Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15172

- 2A5A_HUMAN

UniProt

Q15172 - 2A5A_HUMAN

Protein

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform

Gene

PPP2R5A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.

    GO - Molecular functioni

    1. kinase binding Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. protein phosphatase type 2A regulator activity Source: ProtInc

    GO - Biological processi

    1. negative regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
    2. negative regulation of lipid kinase activity Source: BHF-UCL
    3. positive regulation of protein dephosphorylation Source: BHF-UCL
    4. signal transduction Source: InterPro

    Enzyme and pathway databases

    ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_23879. Platelet sensitization by LDL.
    REACT_682. Mitotic Prometaphase.
    SignaLinkiQ15172.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
    Alternative name(s):
    PP2A B subunit isoform B'-alpha
    PP2A B subunit isoform B56-alpha
    PP2A B subunit isoform PR61-alpha
    Short name:
    PR61alpha
    PP2A B subunit isoform R5-alpha
    Gene namesi
    Name:PPP2R5A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9309. PPP2R5A.

    Subcellular locationi

    Cytoplasm. Nucleus. Chromosomecentromere
    Note: From mitotic prophase to metaphase, localizes at the inner centromere between a pair of sister kinetochores. Decreased expression at the onset of anaphase.

    GO - Cellular componenti

    1. chromosome, centromeric region Source: UniProtKB-SubCell
    2. cytoplasm Source: BHF-UCL
    3. M band Source: BHF-UCL
    4. nucleus Source: UniProtKB-SubCell
    5. protein phosphatase type 2A complex Source: UniProtKB
    6. Z disc Source: Ensembl

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33672.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 486485Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoformPRO_0000071448Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei41 – 411Phosphoserine4 Publications
    Modified residuei42 – 421Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylated on serine residues.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15172.
    PaxDbiQ15172.
    PeptideAtlasiQ15172.
    PRIDEiQ15172.

    2D gel databases

    OGPiQ15172.

    PTM databases

    PhosphoSiteiQ15172.

    Expressioni

    Tissue specificityi

    Widely expressed with the highest expression in heart and skeletal muscle.

    Gene expression databases

    BgeeiQ15172.
    CleanExiHS_PPP2R5A.
    GenevestigatoriQ15172.

    Interactioni

    Subunit structurei

    PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with SGOL1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CHEK2O960172EBI-641666,EBI-1180783
    GNL3Q9BVP23EBI-641666,EBI-641642
    PPP2CAP677753EBI-641666,EBI-712311
    PPP2R1AP301533EBI-641666,EBI-302388
    PPP2R1BP301542EBI-641666,EBI-357094
    SGOL1Q5FBB73EBI-641666,EBI-989069

    Protein-protein interaction databases

    BioGridi111517. 21 interactions.
    DIPiDIP-459N.
    IntActiQ15172. 22 interactions.
    MINTiMINT-88251.
    STRINGi9606.ENSP00000261461.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15172.
    SMRiQ15172. Positions 66-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 54Poly-Ser

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG264925.
    HOGENOMiHOG000067326.
    HOVERGENiHBG000009.
    InParanoidiQ15172.
    KOiK11584.
    OMAiDLFCQKL.
    OrthoDBiEOG7C2R2S.
    PhylomeDBiQ15172.
    TreeFamiTF105556.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR002554. PP2A_B56.
    [Graphical view]
    PANTHERiPTHR10257. PTHR10257. 1 hit.
    PfamiPF01603. B56. 1 hit.
    [Graphical view]
    PIRSFiPIRSF028043. PP2A_B56. 1 hit.
    SUPFAMiSSF48371. SSF48371. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15172-1) [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

    MSSSSPPAGA ASAAISASEK VDGFTRKSVR KAQRQKRSQG SSQFRSQGSQ    50
    AELHPLPQLK DATSNEQQEL FCQKLQQCCI LFDFMDSVSD LKSKEIKRAT 100
    LNELVEYVST NRGVIVESAY SDIVKMISAN IFRTLPPSDN PDFDPEEDEP 150
    TLEASWPHIQ LVYEFFLRFL ESPDFQPSIA KRYIDQKFVQ QLLELFDSED 200
    PRERDFLKTV LHRIYGKFLG LRAFIRKQIN NIFLRFIYET EHFNGVAELL 250
    EILGSIINGF ALPLKAEHKQ FLMKVLIPMH TAKGLALFHA QLAYCVVQFL 300
    EKDTTLTEPV IRGLLKFWPK TCSQKEVMFL GEIEEILDVI EPTQFKKIEE 350
    PLFKQISKCV SSSHFQVAER ALYFWNNEYI LSLIEENIDK ILPIMFASLY 400
    KISKEHWNPT IVALVYNVLK TLMEMNGKLF DDLTSSYKAE RQREKKKELE 450
    REELWKKLEE LKLKKALEKQ NSAYNMHSIL SNTSAE 486
    Length:486
    Mass (Da):56,194
    Last modified:November 1, 1996 - v1
    Checksum:iD31407F7032A6D44
    GO
    Isoform 2 (identifier: Q15172-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-61: MSSSSPPAGAASAAISASEKVDGFTRKSVRKAQRQKRSQGSSQFRSQGSQAELHPLPQLKD → MIMN

    Note: No experimental confirmation available.

    Show »
    Length:429
    Mass (Da):50,244
    Checksum:i8DF4B7962741F179
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521E → F AA sequence (PubMed:8694763)Curated
    Sequence conflicti54 – 541H → S AA sequence (PubMed:8694763)Curated
    Sequence conflicti176 – 1761Q → R in AAH22474. (PubMed:15489334)Curated
    Sequence conflicti389 – 3891D → N in AAH22474. (PubMed:15489334)Curated
    Sequence conflicti451 – 4511R → E AA sequence (PubMed:8694763)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6161MSSSS…PQLKD → MIMN in isoform 2. 1 PublicationVSP_042889Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42373 mRNA. Translation: AAC37601.1.
    AK302202 mRNA. Translation: BAH13648.1.
    AK312530 mRNA. Translation: BAG35429.1.
    AL451060, AL360091 Genomic DNA. Translation: CAH71821.1.
    AL360091, AL451060 Genomic DNA. Translation: CAH73229.1.
    CH471100 Genomic DNA. Translation: EAW93392.1.
    CH471100 Genomic DNA. Translation: EAW93393.1.
    BC022474 mRNA. Translation: AAH22474.1.
    BC110883 mRNA. Translation: AAI10884.1.
    CCDSiCCDS1503.1. [Q15172-1]
    CCDS55686.1. [Q15172-2]
    PIRiI55449.
    RefSeqiNP_001186685.1. NM_001199756.1. [Q15172-2]
    NP_006234.1. NM_006243.3. [Q15172-1]
    UniGeneiHs.744012.

    Genome annotation databases

    EnsembliENST00000261461; ENSP00000261461; ENSG00000066027. [Q15172-1]
    ENST00000537030; ENSP00000442866; ENSG00000066027. [Q15172-2]
    GeneIDi5525.
    KEGGihsa:5525.
    UCSCiuc001hjb.3. human. [Q15172-1]
    uc010ptd.2. human. [Q15172-2]

    Polymorphism databases

    DMDMi7387496.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42373 mRNA. Translation: AAC37601.1 .
    AK302202 mRNA. Translation: BAH13648.1 .
    AK312530 mRNA. Translation: BAG35429.1 .
    AL451060 , AL360091 Genomic DNA. Translation: CAH71821.1 .
    AL360091 , AL451060 Genomic DNA. Translation: CAH73229.1 .
    CH471100 Genomic DNA. Translation: EAW93392.1 .
    CH471100 Genomic DNA. Translation: EAW93393.1 .
    BC022474 mRNA. Translation: AAH22474.1 .
    BC110883 mRNA. Translation: AAI10884.1 .
    CCDSi CCDS1503.1. [Q15172-1 ]
    CCDS55686.1. [Q15172-2 ]
    PIRi I55449.
    RefSeqi NP_001186685.1. NM_001199756.1. [Q15172-2 ]
    NP_006234.1. NM_006243.3. [Q15172-1 ]
    UniGenei Hs.744012.

    3D structure databases

    ProteinModelPortali Q15172.
    SMRi Q15172. Positions 66-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111517. 21 interactions.
    DIPi DIP-459N.
    IntActi Q15172. 22 interactions.
    MINTi MINT-88251.
    STRINGi 9606.ENSP00000261461.

    Chemistry

    BindingDBi Q15172.
    ChEMBLi CHEMBL4763.

    PTM databases

    PhosphoSitei Q15172.

    Polymorphism databases

    DMDMi 7387496.

    2D gel databases

    OGPi Q15172.

    Proteomic databases

    MaxQBi Q15172.
    PaxDbi Q15172.
    PeptideAtlasi Q15172.
    PRIDEi Q15172.

    Protocols and materials databases

    DNASUi 5525.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261461 ; ENSP00000261461 ; ENSG00000066027 . [Q15172-1 ]
    ENST00000537030 ; ENSP00000442866 ; ENSG00000066027 . [Q15172-2 ]
    GeneIDi 5525.
    KEGGi hsa:5525.
    UCSCi uc001hjb.3. human. [Q15172-1 ]
    uc010ptd.2. human. [Q15172-2 ]

    Organism-specific databases

    CTDi 5525.
    GeneCardsi GC01P212458.
    HGNCi HGNC:9309. PPP2R5A.
    MIMi 601643. gene.
    neXtProti NX_Q15172.
    PharmGKBi PA33672.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264925.
    HOGENOMi HOG000067326.
    HOVERGENi HBG000009.
    InParanoidi Q15172.
    KOi K11584.
    OMAi DLFCQKL.
    OrthoDBi EOG7C2R2S.
    PhylomeDBi Q15172.
    TreeFami TF105556.

    Enzyme and pathway databases

    Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_23879. Platelet sensitization by LDL.
    REACT_682. Mitotic Prometaphase.
    SignaLinki Q15172.

    Miscellaneous databases

    ChiTaRSi PPP2R5A. human.
    GeneWikii PPP2R5A.
    GenomeRNAii 5525.
    NextBioi 21392.
    PROi Q15172.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15172.
    CleanExi HS_PPP2R5A.
    Genevestigatori Q15172.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR002554. PP2A_B56.
    [Graphical view ]
    PANTHERi PTHR10257. PTHR10257. 1 hit.
    Pfami PF01603. B56. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF028043. PP2A_B56. 1 hit.
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a new family of protein phosphatase 2A regulatory subunits."
      McCright B., Virshup D.M.
      J. Biol. Chem. 270:26123-26128(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Mammary cancer.
    2. "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 AND 2).
      Tissue: Testis and Tongue.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Hippocampus and Testis.
    6. "The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits."
      Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., Merlevede W., Goris J., Hemmings B.A.
      Biochem. J. 317:187-194(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 47-56; 129-132; 347-354; 448-462 AND 471-480.
      Tissue: Brain.
    7. "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm."
      McCright B., Rivers A.M., Audlin S., Virshup D.M.
      J. Biol. Chem. 271:22081-22089(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
    8. "Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
      Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
      Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SGOL1.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [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].

    Entry informationi

    Entry namei2A5A_HUMAN
    AccessioniPrimary (citable) accession number: Q15172
    Secondary accession number(s): B2R6D2
    , B7Z7L2, D3DT99, Q2NL72, Q5VVB2, Q8TBI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 135 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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