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Q6ZN18

- AEBP2_HUMAN

UniProt

Q6ZN18 - AEBP2_HUMAN

Protein

Zinc finger protein AEBP2

Gene

AEBP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    DNA-binding transcriptional repressor. May interact with and stimulate the activity of the PRC2 complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri261 – 28626C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri300 – 32223C2H2-type 2; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri328 – 35225C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. transcription corepressor activity Source: Ensembl

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200808. PRC2 methylates histones and DNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger protein AEBP2
    Alternative name(s):
    Adipocyte enhancer-binding protein 2
    Short name:
    AE-binding protein 2
    Gene namesi
    Name:AEBP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:24051. AEBP2.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. ESC/E(Z) complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134875401.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 517516Zinc finger protein AEBP2PRO_0000341590Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei18 – 181Phosphoserine2 Publications
    Modified residuei24 – 241Phosphoserine2 Publications
    Modified residuei206 – 2061Phosphoserine3 Publications
    Modified residuei210 – 2101Phosphoserine1 Publication
    Modified residuei211 – 2111Phosphoserine1 Publication
    Modified residuei390 – 3901Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6ZN18.
    PaxDbiQ6ZN18.
    PRIDEiQ6ZN18.

    PTM databases

    PhosphoSiteiQ6ZN18.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6ZN18.
    BgeeiQ6ZN18.
    CleanExiHS_AEBP2.
    GenevestigatoriQ6ZN18.

    Organism-specific databases

    HPAiHPA020893.
    HPA022282.

    Interactioni

    Subunit structurei

    Self-associates. Interacts with EED, EZH2, RBBP4 and SUZ12. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2 By similarity. May also interact with RBBP7.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi125736. 14 interactions.
    DIPiDIP-58581N.
    IntActiQ6ZN18. 3 interactions.
    MINTiMINT-1439056.
    STRINGi9606.ENSP00000381840.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZN18.
    SMRiQ6ZN18. Positions 261-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni209 – 29486Interaction with RBBP4Add
    BLAST
    Regioni353 – 517165Interaction with SUZ12Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi34 – 12390Glu-richAdd
    BLAST
    Compositional biasi61 – 205145Gly-richAdd
    BLAST
    Compositional biasi110 – 256147Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri261 – 28626C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri300 – 32223C2H2-type 2; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri328 – 35225C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG291563.
    HOGENOMiHOG000033826.
    InParanoidiQ6ZN18.
    KOiK17452.
    OMAiQTXVIAK.
    PhylomeDBiQ6ZN18.
    TreeFamiTF328864.

    Family and domain databases

    Gene3Di3.30.160.60. 2 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 3 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
    PS50157. ZINC_FINGER_C2H2_2. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6ZN18-1) [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

    MAAAITDMAD LEELSRLSPL PPGSPGSAAR GRAEPPEEEE EEEEEEEEAE    50
    AEAVAALLLN GGSGGGGGGG GGGVGGGEAE TMSEPSPESA SQAGEDEDEE 100
    EDDEEEEDES SSSGGGEEES SAESLVGSSG GSSSDETRSL SPGAASSSSG 150
    DGDGKEGLEE PKGPRGSQGG GGGGSSSSSV VSSGGDEGYG TGGGGSSATS 200
    GGRRGSLEMS SDGEPLSRMD SEDSISSTIM DVDSTISSGR STPAMMNGQG 250
    STTSSSKNIA YNCCWDQCQA CFNSSPDLAD HIRSIHVDGQ RGGVFVCLWK 300
    GCKVYNTPST SQSWLQRHML THSGDKPFKC VVGGCNASFA SQGGLARHVP 350
    THFSQQNSSK VSSQPKAKEE SPSKAGMNKR RKLKNKRRRS LPRPHDFFDA 400
    QTLDAIRHRA ICFNLSAHIE SLGKGHSVVF HSTVIAKRKE DSGKIKLLLH 450
    WMPEDILPDV WVNESERHQL KTKVVHLSKL PKDTALLLDP NIYRTMPQKR 500
    LKRTLIRKVF NLYLSKQ 517
    Length:517
    Mass (Da):54,467
    Last modified:June 10, 2008 - v2
    Checksum:i6C59888ACEE4F9AF
    GO
    Isoform 2 (identifier: Q6ZN18-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         504-517: Missing.

    Show »
    Length:503
    Mass (Da):52,761
    Checksum:i032090A790243D07
    GO
    Isoform 3 (identifier: Q6ZN18-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-216: Missing.
         217-223: SRMDSED → MYTRRYS

    Show »
    Length:301
    Mass (Da):33,981
    Checksum:iDD766CAAB61DADB3
    GO

    Sequence cautioni

    The sequence AAH15624.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH22220.1 differs from that shown. Reason: Erroneous initiation.
    The sequence EAW96400.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD18513.1 differs from that shown. Reason: Erroneous termination at position 269. Translated as Gln.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 216216Missing in isoform 3. 1 PublicationVSP_034357Add
    BLAST
    Alternative sequencei217 – 2237SRMDSED → MYTRRYS in isoform 3. 1 PublicationVSP_034358
    Alternative sequencei504 – 51714Missing in isoform 2. 1 PublicationVSP_034359Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK131361 mRNA. Translation: BAD18513.1. Sequence problems.
    AK131410 mRNA. Translation: BAD18557.1.
    CH471094 Genomic DNA. Translation: EAW96400.1. Different initiation.
    BC015624 mRNA. Translation: AAH15624.1. Different initiation.
    BC022220 mRNA. Translation: AAH22220.1. Different initiation.
    AB209384 mRNA. Translation: BAD92621.1.
    CCDSiCCDS44841.1. [Q6ZN18-1]
    CCDS44842.1. [Q6ZN18-2]
    CCDS58215.1. [Q6ZN18-3]
    RefSeqiNP_001107648.1. NM_001114176.1. [Q6ZN18-1]
    NP_001253972.1. NM_001267043.1. [Q6ZN18-3]
    NP_694939.2. NM_153207.4. [Q6ZN18-2]
    UniGeneiHs.126497.

    Genome annotation databases

    EnsembliENST00000266508; ENSP00000266508; ENSG00000139154. [Q6ZN18-2]
    ENST00000360995; ENSP00000354267; ENSG00000139154. [Q6ZN18-3]
    ENST00000398864; ENSP00000381840; ENSG00000139154. [Q6ZN18-1]
    GeneIDi121536.
    KEGGihsa:121536.
    UCSCiuc001ree.2. human. [Q6ZN18-1]
    uc001reg.2. human. [Q6ZN18-3]

    Polymorphism databases

    DMDMi190358163.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK131361 mRNA. Translation: BAD18513.1 . Sequence problems.
    AK131410 mRNA. Translation: BAD18557.1 .
    CH471094 Genomic DNA. Translation: EAW96400.1 . Different initiation.
    BC015624 mRNA. Translation: AAH15624.1 . Different initiation.
    BC022220 mRNA. Translation: AAH22220.1 . Different initiation.
    AB209384 mRNA. Translation: BAD92621.1 .
    CCDSi CCDS44841.1. [Q6ZN18-1 ]
    CCDS44842.1. [Q6ZN18-2 ]
    CCDS58215.1. [Q6ZN18-3 ]
    RefSeqi NP_001107648.1. NM_001114176.1. [Q6ZN18-1 ]
    NP_001253972.1. NM_001267043.1. [Q6ZN18-3 ]
    NP_694939.2. NM_153207.4. [Q6ZN18-2 ]
    UniGenei Hs.126497.

    3D structure databases

    ProteinModelPortali Q6ZN18.
    SMRi Q6ZN18. Positions 261-388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125736. 14 interactions.
    DIPi DIP-58581N.
    IntActi Q6ZN18. 3 interactions.
    MINTi MINT-1439056.
    STRINGi 9606.ENSP00000381840.

    PTM databases

    PhosphoSitei Q6ZN18.

    Polymorphism databases

    DMDMi 190358163.

    Proteomic databases

    MaxQBi Q6ZN18.
    PaxDbi Q6ZN18.
    PRIDEi Q6ZN18.

    Protocols and materials databases

    DNASUi 121536.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266508 ; ENSP00000266508 ; ENSG00000139154 . [Q6ZN18-2 ]
    ENST00000360995 ; ENSP00000354267 ; ENSG00000139154 . [Q6ZN18-3 ]
    ENST00000398864 ; ENSP00000381840 ; ENSG00000139154 . [Q6ZN18-1 ]
    GeneIDi 121536.
    KEGGi hsa:121536.
    UCSCi uc001ree.2. human. [Q6ZN18-1 ]
    uc001reg.2. human. [Q6ZN18-3 ]

    Organism-specific databases

    CTDi 121536.
    GeneCardsi GC12P019556.
    HGNCi HGNC:24051. AEBP2.
    HPAi HPA020893.
    HPA022282.
    neXtProti NX_Q6ZN18.
    PharmGKBi PA134875401.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291563.
    HOGENOMi HOG000033826.
    InParanoidi Q6ZN18.
    KOi K17452.
    OMAi QTXVIAK.
    PhylomeDBi Q6ZN18.
    TreeFami TF328864.

    Enzyme and pathway databases

    Reactomei REACT_200808. PRC2 methylates histones and DNA.

    Miscellaneous databases

    ChiTaRSi AEBP2. human.
    GenomeRNAii 121536.
    NextBioi 80766.
    PROi Q6ZN18.

    Gene expression databases

    ArrayExpressi Q6ZN18.
    Bgeei Q6ZN18.
    CleanExi HS_AEBP2.
    Genevestigatori Q6ZN18.

    Family and domain databases

    Gene3Di 3.30.160.60. 2 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 3 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 2 hits.
    PS50157. ZINC_FINGER_C2H2_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORMS 1 AND 3).
      Tissue: Teratocarcinoma and Uterus.
    2. 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] (ISOFORM 2).
      Tissue: Eye and Uterus.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-517 (ISOFORM 1).
      Tissue: Brain.
    5. "Role of histone H3 lysine 27 methylation in Polycomb-group silencing."
      Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y.
      Science 298:1039-1043(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EED; EZH2; RBBP4; RBBP7 AND SUZ12.
    6. "SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex."
      Cao R., Zhang Y.
      Mol. Cell 15:57-67(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH EED; EZH2; RBBP4 AND SUZ12.
    7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-210 AND SER-211, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-24 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-206 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAEBP2_HUMAN
    AccessioniPrimary (citable) accession number: Q6ZN18
    Secondary accession number(s): Q59FS5, Q6ZN62, Q96BG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 91 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3