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P51398

- RT29_HUMAN

UniProt

P51398 - RT29_HUMAN

Protein

28S ribosomal protein S29, mitochondrial

Gene

DAP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Involved in mediating interferon-gamma-induced cell death.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic mitochondrial changes Source: Ensembl
    2. apoptotic signaling pathway Source: ProtInc

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    28S ribosomal protein S29, mitochondrial
    Short name:
    MRP-S29
    Short name:
    S29mt
    Alternative name(s):
    Death-associated protein 3
    Short name:
    DAP-3
    Ionizing radiation resistance conferring protein
    Gene namesi
    Name:DAP3
    Synonyms:MRPS29
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2673. DAP3.

    Subcellular locationi

    Mitochondrion 2 Publications

    GO - Cellular componenti

    1. mitochondrial ribosome Source: InterPro
    2. mitochondrion Source: UniProtKB
    3. nucleolus Source: HPA
    4. nucleus Source: HPA
    5. small ribosomal subunit Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27141.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1818Mitochondrion1 PublicationAdd
    BLAST
    Chaini19 – 39838028S ribosomal protein S29, mitochondrialPRO_0000087717Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei175 – 1751N6-acetyllysine1 Publication
    Modified residuei207 – 2071N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP51398.
    PaxDbiP51398.
    PeptideAtlasiP51398.
    PRIDEiP51398.

    PTM databases

    PhosphoSiteiP51398.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP51398.
    BgeeiP51398.
    CleanExiHS_DAP3.
    GenevestigatoriP51398.

    Organism-specific databases

    HPAiHPA006076.
    HPA023687.

    Interactioni

    Subunit structurei

    Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. Interacts with KIAA0141. Interacts with NOA1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NOA1Q8NC605EBI-355912,EBI-717871

    Protein-protein interaction databases

    BioGridi113587. 29 interactions.
    IntActiP51398. 12 interactions.
    MINTiMINT-1149113.
    STRINGi9606.ENSP00000341692.

    Structurei

    3D structure databases

    ProteinModelPortaliP51398.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG260931.
    HOGENOMiHOG000046851.
    HOVERGENiHBG025946.
    InParanoidiP51398.
    KOiK17408.
    OMAiNERFLNQ.
    OrthoDBiEOG7GQXVS.
    PhylomeDBiP51398.
    TreeFamiTF313726.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR019368. Ribosomal_S23/S29_mit.
    IPR008092. Ribosomal_S29_mit.
    [Graphical view]
    PfamiPF10236. DAP3. 1 hit.
    [Graphical view]
    PRINTSiPR01716. DEATHASSOCP3.
    SUPFAMiSSF52540. SSF52540. 2 hits.

    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: P51398-1) [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

    MMLKGITRLI SRIHKLDPGR FLHMGTQARQ SIAAHLDNQV PVESPRAISR    50
    TNENDPAKHG DQHEGQHYNI SPQDLETVFP HGLPPRFVMQ VKTFSEACLM 100
    VRKPALELLH YLKNTSFAYP AIRYLLYGEK GTGKTLSLCH VIHFCAKQDW 150
    LILHIPDAHL WVKNCRDLLQ SSYNKQRFDQ PLEASTWLKN FKTTNERFLN 200
    QIKVQEKYVW NKRESTEKGS PLGEVVEQGI TRVRNATDAV GIVLKELKRQ 250
    SSLGMFHLLV AVDGINALWG RTTLKREDKS PIAPEELALV HNLRKMMKND 300
    WHGGAIVSAL SQTGSLFKPR KAYLPQELLG KEGFDALDPF IPILVSNYNP 350
    KEFESCIQYY LENNWLQHEK APTEEGKKEL LFLSNANPSL LERHCAYL 398
    Length:398
    Mass (Da):45,566
    Last modified:October 1, 1996 - v1
    Checksum:i778AF183FA04DEC8
    GO
    Isoform 2 (identifier: P51398-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         16-56: Missing.

    Show »
    Length:357
    Mass (Da):41,044
    Checksum:i20E08FFBBF9C2E57
    GO
    Isoform 3 (identifier: P51398-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         57-90: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:364
    Mass (Da):41,673
    Checksum:iA51F7F4E1B0B12B0
    GO

    Sequence cautioni

    The sequence AAA57443.1 differs from that shown. Reason: Frameshift at position 349.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti157 – 1571D → Y in BAG63624. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti240 – 2401V → F.
    Corresponds to variant rs57692591 [ dbSNP | Ensembl ].
    VAR_061811

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei16 – 5641Missing in isoform 2. 1 PublicationVSP_042790Add
    BLAST
    Alternative sequencei57 – 9034Missing in isoform 3. 1 PublicationVSP_044639Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18321 mRNA. Translation: AAA57443.1. Frameshift.
    X83544 mRNA. Translation: CAA58535.1.
    AK293117 mRNA. Translation: BAF85806.1.
    AK298201 mRNA. Translation: BAG60471.1.
    AK302281 mRNA. Translation: BAG63624.1.
    BT019494 mRNA. Translation: AAV38301.1.
    CR749790 mRNA. Translation: CAH18651.1.
    AL162734 Genomic DNA. Translation: CAH71647.1.
    CH471121 Genomic DNA. Translation: EAW53044.1.
    CH471121 Genomic DNA. Translation: EAW53045.1.
    CH471121 Genomic DNA. Translation: EAW53047.1.
    CH471121 Genomic DNA. Translation: EAW53048.1.
    CH471121 Genomic DNA. Translation: EAW53049.1.
    CH471121 Genomic DNA. Translation: EAW53051.1.
    BC107487 mRNA. Translation: AAI07488.1.
    BC107488 mRNA. Translation: AAI07489.1.
    CCDSiCCDS1120.1. [P51398-1]
    CCDS55646.1. [P51398-3]
    CCDS55647.1. [P51398-2]
    PIRiG01589.
    RefSeqiNP_001186778.1. NM_001199849.1. [P51398-1]
    NP_001186779.1. NM_001199850.1. [P51398-3]
    NP_001186780.1. NM_001199851.1. [P51398-2]
    NP_004623.1. NM_004632.3. [P51398-1]
    NP_387506.1. NM_033657.2. [P51398-1]
    XP_005245537.1. XM_005245480.1. [P51398-3]
    XP_005245538.1. XM_005245481.1. [P51398-2]
    UniGeneiHs.516746.

    Genome annotation databases

    EnsembliENST00000343043; ENSP00000341692; ENSG00000132676. [P51398-1]
    ENST00000368336; ENSP00000357320; ENSG00000132676. [P51398-1]
    ENST00000421487; ENSP00000412605; ENSG00000132676. [P51398-3]
    ENST00000471642; ENSP00000476592; ENSG00000132676. [P51398-2]
    ENST00000535183; ENSP00000445003; ENSG00000132676. [P51398-2]
    GeneIDi7818.
    KEGGihsa:7818.
    UCSCiuc001flq.3. human. [P51398-1]
    uc010pgl.2. human. [P51398-2]

    Polymorphism databases

    DMDMi1706299.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18321 mRNA. Translation: AAA57443.1 . Frameshift.
    X83544 mRNA. Translation: CAA58535.1 .
    AK293117 mRNA. Translation: BAF85806.1 .
    AK298201 mRNA. Translation: BAG60471.1 .
    AK302281 mRNA. Translation: BAG63624.1 .
    BT019494 mRNA. Translation: AAV38301.1 .
    CR749790 mRNA. Translation: CAH18651.1 .
    AL162734 Genomic DNA. Translation: CAH71647.1 .
    CH471121 Genomic DNA. Translation: EAW53044.1 .
    CH471121 Genomic DNA. Translation: EAW53045.1 .
    CH471121 Genomic DNA. Translation: EAW53047.1 .
    CH471121 Genomic DNA. Translation: EAW53048.1 .
    CH471121 Genomic DNA. Translation: EAW53049.1 .
    CH471121 Genomic DNA. Translation: EAW53051.1 .
    BC107487 mRNA. Translation: AAI07488.1 .
    BC107488 mRNA. Translation: AAI07489.1 .
    CCDSi CCDS1120.1. [P51398-1 ]
    CCDS55646.1. [P51398-3 ]
    CCDS55647.1. [P51398-2 ]
    PIRi G01589.
    RefSeqi NP_001186778.1. NM_001199849.1. [P51398-1 ]
    NP_001186779.1. NM_001199850.1. [P51398-3 ]
    NP_001186780.1. NM_001199851.1. [P51398-2 ]
    NP_004623.1. NM_004632.3. [P51398-1 ]
    NP_387506.1. NM_033657.2. [P51398-1 ]
    XP_005245537.1. XM_005245480.1. [P51398-3 ]
    XP_005245538.1. XM_005245481.1. [P51398-2 ]
    UniGenei Hs.516746.

    3D structure databases

    ProteinModelPortali P51398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113587. 29 interactions.
    IntActi P51398. 12 interactions.
    MINTi MINT-1149113.
    STRINGi 9606.ENSP00000341692.

    PTM databases

    PhosphoSitei P51398.

    Polymorphism databases

    DMDMi 1706299.

    Proteomic databases

    MaxQBi P51398.
    PaxDbi P51398.
    PeptideAtlasi P51398.
    PRIDEi P51398.

    Protocols and materials databases

    DNASUi 7818.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343043 ; ENSP00000341692 ; ENSG00000132676 . [P51398-1 ]
    ENST00000368336 ; ENSP00000357320 ; ENSG00000132676 . [P51398-1 ]
    ENST00000421487 ; ENSP00000412605 ; ENSG00000132676 . [P51398-3 ]
    ENST00000471642 ; ENSP00000476592 ; ENSG00000132676 . [P51398-2 ]
    ENST00000535183 ; ENSP00000445003 ; ENSG00000132676 . [P51398-2 ]
    GeneIDi 7818.
    KEGGi hsa:7818.
    UCSCi uc001flq.3. human. [P51398-1 ]
    uc010pgl.2. human. [P51398-2 ]

    Organism-specific databases

    CTDi 7818.
    GeneCardsi GC01P155657.
    HGNCi HGNC:2673. DAP3.
    HPAi HPA006076.
    HPA023687.
    MIMi 602074. gene.
    neXtProti NX_P51398.
    PharmGKBi PA27141.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260931.
    HOGENOMi HOG000046851.
    HOVERGENi HBG025946.
    InParanoidi P51398.
    KOi K17408.
    OMAi NERFLNQ.
    OrthoDBi EOG7GQXVS.
    PhylomeDBi P51398.
    TreeFami TF313726.

    Miscellaneous databases

    GeneWikii DAP3.
    GenomeRNAii 7818.
    NextBioi 30217.
    PROi P51398.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51398.
    Bgeei P51398.
    CleanExi HS_DAP3.
    Genevestigatori P51398.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR019368. Ribosomal_S23/S29_mit.
    IPR008092. Ribosomal_S29_mit.
    [Graphical view ]
    Pfami PF10236. DAP3. 1 hit.
    [Graphical view ]
    PRINTSi PR01716. DEATHASSOCP3.
    SUPFAMi SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "The molecular genetics of human diseases with defective DNA damage processing."
      Henning K.A.
      Thesis (1993), University of Stanford, United States
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Cervix carcinoma.
    2. "Isolation of DAP3, a novel mediator of interferon-gamma-induced cell death."
      Kissil J.L., Deiss L.P., Bayewitch M., Raveh T., Khaspekov G., Kimchi A.
      J. Biol. Chem. 270:27932-27936(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORMS 1; 2 AND 3).
      Tissue: Testis.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon endothelium.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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).
    9. "The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders."
      Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S., Watanabe K., Tanaka T.
      Genomics 77:65-70(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-235.
    10. Cited for: SUBCELLULAR LOCATION, TRANSIT PEPTIDE CLEAVAGE SITE.
    11. "The small subunit of the mammalian mitochondrial ribosome: identification of the full complement of ribosomal proteins present."
      Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.
      J. Biol. Chem. 276:19363-19374(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    12. "hNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis."
      Tang T., Zheng B., Chen S.H., Murphy A.N., Kudlicka K., Zhou H., Farquhar M.G.
      J. Biol. Chem. 284:5414-5424(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOA1.
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-175 AND LYS-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Identification of DELE, a novel DAP3-binding protein which is crucial for death receptor-mediated apoptosis induction."
      Harada T., Iwai A., Miyazaki T.
      Apoptosis 15:1247-1255(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KIAA0141.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRT29_HUMAN
    AccessioniPrimary (citable) accession number: P51398
    Secondary accession number(s): B4DP59
    , B4DY62, E7EM60, Q13044, Q68CT7, Q96Q20
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 130 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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

    External Data

    Dasty 3