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Q15172

- 2A5A_HUMAN

UniProt

Q15172 - 2A5A_HUMAN

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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

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 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
Complete GO annotation...

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-KW
  2. cytoplasm Source: BHF-UCL
  3. M band Source: BHF-UCL
  4. nucleus Source: UniProtKB-KW
  5. protein phosphatase type 2A complex Source: UniProtKB
  6. Z disc Source: Ensembl
Complete GO annotation...

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 – 411Phosphoserine3 Publications
Modified residuei42 – 421Phosphoserine3 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. 27 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.
GeneTreeiENSGT00550000074525.
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

        10         20         30         40         50
MSSSSPPAGA ASAAISASEK VDGFTRKSVR KAQRQKRSQG SSQFRSQGSQ
60 70 80 90 100
AELHPLPQLK DATSNEQQEL FCQKLQQCCI LFDFMDSVSD LKSKEIKRAT
110 120 130 140 150
LNELVEYVST NRGVIVESAY SDIVKMISAN IFRTLPPSDN PDFDPEEDEP
160 170 180 190 200
TLEASWPHIQ LVYEFFLRFL ESPDFQPSIA KRYIDQKFVQ QLLELFDSED
210 220 230 240 250
PRERDFLKTV LHRIYGKFLG LRAFIRKQIN NIFLRFIYET EHFNGVAELL
260 270 280 290 300
EILGSIINGF ALPLKAEHKQ FLMKVLIPMH TAKGLALFHA QLAYCVVQFL
310 320 330 340 350
EKDTTLTEPV IRGLLKFWPK TCSQKEVMFL GEIEEILDVI EPTQFKKIEE
360 370 380 390 400
PLFKQISKCV SSSHFQVAER ALYFWNNEYI LSLIEENIDK ILPIMFASLY
410 420 430 440 450
KISKEHWNPT IVALVYNVLK TLMEMNGKLF DDLTSSYKAE RQREKKKELE
460 470 480
REELWKKLEE LKLKKALEKQ NSAYNMHSIL SNTSAE
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. 27 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.
GeneTreei ENSGT00550000074525.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 136 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