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Q8NG27

- PJA1_HUMAN

UniProt

Q8NG27 - PJA1_HUMAN

Protein

E3 ubiquitin-protein ligase Praja-1

Gene

PJA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (23 May 2003)
      Previous versions | rss
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    Functioni

    Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome By similarity. May be involved in protein sorting.By similarity1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri595 – 63642RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. ubiquitin-protein transferase activity Source: Ensembl
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. protein catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase Praja-1 (EC:6.3.2.-)
    Short name:
    Praja1
    Alternative name(s):
    RING finger protein 70
    Gene namesi
    Name:PJA1
    Synonyms:RNF70
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:16648. PJA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33342.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 643643E3 ubiquitin-protein ligase Praja-1PRO_0000055999Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei277 – 2771Phosphothreonine2 Publications

    Post-translational modificationi

    Substrate for E2-dependent ubiquitination.

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8NG27.
    PaxDbiQ8NG27.
    PRIDEiQ8NG27.

    PTM databases

    PhosphoSiteiQ8NG27.

    Expressioni

    Tissue specificityi

    Expressed in various regions of the brain including the cerebellum, cerebral cortex, medulla, occipital pole, frontal lobe, temporal lobe and putamen. Highest levels in the cerebral cortex.1 Publication

    Gene expression databases

    ArrayExpressiQ8NG27.
    BgeeiQ8NG27.
    CleanExiHS_PJA1.
    GenevestigatoriQ8NG27.

    Organism-specific databases

    HPAiHPA000595.

    Interactioni

    Subunit structurei

    Binds ubiquitin-conjugating enzymes (E2s). In vitro, interacts with the ubiquitin-conjugating enzyme, UBE2D2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAGED1Q9Y5V34EBI-714606,EBI-716006
    NDNL2Q96MG72EBI-714606,EBI-2557356

    Protein-protein interaction databases

    BioGridi122109. 37 interactions.
    IntActiQ8NG27. 12 interactions.
    MINTiMINT-1384058.
    STRINGi9606.ENSP00000355014.

    Structurei

    Secondary structure

    1
    643
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi571 – 5755
    Beta strandi579 – 5813
    Beta strandi587 – 5915
    Turni596 – 5983
    Beta strandi607 – 6115
    Turni612 – 6143
    Beta strandi615 – 6184
    Helixi619 – 6268
    Turni633 – 6353
    Beta strandi638 – 6403

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L0BNMR-A564-643[»]
    ProteinModelPortaliQ8NG27.
    SMRiQ8NG27. Positions 532-643.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi276 – 2827Poly-Asp
    Compositional biasi340 – 3434Poly-Arg

    Domaini

    The RING-type zinc finger domain interacts with an ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination.By similarity

    Sequence similaritiesi

    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri595 – 63642RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG239209.
    HOGENOMiHOG000230900.
    HOVERGENiHBG003815.
    InParanoidiQ8NG27.
    KOiK10633.
    OMAiYSRYPPR.
    OrthoDBiEOG7TJ3HJ.
    PhylomeDBiQ8NG27.
    TreeFamiTF330711.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF13639. zf-RING_2. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8NG27-1) [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

    MGQESSKPVW PNPTGGYQSN TGRRYGRRHA YVSFRPPTSQ RERIASQRKT    50
    NSEVPMHRSA PSQTTKRSRS PFSTTRRSWD DSESSGTNLN IDNEDYSRYP 100
    PREYRASGSR RGMAYGHIDS YGADDSEEEG AGPVERPPVR GKTGKFKDDK 150
    LYDPEKGARS LAGPPPHFSS FSRDVREERD KLDPVPAARC SASRADFLPQ 200
    SSVASQSSSE GKLATKGDSS ERERREQNLP ARPSRAPVSI CGGGENTSKS 250
    AEEPVVRPKI RNLASPNCVK PKIFFDTDDD DDMPHSTSRW RDTANDNEGH 300
    SDGLARRGRG ESSSGYPEPK YPEDKREARS DQVKPEKVPR RRRTMADPDF 350
    WTHSDDYYKY CDEDSDSDKE WIAALRRKYR SREQTLSSSG ESWETLPGKE 400
    EREPPQAKVS ASTGTSPGPG ASASAGAGAG ASAGSNGSNY LEEVREPSLQ 450
    EEQASLEEGE IPWLQYHEND SSSEGDNDSG HELMQPGVFM LDGNNNLEDD 500
    SSVSEDLEVD WSLFDGFADG LGVAEAISYV DPQFLTYMAL EERLAQAMET 550
    ALAHLESLAV DVEVANPPAS KESIDALPEI LVTEDHGAVG QEMCCPICCS 600
    EYVKGEVATE LPCHHYFHKP CVSIWLQKSG TCPVCRCMFP PPL 643
    Length:643
    Mass (Da):71,002
    Last modified:May 23, 2003 - v2
    Checksum:iF3DFD1F77809318D
    GO
    Isoform 2 (identifier: Q8NG27-2) [UniParc]FASTAAdd to Basket

    Also known as: PJA1-beta, Praja1-beta

    The sequence of this isoform differs from the canonical sequence as follows:
         98-285: Missing.

    Note: No experimental confirmation available. PubMed:12036302 reported that isoform 2 arises by alternative initiation.

    Show »
    Length:455
    Mass (Da):50,445
    Checksum:iA4C247465CF65396
    GO
    Isoform 3 (identifier: Q8NG27-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-55: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:588
    Mass (Da):64,729
    Checksum:i2D1B424ED1BA7D87
    GO

    Sequence cautioni

    The sequence BAB13928.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti432 – 4321S → N.1 Publication
    Corresponds to variant rs5937160 [ dbSNP | Ensembl ].
    VAR_052088
    Natural varianti606 – 6061E → D.1 Publication
    Corresponds to variant rs11539157 [ dbSNP | Ensembl ].
    VAR_052089

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5555Missing in isoform 3. CuratedVSP_046995Add
    BLAST
    Alternative sequencei98 – 285188Missing in isoform 2. 1 PublicationVSP_007518Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF262024 mRNA. Translation: AAM53039.1.
    AF264620 mRNA. Translation: AAM53040.1.
    AL157699 Genomic DNA. Translation: CAI41604.1.
    AL157699 Genomic DNA. Translation: CAI41605.1.
    CH471132 Genomic DNA. Translation: EAX05367.1.
    BC048323 mRNA. Translation: AAH48323.1.
    BC075803 mRNA. Translation: AAH75803.1.
    BC105051 mRNA. Translation: AAI05052.1.
    BC105053 mRNA. Translation: AAI05054.1.
    AK021892 mRNA. Translation: BAB13928.1. Different initiation.
    CCDSiCCDS14392.1. [Q8NG27-2]
    CCDS14393.1. [Q8NG27-1]
    CCDS35316.1. [Q8NG27-3]
    RefSeqiNP_001027568.1. NM_001032396.2. [Q8NG27-3]
    NP_071763.2. NM_022368.4. [Q8NG27-2]
    NP_660095.1. NM_145119.3. [Q8NG27-1]
    XP_005262349.1. XM_005262292.1. [Q8NG27-3]
    UniGeneiHs.522679.

    Genome annotation databases

    EnsembliENST00000361478; ENSP00000355014; ENSG00000181191. [Q8NG27-1]
    ENST00000374571; ENSP00000363699; ENSG00000181191. [Q8NG27-3]
    ENST00000374583; ENSP00000363711; ENSG00000181191. [Q8NG27-1]
    ENST00000374584; ENSP00000363712; ENSG00000181191. [Q8NG27-2]
    GeneIDi64219.
    KEGGihsa:64219.
    UCSCiuc004dxg.3. human. [Q8NG27-2]
    uc004dxh.3. human. [Q8NG27-1]

    Polymorphism databases

    DMDMi31076980.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF262024 mRNA. Translation: AAM53039.1 .
    AF264620 mRNA. Translation: AAM53040.1 .
    AL157699 Genomic DNA. Translation: CAI41604.1 .
    AL157699 Genomic DNA. Translation: CAI41605.1 .
    CH471132 Genomic DNA. Translation: EAX05367.1 .
    BC048323 mRNA. Translation: AAH48323.1 .
    BC075803 mRNA. Translation: AAH75803.1 .
    BC105051 mRNA. Translation: AAI05052.1 .
    BC105053 mRNA. Translation: AAI05054.1 .
    AK021892 mRNA. Translation: BAB13928.1 . Different initiation.
    CCDSi CCDS14392.1. [Q8NG27-2 ]
    CCDS14393.1. [Q8NG27-1 ]
    CCDS35316.1. [Q8NG27-3 ]
    RefSeqi NP_001027568.1. NM_001032396.2. [Q8NG27-3 ]
    NP_071763.2. NM_022368.4. [Q8NG27-2 ]
    NP_660095.1. NM_145119.3. [Q8NG27-1 ]
    XP_005262349.1. XM_005262292.1. [Q8NG27-3 ]
    UniGenei Hs.522679.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L0B NMR - A 564-643 [» ]
    ProteinModelPortali Q8NG27.
    SMRi Q8NG27. Positions 532-643.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122109. 37 interactions.
    IntActi Q8NG27. 12 interactions.
    MINTi MINT-1384058.
    STRINGi 9606.ENSP00000355014.

    PTM databases

    PhosphoSitei Q8NG27.

    Polymorphism databases

    DMDMi 31076980.

    Proteomic databases

    MaxQBi Q8NG27.
    PaxDbi Q8NG27.
    PRIDEi Q8NG27.

    Protocols and materials databases

    DNASUi 64219.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361478 ; ENSP00000355014 ; ENSG00000181191 . [Q8NG27-1 ]
    ENST00000374571 ; ENSP00000363699 ; ENSG00000181191 . [Q8NG27-3 ]
    ENST00000374583 ; ENSP00000363711 ; ENSG00000181191 . [Q8NG27-1 ]
    ENST00000374584 ; ENSP00000363712 ; ENSG00000181191 . [Q8NG27-2 ]
    GeneIDi 64219.
    KEGGi hsa:64219.
    UCSCi uc004dxg.3. human. [Q8NG27-2 ]
    uc004dxh.3. human. [Q8NG27-1 ]

    Organism-specific databases

    CTDi 64219.
    GeneCardsi GC0XM068297.
    HGNCi HGNC:16648. PJA1.
    HPAi HPA000595.
    MIMi 300420. gene.
    neXtProti NX_Q8NG27.
    PharmGKBi PA33342.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239209.
    HOGENOMi HOG000230900.
    HOVERGENi HBG003815.
    InParanoidi Q8NG27.
    KOi K10633.
    OMAi YSRYPPR.
    OrthoDBi EOG7TJ3HJ.
    PhylomeDBi Q8NG27.
    TreeFami TF330711.

    Enzyme and pathway databases

    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    GeneWikii PJA1.
    GenomeRNAii 64219.
    NextBioi 66135.
    PROi Q8NG27.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8NG27.
    Bgeei Q8NG27.
    CleanExi HS_PJA1.
    Genevestigatori Q8NG27.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF13639. zf-RING_2. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain."
      Yu P., Chen Y., Tagle D.A., Cai T.
      Genomics 79:869-874(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH UBE2D2.
      Tissue: Brain.
    2. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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), VARIANTS ASN-432 AND ASP-606.
      Tissue: Brain, Kidney and Uterus.
    5. "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] OF 282-643 (ISOFORM 1).
      Tissue: Embryo.
    6. "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 THR-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    7. "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 THR-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPJA1_HUMAN
    AccessioniPrimary (citable) accession number: Q8NG27
    Secondary accession number(s): A2A322
    , Q5JUT8, Q5JUT9, Q8NG28, Q9HAC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 23, 2003
    Last sequence update: May 23, 2003
    Last modified: October 1, 2014
    This is version 116 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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