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P68402

- PA1B2_HUMAN

UniProt

P68402 - PA1B2_HUMAN

Protein

Platelet-activating factor acetylhydrolase IB subunit beta

Gene

PAFAH1B2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      Previous versions | rss
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    Functioni

    Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit.

    Catalytic activityi

    1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei48 – 481By similarity
    Active sitei193 – 1931By similarity
    Active sitei196 – 1961By similarity

    GO - Molecular functioni

    1. 1-alkyl-2-acetylglycerophosphocholine esterase activity Source: UniProtKB-EC

    GO - Biological processi

    1. brain development Source: Ensembl
    2. lipid catabolic process Source: UniProtKB-KW
    3. lipid metabolic process Source: ProtInc
    4. positive regulation of macroautophagy Source: BHF-UCL
    5. spermatogenesis Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet-activating factor acetylhydrolase IB subunit beta (EC:3.1.1.47)
    Alternative name(s):
    PAF acetylhydrolase 30 kDa subunit
    Short name:
    PAF-AH 30 kDa subunit
    PAF-AH subunit beta
    Short name:
    PAFAH subunit beta
    Gene namesi
    Name:PAFAH1B2
    Synonyms:PAFAHB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:8575. PAFAH1B2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. nucleolus Source: HPA
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32906.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 229228Platelet-activating factor acetylhydrolase IB subunit betaPRO_0000058151Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei2 – 21Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP68402.
    PaxDbiP68402.
    PeptideAtlasiP68402.
    PRIDEiP68402.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00026546.

    PTM databases

    PhosphoSiteiP68402.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiP68402.
    BgeeiP68402.
    CleanExiHS_PAFAH1B2.
    GenevestigatoriP68402.

    Organism-specific databases

    HPAiHPA051836.

    Interactioni

    Subunit structurei

    Cytosolic PAF-AH IB is formed of three subunits of 45 kDa (alpha), 30 kDa (beta) and 29 kDa (gamma). The catalytic activity of the enzyme resides in the beta and gamma subunits, whereas the alpha subunit has regulatory activity. Trimer formation is not essential for the catalytic activity.

    Protein-protein interaction databases

    BioGridi111086. 37 interactions.
    IntActiP68402. 15 interactions.
    MINTiMINT-5002700.
    STRINGi9606.ENSP00000304006.

    Structurei

    Secondary structure

    1
    229
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 103
    Beta strandi19 – 213
    Helixi23 – 3715
    Beta strandi41 – 477
    Helixi48 – 536
    Helixi57 – 626
    Helixi64 – 663
    Beta strandi68 – 725
    Helixi78 – 869
    Turni87 – 904
    Beta strandi96 – 1016
    Helixi111 – 12818
    Beta strandi133 – 1375
    Beta strandi143 – 1453
    Helixi148 – 16316
    Beta strandi164 – 1674
    Beta strandi170 – 1734
    Turni188 – 1903
    Beta strandi194 – 1974
    Helixi199 – 21921

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VYHX-ray3.40A/B/E/F/I/J/M/N/Q/R1-229[»]
    ProteinModelPortaliP68402.
    SMRiP68402. Positions 6-217.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68402.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG69837.
    HOGENOMiHOG000232143.
    HOVERGENiHBG053477.
    InParanoidiP68402.
    KOiK16795.
    OMAiNIRPKVV.
    OrthoDBiEOG7HB5BS.
    PhylomeDBiP68402.
    TreeFamiTF323955.

    Family and domain databases

    Gene3Di3.40.50.1110. 1 hit.
    InterProiIPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P68402-1) [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

    MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV    50
    QLMQQYEIWR ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV 100
    WVGTNNHENT AEEVAGGIEA IVQLINTRQP QAKIIVLGLL PRGEKPNPLR 150
    QKNAKVNQLL KVSLPKLANV QLLDTDGGFV HSDGAISCHD MFDFLHLTGG 200
    GYAKICKPLH ELIMQLLEET PEEKQTTIA 229
    Length:229
    Mass (Da):25,569
    Last modified:November 23, 2004 - v1
    Checksum:i14CF5D48621AA504
    GO
    Isoform 2 (identifier: P68402-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         138-229: GLLPRGEKPN...TPEEKQTTIA → IIYWQDEQDYHERKVQMD

    Show »
    Length:155
    Mass (Da):17,833
    Checksum:iA4AF3D6025CD9E43
    GO
    Isoform 3 (identifier: P68402-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         133-229: Missing.

    Show »
    Length:132
    Mass (Da):14,888
    Checksum:i6663DB0A3B3202D7
    GO
    Isoform 4 (identifier: P68402-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         139-229: LLPRGEKPNP...TPEEKQTTIA → KAAASKYSIS...KSRWTEEILH

    Show »
    Length:202
    Mass (Da):22,734
    Checksum:i07A9CD88A4B99B35
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 4 (identifier: P68402-4)
    Sequence conflicti151 – 1511V → M in ABI58227. (PubMed:18155631)Curated
    Sequence conflicti151 – 1511V → M in ABI58228. (PubMed:18155631)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei133 – 22997Missing in isoform 3. 1 PublicationVSP_043217Add
    BLAST
    Alternative sequencei138 – 22992GLLPR…QTTIA → IIYWQDEQDYHERKVQMD in isoform 2. 1 PublicationVSP_042896Add
    BLAST
    Alternative sequencei139 – 22991LLPRG…QTTIA → KAAASKYSISEIVRLEQGSV NWSIGTYPDDTPATTRPAIL QLFTGKMSRITMKEKSRWTE EILH in isoform 4. 1 PublicationVSP_044680Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63390 mRNA. Translation: BAA19917.1.
    DQ836738 mRNA. Translation: ABI58225.1.
    DQ836739 mRNA. Translation: ABI58226.1.
    DQ836740 mRNA. Translation: ABI58227.1.
    DQ836741 mRNA. Translation: ABI58228.1.
    DQ836742 mRNA. Translation: ABI58229.1.
    DQ836743 mRNA. Translation: ABI58230.1.
    AK292973 mRNA. Translation: BAF85662.1.
    CR456736 mRNA. Translation: CAG33017.1.
    EF445007 Genomic DNA. Translation: ACA06040.1.
    AP005018 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67281.1.
    BC000398 mRNA. Translation: AAH00398.1.
    BC019301 mRNA. Translation: AAH19301.1.
    CCDSiCCDS53713.1. [P68402-3]
    CCDS53714.1. [P68402-4]
    CCDS53715.1. [P68402-2]
    CCDS8380.1. [P68402-1]
    PIRiJC5409.
    RefSeqiNP_001171675.1. NM_001184746.1. [P68402-4]
    NP_001171676.1. NM_001184747.1. [P68402-2]
    NP_001171677.1. NM_001184748.1. [P68402-3]
    NP_002563.1. NM_002572.3. [P68402-1]
    UniGeneiHs.728488.

    Genome annotation databases

    EnsembliENST00000419197; ENSP00000388742; ENSG00000168092. [P68402-3]
    ENST00000527958; ENSP00000435289; ENSG00000168092. [P68402-1]
    ENST00000529887; ENSP00000434951; ENSG00000168092. [P68402-2]
    ENST00000530272; ENSP00000431365; ENSG00000168092. [P68402-4]
    GeneIDi5049.
    KEGGihsa:5049.
    UCSCiuc001pqe.2. human. [P68402-1]
    uc009yzk.2. human. [P68402-2]

    Polymorphism databases

    DMDMi55977294.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63390 mRNA. Translation: BAA19917.1 .
    DQ836738 mRNA. Translation: ABI58225.1 .
    DQ836739 mRNA. Translation: ABI58226.1 .
    DQ836740 mRNA. Translation: ABI58227.1 .
    DQ836741 mRNA. Translation: ABI58228.1 .
    DQ836742 mRNA. Translation: ABI58229.1 .
    DQ836743 mRNA. Translation: ABI58230.1 .
    AK292973 mRNA. Translation: BAF85662.1 .
    CR456736 mRNA. Translation: CAG33017.1 .
    EF445007 Genomic DNA. Translation: ACA06040.1 .
    AP005018 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67281.1 .
    BC000398 mRNA. Translation: AAH00398.1 .
    BC019301 mRNA. Translation: AAH19301.1 .
    CCDSi CCDS53713.1. [P68402-3 ]
    CCDS53714.1. [P68402-4 ]
    CCDS53715.1. [P68402-2 ]
    CCDS8380.1. [P68402-1 ]
    PIRi JC5409.
    RefSeqi NP_001171675.1. NM_001184746.1. [P68402-4 ]
    NP_001171676.1. NM_001184747.1. [P68402-2 ]
    NP_001171677.1. NM_001184748.1. [P68402-3 ]
    NP_002563.1. NM_002572.3. [P68402-1 ]
    UniGenei Hs.728488.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VYH X-ray 3.40 A/B/E/F/I/J/M/N/Q/R 1-229 [» ]
    ProteinModelPortali P68402.
    SMRi P68402. Positions 6-217.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111086. 37 interactions.
    IntActi P68402. 15 interactions.
    MINTi MINT-5002700.
    STRINGi 9606.ENSP00000304006.

    Chemistry

    ChEMBLi CHEMBL4463.

    PTM databases

    PhosphoSitei P68402.

    Polymorphism databases

    DMDMi 55977294.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00026546.

    Proteomic databases

    MaxQBi P68402.
    PaxDbi P68402.
    PeptideAtlasi P68402.
    PRIDEi P68402.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000419197 ; ENSP00000388742 ; ENSG00000168092 . [P68402-3 ]
    ENST00000527958 ; ENSP00000435289 ; ENSG00000168092 . [P68402-1 ]
    ENST00000529887 ; ENSP00000434951 ; ENSG00000168092 . [P68402-2 ]
    ENST00000530272 ; ENSP00000431365 ; ENSG00000168092 . [P68402-4 ]
    GeneIDi 5049.
    KEGGi hsa:5049.
    UCSCi uc001pqe.2. human. [P68402-1 ]
    uc009yzk.2. human. [P68402-2 ]

    Organism-specific databases

    CTDi 5049.
    GeneCardsi GC11P117014.
    H-InvDB HIX0022939.
    HGNCi HGNC:8575. PAFAH1B2.
    HPAi HPA051836.
    MIMi 602508. gene.
    neXtProti NX_P68402.
    PharmGKBi PA32906.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG69837.
    HOGENOMi HOG000232143.
    HOVERGENi HBG053477.
    InParanoidi P68402.
    KOi K16795.
    OMAi NIRPKVV.
    OrthoDBi EOG7HB5BS.
    PhylomeDBi P68402.
    TreeFami TF323955.

    Miscellaneous databases

    ChiTaRSi PAFAH1B2. human.
    EvolutionaryTracei P68402.
    GeneWikii PAFAH1B2.
    GenomeRNAii 5049.
    NextBioi 19456.
    PROi P68402.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P68402.
    Bgeei P68402.
    CleanExi HS_PAFAH1B2.
    Genevestigatori P68402.

    Family and domain databases

    Gene3Di 3.40.50.1110. 1 hit.
    InterProi IPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Differential tissue distribution of the beta- and gamma-subunits of human cytosolic platelet-activating factor acetylhydrolase (isoform I)."
      Adachi H., Tsujimoto M., Hattori M., Arai H., Inoue K.
      Biochem. Biophys. Res. Commun. 233:10-13(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Fetal liver.
    2. "Novel isoforms of intracellular platelet activating factor acetylhydrolase (PAFAH1b2) in human testis; encoded by alternatively spliced mRNAs."
      Scott B.T., Olson N., Long G.L., Bovill E.G.
      Prostaglandins Other Lipid Mediat. 85:69-80(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE SPLICING.
      Tissue: Testis.
    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 1).
      Tissue: Trachea.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. NHLBI resequencing and genotyping service (RS&G)
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 1).
      Tissue: Lung.
    9. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 61-79, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "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 SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPA1B2_HUMAN
    AccessioniPrimary (citable) accession number: P68402
    Secondary accession number(s): A8DPS5
    , A8DPS6, A8DPS7, E9PEJ5, E9PLP3, O00687, Q29459, Q6IBR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 113 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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