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Q9H7F0

- AT133_HUMAN

UniProt

Q9H7F0 - AT133_HUMAN

Protein

Probable cation-transporting ATPase 13A3

Gene

ATP13A3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 4 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei498 – 49814-aspartylphosphate intermediateBy similarity
    Metal bindingi883 – 8831MagnesiumBy similarity
    Metal bindingi887 – 8871MagnesiumBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cation-transporting ATPase activity Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable cation-transporting ATPase 13A3 (EC:3.6.3.-)
    Alternative name(s):
    ATPase family homolog up-regulated in senescence cells 1
    Gene namesi
    Name:ATP13A3
    Synonyms:AFURS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:24113. ATP13A3.

    Subcellular locationi

    Membrane By similarity; Multi-pass membrane protein By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134971145.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12261226Probable cation-transporting ATPase 13A3PRO_0000046425Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei98 – 981Phosphoserine2 Publications
    Modified residuei817 – 8171Phosphoserine6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H7F0.
    PaxDbiQ9H7F0.
    PRIDEiQ9H7F0.

    PTM databases

    PhosphoSiteiQ9H7F0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H7F0.
    BgeeiQ9H7F0.
    CleanExiHS_ATP13A3.
    GenevestigatoriQ9H7F0.

    Organism-specific databases

    HPAiHPA029471.

    Interactioni

    Protein-protein interaction databases

    BioGridi122719. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H7F0.
    SMRiQ9H7F0. Positions 163-1027.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei29 – 4921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei206 – 22621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei233 – 25321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei410 – 43021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei449 – 46921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei941 – 96121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei963 – 98321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1000 – 102021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1074 – 109421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1106 – 112621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1144 – 116421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi231 – 2344Poly-Tyr

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    HOGENOMiHOG000171813.
    HOVERGENiHBG065757.
    InParanoidiQ9H7F0.
    KOiK14951.
    OMAiENRHRIS.
    OrthoDBiEOG7B5WV2.
    PhylomeDBiQ9H7F0.
    TreeFamiTF300331.

    Family and domain databases

    Gene3Di2.70.150.10. 1 hit.
    3.40.1110.10. 2 hits.
    3.40.50.1000. 2 hits.
    InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
    IPR006544. ATPase_P-typ_Cation_typ_V.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view]
    PfamiPF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF12409. P5-ATPase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SUPFAMiSSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 2 hits.
    TIGRFAMsiTIGR01494. ATPase_P-type. 3 hits.
    TIGR01657. P-ATPase-V. 1 hit.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H7F0-1) [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

    MDREERKTIN QGQEDEMEIY GYNLSRWKLA IVSLGVICSG GFLLLLLYWM     50
    PEWRVKATCV RAAIKDCEVV LLRTTDEFKM WFCAKIRVLS LETYPVSSPK 100
    SMSNKLSNGH AVCLIENPTE ENRHRISKYS QTESQQIRYF THHSVKYFWN 150
    DTIHNFDFLK GLDEGVSCTS IYEKHSAGLT KGMHAYRKLL YGVNEIAVKV 200
    PSVFKLLIKE VLNPFYIFQL FSVILWSTDE YYYYALAIVV MSIVSIVSSL 250
    YSIRKQYVML HDMVATHSTV RVSVCRVNEE IEEIFSTDLV PGDVMVIPLN 300
    GTIMPCDAVL INGTCIVNES MLTGESVPVT KTNLPNPSVD VKGIGDELYN 350
    PETHKRHTLF CGTTVIQTRF YTGELVKAIV VRTGFSTSKG QLVRSILYPK 400
    PTDFKLYRDA YLFLLCLVAV AGIGFIYTII NSILNEVQVG VIIIESLDII 450
    TITVPPALPA AMTAGIVYAQ RRLKKIGIFC ISPQRINICG QLNLVCFDKT 500
    GTLTEDGLDL WGIQRVENAR FLSPEENVCN EMLVKSQFVA CMATCHSLTK 550
    IEGVLSGDPL DLKMFEAIGW ILEEATEEET ALHNRIMPTV VRPPKQLLPE 600
    STPAGNQEME LFELPATYEI GIVRQFPFSS ALQRMSVVAR VLGDRKMDAY 650
    MKGAPEAIAG LCKPETVPVD FQNVLEDFTK QGFRVIALAH RKLESKLTWH 700
    KVQNISRDAI ENNMDFMGLI IMQNKLKQET PAVLEDLHKA NIRTVMVTGD 750
    SMLTAVSVAR DCGMILPQDK VIIAEALPPK DGKVAKINWH YADSLTQCSH 800
    PSAIDPEAIP VKLVHDSLED LQMTRYHFAM NGKSFSVILE HFQDLVPKLM 850
    LHGTVFARMA PDQKTQLIEA LQNVDYFVGM CGDGANDCGA LKRAHGGISL 900
    SELEASVASP FTSKTPSISC VPNLIREGRA ALITSFCVFK FMALYSIIQY 950
    FSVTLLYSIL SNLGDFQFLF IDLAIILVVV FTMSLNPAWK ELVAQRPPSG 1000
    LISGALLFSV LSQIIICIGF QSLGFFWVKQ QPWYEVWHPK SDACNTTGSG 1050
    FWNSSHVDNE TELDEHNIQN YENTTVFFIS SFQYLIVAIA FSKGKPFRQP 1100
    CYKNYFFVFS VIFLYIFILF IMLYPVASVD QVLQIVCVPY QWRVTMLIIV 1150
    LVNAFVSITV EESVDRWGKC CLPWALGCRK KTPKAKYMYL AQELLVDPEW 1200
    PPKPQTTTEA KALVKENGSC QIITIT 1226
    Length:1,226
    Mass (Da):138,043
    Last modified:February 10, 2009 - v4
    Checksum:i8DD1C0451223C7AB
    GO
    Isoform 2 (identifier: Q9H7F0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-277: Missing.
         278-279: NE → MS
         936-978: FCVFKFMALY...LFIDLAIILV → SCELALFSIV...FHNCAFYSLV
         979-1226: Missing.

    Note: Dubious isoform produced through aberrant splice sites.

    Show »
    Length:701
    Mass (Da):77,310
    Checksum:i7927AFFE8413247F
    GO

    Sequence cautioni

    The sequence BAB14942.1 differs from that shown. Reason: Frameshift at position 1065.
    The sequence BAB14942.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC11398.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti347 – 3471E → Q in CAC84902. (PubMed:11867234)Curated
    Sequence conflicti730 – 7301T → P in CAC84902. (PubMed:11867234)Curated
    Sequence conflicti784 – 7841V → F in BAC11398. (PubMed:14702039)Curated
    Sequence conflicti807 – 8071E → G in BAC11398. (PubMed:14702039)Curated
    Sequence conflicti964 – 9641G → R in BAC11398. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 277277Missing in isoform 2. 1 PublicationVSP_007314Add
    BLAST
    Alternative sequencei278 – 2792NE → MS in isoform 2. 1 PublicationVSP_036300
    Alternative sequencei936 – 97843FCVFK…AIILV → SCELALFSIVTYSLDHFIIS ILISSMLVLFFSDFHNCAFY SLV in isoform 2. 1 PublicationVSP_007315Add
    BLAST
    Alternative sequencei979 – 1226248Missing in isoform 2. 1 PublicationVSP_007316Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ306929 mRNA. Translation: CAC84902.1.
    AC108676 Genomic DNA. No translation available.
    AC125362 Genomic DNA. No translation available.
    AK024639 mRNA. Translation: BAB14942.1. Sequence problems.
    AK075094 mRNA. Translation: BAC11398.1. Different initiation.
    CCDSiCCDS43187.1. [Q9H7F0-1]
    RefSeqiNP_078800.3. NM_024524.3. [Q9H7F0-1]
    UniGeneiHs.529609.

    Genome annotation databases

    EnsembliENST00000256031; ENSP00000256031; ENSG00000133657. [Q9H7F0-1]
    ENST00000439040; ENSP00000416508; ENSG00000133657. [Q9H7F0-1]
    GeneIDi79572.
    KEGGihsa:79572.
    UCSCiuc003fty.4. human. [Q9H7F0-1]

    Polymorphism databases

    DMDMi223590262.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ306929 mRNA. Translation: CAC84902.1 .
    AC108676 Genomic DNA. No translation available.
    AC125362 Genomic DNA. No translation available.
    AK024639 mRNA. Translation: BAB14942.1 . Sequence problems.
    AK075094 mRNA. Translation: BAC11398.1 . Different initiation.
    CCDSi CCDS43187.1. [Q9H7F0-1 ]
    RefSeqi NP_078800.3. NM_024524.3. [Q9H7F0-1 ]
    UniGenei Hs.529609.

    3D structure databases

    ProteinModelPortali Q9H7F0.
    SMRi Q9H7F0. Positions 163-1027.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122719. 1 interaction.

    PTM databases

    PhosphoSitei Q9H7F0.

    Polymorphism databases

    DMDMi 223590262.

    Proteomic databases

    MaxQBi Q9H7F0.
    PaxDbi Q9H7F0.
    PRIDEi Q9H7F0.

    Protocols and materials databases

    DNASUi 79572.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256031 ; ENSP00000256031 ; ENSG00000133657 . [Q9H7F0-1 ]
    ENST00000439040 ; ENSP00000416508 ; ENSG00000133657 . [Q9H7F0-1 ]
    GeneIDi 79572.
    KEGGi hsa:79572.
    UCSCi uc003fty.4. human. [Q9H7F0-1 ]

    Organism-specific databases

    CTDi 79572.
    GeneCardsi GC03M194123.
    HGNCi HGNC:24113. ATP13A3.
    HPAi HPA029471.
    MIMi 610232. gene.
    neXtProti NX_Q9H7F0.
    PharmGKBi PA134971145.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0474.
    HOGENOMi HOG000171813.
    HOVERGENi HBG065757.
    InParanoidi Q9H7F0.
    KOi K14951.
    OMAi ENRHRIS.
    OrthoDBi EOG7B5WV2.
    PhylomeDBi Q9H7F0.
    TreeFami TF300331.

    Miscellaneous databases

    GeneWikii ATP13A3.
    GenomeRNAii 79572.
    NextBioi 68532.
    PROi Q9H7F0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H7F0.
    Bgeei Q9H7F0.
    CleanExi HS_ATP13A3.
    Genevestigatori Q9H7F0.

    Family and domain databases

    Gene3Di 2.70.150.10. 1 hit.
    3.40.1110.10. 2 hits.
    3.40.50.1000. 2 hits.
    InterProi IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR006544. ATPase_P-typ_Cation_typ_V.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view ]
    Pfami PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF12409. P5-ATPase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SUPFAMi SSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 2 hits.
    TIGRFAMsi TIGR01494. ATPase_P-type. 3 hits.
    TIGR01657. P-ATPase-V. 1 hit.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning the AFURS1 gene which is up-regulated in senescent human parenchymal kidney cells."
      Habtemichael N., Kovacs G.
      Gene 283:271-275(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] OF 402-1226 (ISOFORM 1).
      Tissue: Coronary artery and Placenta.
    4. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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-98 AND SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "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-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAT133_HUMAN
    AccessioniPrimary (citable) accession number: Q9H7F0
    Secondary accession number(s): Q8NC11, Q96KS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 117 of the entry and version 4 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 3
      Human chromosome 3: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3