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Protein

Cytosolic phospholipase A2 beta

Gene

PLA2G4B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position with a preference for arachidonoyl phospholipids. Has a much weaker activity than PLA2G4A. Isoform 3 has calcium-dependent activity against palmitoyl-arachidonyl-phosphatidylethanolamine and low level lysophospholipase activity but no activity against phosphatidylcholine. Isoform 5 does have activity against phosphatidylcholine.3 Publications

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.3 Publications

Enzyme regulationi

Stimulated by cytosolic Ca2+.2 Publications

Kineticsi

    1. Vmax=7.9 pmol/min/mg enzyme (isoform 5)1 Publication
    2. Vmax=3.6 pmol/min/µg enzyme with cAMP as substrate (isoform 4)1 Publication
    3. Vmax=140 nmol/min/µg enzyme with 1-[14C]16:0-2-lyso-PC as substrate (isoform 5)1 Publication
    4. Vmax=1.6 nmol/min/µg enzyme with 1-[14C]16:0-2-lyso-PC as substrate (isoform 3)1 Publication
    5. Vmax=2.1 nmol/min/µg enzyme with 1-16:0-2-[14C]20:4-PC as substrate (isoform 5)1 Publication
    6. Vmax=0.6 nmol/min/µg enzyme with 1-16:0-2-[14C]20:4-PE as substrate (isoform 5)1 Publication
    7. Vmax=0.8 nmol/min/µg enzyme with 1-16:0-2-[14C]20:4-PE as substrate (isoform 3)1 Publication
    8. Vmax=0.3 nmol/min/µg enzyme with 1-16:0-2-[14C]18:2-PE as substrate (isoform 3)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei335 – 3351NucleophileBy similarity
    Active sitei615 – 6151Proton acceptorBy similarity

    GO - Molecular functioni

    • calcium-dependent phospholipase A2 activity Source: UniProtKB
    • calcium-dependent phospholipid binding Source: UniProtKB
    • calcium ion binding Source: UniProtKB
    • lysophospholipase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_120829. Acyl chain remodelling of PC.
    REACT_120906. Synthesis of PA.
    REACT_120977. Hydrolysis of LPC.
    REACT_121324. Acyl chain remodelling of PG.
    REACT_121369. Acyl chain remodelling of PE.
    REACT_121384. Acyl chain remodelling of PS.
    REACT_18273. XBP1(S) activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosolic phospholipase A2 beta (EC:3.1.1.4)
    Short name:
    cPLA2-beta
    Alternative name(s):
    Phospholipase A2 group IVB
    Gene namesi
    Name:PLA2G4B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:9036. PLA2G4B.

    Subcellular locationi

    • Cytoplasmcytosol 1 Publication
    Isoform 3 :

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • early endosome membrane Source: UniProtKB-SubCell
    • extracellular region Source: UniProtKB
    • mitochondrial inner membrane Source: Reactome
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi335 – 3351S → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi417 – 4171H → A: No effect. 1 Publication
    Mutagenesisi615 – 6151D → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi632 – 6321R → A: Abolishes enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA165479070.

    Polymorphism and mutation databases

    BioMutaiPLA2G4B.
    DMDMi300669659.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 781781Cytosolic phospholipase A2 betaPRO_0000247021Add
    BLAST

    Proteomic databases

    MaxQBiP0C869.
    PaxDbiP0C869.
    PRIDEiP0C869.

    PTM databases

    PhosphoSiteiP0C869.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed at higher level in brain, heart, liver, cerebellum and pancreas. Isoform 3 is widely expressed.3 Publications

    Gene expression databases

    BgeeiP0C869.
    ExpressionAtlasiP0C869. baseline.
    GenevisibleiP0C869. HS.

    Organism-specific databases

    HPAiHPA005726.

    Interactioni

    Protein-protein interaction databases

    BioGridi114229. 2 interactions.
    936685. 4 interactions.
    IntActiP0C869. 3 interactions.
    STRINGi9606.ENSP00000396045.

    Structurei

    3D structure databases

    ProteinModelPortaliP0C869.
    SMRiP0C869. Positions 11-130, 189-777.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9797C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini246 – 781536PLA2cPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca2+ (By similarity).By similarity

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 PLA2c domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG239428.
    GeneTreeiENSGT00550000074489.
    HOVERGENiHBG080412.
    InParanoidiP0C869.
    KOiK16342.
    OMAiYNICNNQ.
    OrthoDBiEOG70CR62.
    PhylomeDBiP0C869.
    TreeFamiTF325228.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR016035. Acyl_Trfase/lysoPLipase.
    IPR000008. C2_dom.
    IPR002642. LysoPLipase_cat_dom.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF01735. PLA2_B. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 1 hit.
    SM00022. PLAc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF52151. SSF52151. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS51210. PLA2C. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P0C869-1) [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

            10         20         30         40         50
    MAVAEVSRTC LLTVRVLQAH RLPSKDLVTP SDCYVTLWLP TACSHRLQTR
    60 70 80 90 100
    TVKNSSSPVW NQSFHFRIHR QLKNVMELKV FDQDLVTGDD PVLSVLFDAG
    110 120 130 140 150
    TLRAGEFRRE SFSLSPQGEG RLEVEFRLQS LADRGEWLVS NGVLVARELS
    160 170 180 190 200
    CLHVQLEETG DQKSSEHRVQ LVVPGSCEGP QEASVGTGTF RFHCPACWEQ
    210 220 230 240 250
    ELSIRLQDAP EEQLKAPLSA LPSGQVVRLV FPTSQEPLMR VELKKEAGLR
    260 270 280 290 300
    ELAVRLGFGP CAEEQAFLSR RKQVVAAALR QALQLDGDLQ EDEIPVVAIM
    310 320 330 340 350
    ATGGGIRAMT SLYGQLAGLK ELGLLDCVSY ITGASGSTWA LANLYEDPEW
    360 370 380 390 400
    SQKDLAGPTE LLKTQVTKNK LGVLAPSQLQ RYRQELAERA RLGYPSCFTN
    410 420 430 440 450
    LWALINEALL HDEPHDHKLS DQREALSHGQ NPLPIYCALN TKGQSLTTFE
    460 470 480 490 500
    FGEWCEFSPY EVGFPKYGAF IPSELFGSEF FMGQLMKRLP ESRICFLEGI
    510 520 530 540 550
    WSNLYAANLQ DSLYWASEPS QFWDRWVRNQ ANLDKEQVPL LKIEEPPSTA
    560 570 580 590 600
    GRIAEFFTDL LTWRPLAQAT HNFLRGLHFH KDYFQHPHFS TWKATTLDGL
    610 620 630 640 650
    PNQLTPSEPH LCLLDVGYLI NTSCLPLLQP TRDVDLILSL DYNLHGAFQQ
    660 670 680 690 700
    LQLLGRFCQE QGIPFPPISP SPEEQLQPRE CHTFSDPTCP GAPAVLHFPL
    710 720 730 740 750
    VSDSFREYSA PGVRRTPEEA AAGEVNLSSS DSPYHYTKVT YSQEDVDKLL
    760 770 780
    HLTHYNVCNN QEQLLEALRQ AVQRRRQRRP H
    Length:781
    Mass (Da):87,978
    Last modified:July 13, 2010 - v2
    Checksum:i4C5C6861E7BAB1B8
    GO
    Isoform 2 (identifier: P0C869-7) [UniParc]FASTAAdd to basket

    Also known as: beta2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MAV → MAEAALEAVR...KVVDEEAMEK
         650-662: QLQLLGRFCQEQG → GSGGHPRRRQLGR
         663-781: Missing.

    Note: Based on a naturally occurring readthrough transcript which produces a JMJD7-PLA2G4B fusion protein.
    Show »
    Length:893
    Mass (Da):100,516
    Checksum:i0A7C3BE752C48F55
    GO
    Isoform 3 (identifier: P0C869-8) [UniParc]FASTAAdd to basket

    Also known as: beta3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MAV → MAEAALEAVR...KVVDEEAMEK
         641-765: Missing.

    Note: Based on a naturally occurring readthrough transcript which produces a JMJD7-PLA2G4B fusion protein.
    Show »
    Length:887
    Mass (Da):100,094
    Checksum:i4C5CC6D084F2DF99
    GO
    Isoform 4 (identifier: P0C869-4) [UniParc] [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-299: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:482
    Mass (Da):54,679
    Checksum:iEB8FC2F2EB2AE258
    GO
    Isoform 5 (identifier: P0C869-6) [UniParc]FASTAAdd to basket

    Also known as: Beta1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MAV → MAEAALEAVR...KVVDEEAMEK

    Note: Based on a naturally occurring readthrough transcript which produces a JMJD7-PLA2G4B fusion protein.
    Show »
    Length:1,012
    Mass (Da):114,121
    Checksum:i989EDB4AD3CF19DD
    GO

    Sequence cautioni

    The sequence BAD92387.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381L → F in AAD32135 (PubMed:10358058).Curated
    Sequence conflicti162 – 1621Q → P in ABF69195 (PubMed:16617059).Curated
    Sequence conflicti162 – 1621Q → P in ABF69196 (PubMed:16617059).Curated
    Sequence conflicti438 – 4381A → V in ABF69195 (PubMed:16617059).Curated
    Sequence conflicti517 – 5171S → P in ABF69195 (PubMed:16617059).Curated
    Sequence conflicti575 – 5751R → C in BAG61401 (PubMed:14702039).Curated
    Sequence conflicti723 – 7231G → E in BAG61401 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti191 – 1911R → C.1 Publication
    Corresponds to variant rs3816533 [ dbSNP | Ensembl ].
    VAR_027047
    Natural varianti239 – 2391M → I.
    Corresponds to variant rs2290552 [ dbSNP | Ensembl ].
    VAR_027048
    Natural varianti391 – 3911R → H.
    Corresponds to variant rs34807597 [ dbSNP | Ensembl ].
    VAR_034365
    Natural varianti591 – 5911T → I.
    Corresponds to variant rs36126315 [ dbSNP | Ensembl ].
    VAR_060082

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 299299Missing in isoform 4. 1 PublicationVSP_019871Add
    BLAST
    Alternative sequencei1 – 33MAV → MAEAALEAVRSELREFPAAA RELCVPLAVPYLDKPPTPLH FYRDWVCPNRPCIIRNALQH WPALQKWSLPYFRATVGSTE VSVAVTPDGYADAVRGDRFM MPAERRLPLSFVLDVLEGRA QHPGVLYVQKQCSNLPSELP QLLPDLESHVPWASEALGKM PDAVNFWLGEAAAVTSLHKD HYENLYCVVSGEKHFLFHPP SDRPFIPYELYTPATYQLTE EGTFKVVDEEAMEK in isoform 2, isoform 3 and isoform 5. 3 PublicationsVSP_039387
    Alternative sequencei641 – 765125Missing in isoform 3. 1 PublicationVSP_039388Add
    BLAST
    Alternative sequencei650 – 66213QLQLL…CQEQG → GSGGHPRRRQLGR in isoform 2. 1 PublicationVSP_039389Add
    BLAST
    Alternative sequencei663 – 781119Missing in isoform 2. 1 PublicationVSP_039390Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF065215 mRNA. Translation: AAC78836.1.
    AF121908 mRNA. Translation: AAD32135.1.
    DQ523799 mRNA. Translation: ABF69195.1.
    DQ523800 mRNA. Translation: ABF69196.1.
    AK299419 mRNA. Translation: BAG61401.1.
    AB209150 mRNA. Translation: BAD92387.1. Different initiation.
    AC020659 Genomic DNA. No translation available.
    CCDSiCCDS45241.1.
    RefSeqiNP_001108105.1. NM_001114633.1. [P0C869-1]
    NP_001185517.1. NM_001198588.1. [P0C869-7]
    NP_005081.1. NM_005090.3. [P0C869-6]
    UniGeneiHs.198161.

    Genome annotation databases

    EnsembliENST00000452633; ENSP00000396045; ENSG00000243708. [P0C869-1]
    ENST00000458483; ENSP00000416610; ENSG00000243708. [P0C869-1]
    GeneIDi100137049.
    8681.
    KEGGihsa:100137049.
    hsa:8681.
    UCSCiuc001zoo.4. human. [P0C869-6]
    uc001zoq.4. human.
    uc010bcn.3. human. [P0C869-7]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF065215 mRNA. Translation: AAC78836.1.
    AF121908 mRNA. Translation: AAD32135.1.
    DQ523799 mRNA. Translation: ABF69195.1.
    DQ523800 mRNA. Translation: ABF69196.1.
    AK299419 mRNA. Translation: BAG61401.1.
    AB209150 mRNA. Translation: BAD92387.1. Different initiation.
    AC020659 Genomic DNA. No translation available.
    CCDSiCCDS45241.1.
    RefSeqiNP_001108105.1. NM_001114633.1. [P0C869-1]
    NP_001185517.1. NM_001198588.1. [P0C869-7]
    NP_005081.1. NM_005090.3. [P0C869-6]
    UniGeneiHs.198161.

    3D structure databases

    ProteinModelPortaliP0C869.
    SMRiP0C869. Positions 11-130, 189-777.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114229. 2 interactions.
    936685. 4 interactions.
    IntActiP0C869. 3 interactions.
    STRINGi9606.ENSP00000396045.

    Chemistry

    ChEMBLiCHEMBL4136.

    PTM databases

    PhosphoSiteiP0C869.

    Polymorphism and mutation databases

    BioMutaiPLA2G4B.
    DMDMi300669659.

    Proteomic databases

    MaxQBiP0C869.
    PaxDbiP0C869.
    PRIDEiP0C869.

    Protocols and materials databases

    DNASUi8681.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000452633; ENSP00000396045; ENSG00000243708. [P0C869-1]
    ENST00000458483; ENSP00000416610; ENSG00000243708. [P0C869-1]
    GeneIDi100137049.
    8681.
    KEGGihsa:100137049.
    hsa:8681.
    UCSCiuc001zoo.4. human. [P0C869-6]
    uc001zoq.4. human.
    uc010bcn.3. human. [P0C869-7]

    Organism-specific databases

    CTDi100137049.
    8681.
    GeneCardsiGC15P042129.
    HGNCiHGNC:9036. PLA2G4B.
    HPAiHPA005726.
    MIMi606088. gene.
    neXtProtiNX_P0C869.
    PharmGKBiPA165479070.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG239428.
    GeneTreeiENSGT00550000074489.
    HOVERGENiHBG080412.
    InParanoidiP0C869.
    KOiK16342.
    OMAiYNICNNQ.
    OrthoDBiEOG70CR62.
    PhylomeDBiP0C869.
    TreeFamiTF325228.

    Enzyme and pathway databases

    ReactomeiREACT_120829. Acyl chain remodelling of PC.
    REACT_120906. Synthesis of PA.
    REACT_120977. Hydrolysis of LPC.
    REACT_121324. Acyl chain remodelling of PG.
    REACT_121369. Acyl chain remodelling of PE.
    REACT_121384. Acyl chain remodelling of PS.
    REACT_18273. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    GeneWikiiPLA2G4B.
    NextBioi20774774.
    PROiP0C869.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP0C869.
    ExpressionAtlasiP0C869. baseline.
    GenevisibleiP0C869. HS.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR016035. Acyl_Trfase/lysoPLipase.
    IPR000008. C2_dom.
    IPR002642. LysoPLipase_cat_dom.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF01735. PLA2_B. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 1 hit.
    SM00022. PLAc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF52151. SSF52151. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS51210. PLA2C. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2."
      Pickard R.T., Strifler B.A., Kramer R.M., Sharp J.D.
      J. Biol. Chem. 274:8823-8831(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-335; HIS-417; ASP-615 AND ARG-632.
    2. "Molecular characterization of cytosolic phospholipase A2-beta."
      Song C., Chang X.J., Bean K.M., Proia M.S., Knopf J.L., Kriz R.W.
      J. Biol. Chem. 274:17063-17067(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
    3. "Identification of the expressed form of human cytosolic phospholipase A2beta (cPLA2beta): cPLA2beta3 is a novel variant localized to mitochondria and early endosomes."
      Ghosh M., Loper R., Gelb M.H., Leslie C.C.
      J. Biol. Chem. 281:16615-16624(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    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] (ISOFORM 1), VARIANT CYS-191.
      Tissue: Tongue.
    5. 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] (ISOFORM 4).
      Tissue: Brain.
    6. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiPA24B_HUMAN
    AccessioniPrimary (citable) accession number: P0C869
    Secondary accession number(s): B4DRT9
    , O95712, Q19KD5, Q19KD6, Q59GF9, Q8TB10, Q9UKV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: July 13, 2010
    Last modified: June 24, 2015
    This is version 71 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

    Caution

    Most tissues also express read-through transcripts from this gene into the upstream gene (JMJD7), some of which may encode fusion proteins.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.