Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P30086

- PEBP1_HUMAN

UniProt

P30086 - PEBP1_HUMAN

Protein

Phosphatidylethanolamine-binding protein 1

Gene

PEBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase By similarity. Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation.By similarity1 Publication
    HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor By similarity.By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. enzyme binding Source: UniProtKB
    3. phosphatidylethanolamine binding Source: ProtInc
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein kinase binding Source: UniProtKB
    7. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiP30086.

    Protein family/group databases

    MEROPSiI51.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylethanolamine-binding protein 1
    Short name:
    PEBP-1
    Alternative name(s):
    HCNPpp
    Neuropolypeptide h3
    Prostatic-binding protein
    Raf kinase inhibitor protein
    Short name:
    RKIP
    Cleaved into the following chain:
    Gene namesi
    Name:PEBP1
    Synonyms:PBP, PEBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:8630. PEBP1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32968.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 187186Phosphatidylethanolamine-binding protein 1PRO_0000023271Add
    BLAST
    Peptidei2 – 1211Hippocampal cholinergic neurostimulating peptidePRO_0000023272Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei42 – 421Phosphothreonine1 Publication
    Modified residuei52 – 521Phosphoserine4 Publications

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP30086.
    PaxDbiP30086.
    PeptideAtlasiP30086.
    PRIDEiP30086.

    2D gel databases

    DOSAC-COBS-2DPAGEP30086.
    OGPiP30086.
    REPRODUCTION-2DPAGEIPI00219446.
    P30086.
    SWISS-2DPAGEP30086.
    UCD-2DPAGEP30086.

    PTM databases

    PhosphoSiteiP30086.

    Expressioni

    Gene expression databases

    ArrayExpressiP30086.
    BgeeiP30086.
    CleanExiHS_PEBP1.
    GenevestigatoriP30086.

    Organism-specific databases

    HPAiCAB009906.
    CAB013493.
    HPA008819.

    Interactioni

    Subunit structurei

    Has a tendency to form dimers by disulfide cross-linking By similarity. Interacts with RAF1 and this interaction is enhanced if RAF1 is phosphorylated on residues 'Ser-338', 'Ser-339', 'Tyr-340' and 'Tyr-341'. Interacts with ALOX15; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAF1P040497EBI-716384,EBI-365996

    Protein-protein interaction databases

    BioGridi111076. 17 interactions.
    DIPiDIP-44269N.
    IntActiP30086. 8 interactions.
    MINTiMINT-5002544.
    STRINGi9606.ENSP00000261313.

    Structurei

    Secondary structure

    1
    187
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 73
    Turni8 – 125
    Helixi14 – 163
    Beta strandi22 – 243
    Beta strandi26 – 283
    Beta strandi32 – 343
    Turni43 – 464
    Beta strandi51 – 544
    Beta strandi62 – 7110
    Beta strandi76 – 783
    Beta strandi84 – 9310
    Helixi97 – 993
    Beta strandi100 – 1045
    Beta strandi118 – 12912
    Beta strandi140 – 1423
    Turni144 – 1463
    Helixi151 – 1577
    Beta strandi164 – 1718
    Helixi177 – 1837
    Turni184 – 1863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BD9X-ray2.05A/B1-187[»]
    1BEHX-ray1.75A/B1-187[»]
    2L7WNMR-A1-187[»]
    2QYQX-ray1.95A1-187[»]
    ProteinModelPortaliP30086.
    SMRiP30086. Positions 3-186.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30086.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni93 – 13442Interaction with RAF1Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1881.
    HOGENOMiHOG000237655.
    HOVERGENiHBG008165.
    InParanoidiP30086.
    OMAiNDVSSGC.
    OrthoDBiEOG7P02K3.
    PhylomeDBiP30086.
    TreeFamiTF315074.

    Family and domain databases

    Gene3Di3.90.280.10. 1 hit.
    InterProiIPR001858. Phosphotidylethanolamine-bd_CS.
    IPR008914. PtdEtn-bd_prot_PEBP.
    [Graphical view]
    PfamiPF01161. PBP. 1 hit.
    [Graphical view]
    SUPFAMiSSF49777. SSF49777. 1 hit.
    PROSITEiPS01220. PBP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P30086-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPVDLSKWSG PLSLQEVDEQ PQHPLHVTYA GAAVDELGKV LTPTQVKNRP    50
    TSISWDGLDS GKLYTLVLTD PDAPSRKDPK YREWHHFLVV NMKGNDISSG 100
    TVLSDYVGSG PPKGTGLHRY VWLVYEQDRP LKCDEPILSN RSGDHRGKFK 150
    VASFRKKYEL RAPVAGTCYQ AEWDDYVPKL YEQLSGK 187
    Length:187
    Mass (Da):21,057
    Last modified:January 23, 2007 - v3
    Checksum:iF1E9F17E2CD11C36
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81W → K(PubMed:7637590)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91S → N.
    VAR_006048

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16111 mRNA. Translation: BAA03684.1.
    X75252 mRNA. Translation: CAA53031.1.
    X85033 mRNA. Translation: CAA59404.1.
    AK311927 mRNA. Translation: BAG34868.1.
    CH471054 Genomic DNA. Translation: EAW98122.1.
    BC008714 mRNA. Translation: AAH08714.1.
    BC017396 mRNA. Translation: AAH17396.1.
    BC031102 mRNA. Translation: AAH31102.1.
    S76773 mRNA. Translation: AAD14234.1.
    CCDSiCCDS9187.1.
    PIRiI53745.
    RefSeqiNP_002558.1. NM_002567.2.
    UniGeneiHs.433863.

    Genome annotation databases

    EnsembliENST00000261313; ENSP00000261313; ENSG00000089220.
    GeneIDi5037.
    KEGGihsa:5037.
    UCSCiuc001twu.1. human.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16111 mRNA. Translation: BAA03684.1 .
    X75252 mRNA. Translation: CAA53031.1 .
    X85033 mRNA. Translation: CAA59404.1 .
    AK311927 mRNA. Translation: BAG34868.1 .
    CH471054 Genomic DNA. Translation: EAW98122.1 .
    BC008714 mRNA. Translation: AAH08714.1 .
    BC017396 mRNA. Translation: AAH17396.1 .
    BC031102 mRNA. Translation: AAH31102.1 .
    S76773 mRNA. Translation: AAD14234.1 .
    CCDSi CCDS9187.1.
    PIRi I53745.
    RefSeqi NP_002558.1. NM_002567.2.
    UniGenei Hs.433863.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BD9 X-ray 2.05 A/B 1-187 [» ]
    1BEH X-ray 1.75 A/B 1-187 [» ]
    2L7W NMR - A 1-187 [» ]
    2QYQ X-ray 1.95 A 1-187 [» ]
    ProteinModelPortali P30086.
    SMRi P30086. Positions 3-186.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111076. 17 interactions.
    DIPi DIP-44269N.
    IntActi P30086. 8 interactions.
    MINTi MINT-5002544.
    STRINGi 9606.ENSP00000261313.

    Protein family/group databases

    MEROPSi I51.002.

    PTM databases

    PhosphoSitei P30086.

    2D gel databases

    DOSAC-COBS-2DPAGE P30086.
    OGPi P30086.
    REPRODUCTION-2DPAGE IPI00219446.
    P30086.
    SWISS-2DPAGE P30086.
    UCD-2DPAGE P30086.

    Proteomic databases

    MaxQBi P30086.
    PaxDbi P30086.
    PeptideAtlasi P30086.
    PRIDEi P30086.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261313 ; ENSP00000261313 ; ENSG00000089220 .
    GeneIDi 5037.
    KEGGi hsa:5037.
    UCSCi uc001twu.1. human.

    Organism-specific databases

    CTDi 5037.
    GeneCardsi GC12P118573.
    HGNCi HGNC:8630. PEBP1.
    HPAi CAB009906.
    CAB013493.
    HPA008819.
    MIMi 604591. gene.
    neXtProti NX_P30086.
    PharmGKBi PA32968.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1881.
    HOGENOMi HOG000237655.
    HOVERGENi HBG008165.
    InParanoidi P30086.
    OMAi NDVSSGC.
    OrthoDBi EOG7P02K3.
    PhylomeDBi P30086.
    TreeFami TF315074.

    Enzyme and pathway databases

    SignaLinki P30086.

    Miscellaneous databases

    ChiTaRSi PEBP1. human.
    EvolutionaryTracei P30086.
    GeneWikii Phosphatidylethanolamine_binding_protein_1.
    GenomeRNAii 5037.
    NextBioi 19408.
    PROi P30086.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30086.
    Bgeei P30086.
    CleanExi HS_PEBP1.
    Genevestigatori P30086.

    Family and domain databases

    Gene3Di 3.90.280.10. 1 hit.
    InterProi IPR001858. Phosphotidylethanolamine-bd_CS.
    IPR008914. PtdEtn-bd_prot_PEBP.
    [Graphical view ]
    Pfami PF01161. PBP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49777. SSF49777. 1 hit.
    PROSITEi PS01220. PBP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human cDNA sequence homologue of bovine phosphatidylethanolamine-binding protein."
      Hori N., Keon-Sang C., Murakawa K., Matoba R., Fukushima A., Okubo K., Matsubara K.
      Gene 140:293-294(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein."
      Tohdoh N., Tojo S., Agui H., Ojika K.
      Brain Res. Mol. Brain Res. 30:381-384(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    3. Hall L.
      Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    4. "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].
      Tissue: Cerebellum.
    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].
      Tissue: Brain, Hypothalamus and Lung.
    7. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11.
      Tissue: Liver.
    8. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 8-39; 48-77; 81-113; 120-141 AND 162-187, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    9. "Amino acid sequence of the Homo sapiens brain 21-23-kDa protein (neuropolypeptide h3), comparison with its counterparts from Rattus norvegicus and Bos taurus species, and expression of its mRNA in different tissues."
      Seddiqi N., Bollengier F., Alliel P.M., Perin J.-P., Bonnet F., Bucquoy S., Jolles P., Schoentgen F.
      J. Mol. Evol. 39:655-660(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-187.
      Tissue: Brain.
    10. Cited for: CHARACTERIZATION OF HCNP.
    11. Cited for: INTERACTION WITH RAF-1.
    12. "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.
    13. "The RKIP (Raf-1 Kinase Inhibitor Protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK."
      Rath O., Park S., Tang H.H., Banfield M.J., Brady R.L., Lee Y.C., Dignam J.D., Sedivy J.M., Kolch W., Yeung K.C.
      Cell. Signal. 20:935-941(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAF1.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 AND SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells."
      Zhao J., O'Donnell V.B., Balzar S., St Croix C.M., Trudeau J.B., Wenzel S.E.
      Proc. Natl. Acad. Sci. U.S.A. 108:14246-14251(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALOX15.
    19. "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-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction."
      Banfield M.J., Barker J.J., Perry A.C., Brady R.L.
      Structure 6:1245-1254(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).

    Entry informationi

    Entry nameiPEBP1_HUMAN
    AccessioniPrimary (citable) accession number: P30086
    Secondary accession number(s): B2R4S1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 156 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3