
    AC108688 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79394.1 .
    CH471052 Genomic DNA. Translation: EAW79395.1 .
    CH471052 Genomic DNA. Translation: EAW79396.1 .
    CH471052 Genomic DNA. Translation: EAW79398.1 .
    BC018971 mRNA. Translation: AAH18971.1 .
    BC050260 mRNA. Translation: AAH50260.1 .
    U96633 Genomic DNA. Translation: AAB57692.1 .
    CCDSi CCDS3031.1.
    RefSeqi NP_068799.2. NM_021964.2.
    UniGenei Hs.592591.

    3D structure databases

    ProteinModelPortali Q9UQR1.
    SMRi Q9UQR1. Positions 138-324, 350-385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113501. 13 interactions.
    IntActi Q9UQR1. 4 interactions.
    STRINGi 9606.ENSP00000353863.

    PTM databases

    PhosphoSitei Q9UQR1.

    Polymorphism databases

    DMDMi 12643385.

    Proteomic databases

    MaxQBi Q9UQR1.
    PaxDbi Q9UQR1.
    PRIDEi Q9UQR1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360647 ; ENSP00000353863 ; ENSG00000163848 .
    ENST00000484491 ; ENSP00000420335 ; ENSG00000163848 .
    ENST00000485866 ; ENSP00000420448 ; ENSG00000163848 .
    ENST00000492394 ; ENSP00000419322 ; ENSG00000163848 .
    ENST00000544464 ; ENSP00000437916 ; ENSG00000163848 .
    GeneIDi 7707.
    KEGGi hsa:7707.
    UCSCi uc003ehx.4. human.

    Organism-specific databases

    CTDi 7707.
    GeneCardsi GC03M124944.
    HGNCi HGNC:12933. ZNF148.
    HPAi CAB017486.
    HPA001656.
    MIMi 601897. gene.
    neXtProti NX_Q9UQR1.
    PharmGKBi PA37520.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000293204.
    HOVERGENi HBG054247.
    InParanoidi Q9UQR1.
    OMAi NDAYLNN.
    OrthoDBi EOG76QFGM.
    PhylomeDBi Q9UQR1.
    TreeFami TF331779.

    Enzyme and pathway databases

    SignaLinki Q9UQR1.

    Miscellaneous databases

    GeneWikii ZNF148.
    GenomeRNAii 7707.
    NextBioi 29880.
    PROi Q9UQR1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UQR1.
    Bgeei Q9UQR1.
    CleanExi HS_ZNF148.
    Genevestigatori Q9UQR1.

    Family and domain databases

    Gene3Di 3.30.160.60. 4 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 4 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 4 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human ZBP-89 homolog, located at chromosome 3q21, represses gastrin gene expression."
      Law D.J., Tarle S.A., Merchant J.L.
      Mamm. Genome 9:165-167(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Human stromelysin gene promoter activity is modulated by transcription factor ZBP-89."
      Ye S., Whatling C., Watkins H., Henney A.
      FEBS Lett. 450:268-272(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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).
      Tissue: B-cell and Kidney.
    6. "The growth-regulating transcription factor ZBP-89 is located at human chromosome 3q21 and mouse chromosome 8B1."
      Law D.J., Chen X.N., Korenberg J.R., Mortensen E.R., Merchant J.L.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-665.
    7. "Regulation of murine cytochrome c oxidase Vb gene expression during myogenesis: YY-1 and heterogeneous nuclear ribonucleoprotein D-like protein (JKTBP1) reciprocally regulate transcription activity by physical interaction with the BERF-1/ZBP-89 factor."
      Boopathi E., Lenka N., Prabu S.K., Fang J.-K., Wilkinson F., Atchison M., Giallongo A., Avadhani N.G.
      J. Biol. Chem. 279:35242-35254(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HNRNPDL.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-194; SER-250; SER-306; SER-412 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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].
    11. "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-306 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-607, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-306; SER-665 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiZN148_HUMAN
    AccessioniPrimary (citable) accession number: Q9UQR1
    Secondary accession number(s): D3DN27
    , O00389, O43591, Q58EY5, Q6PJ98
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: January 24, 2001
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 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 3
      Human chromosome 3: 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