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Protein

Heterogeneous nuclear ribonucleoproteins A2/B1

Gene

Hnrnpa2b1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (By similarity). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoproteins A2/B1
Short name:
hnRNP A2/B1
Gene namesi
Name:Hnrnpa2b1
Synonyms:Hnrpa2b1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:104819. Hnrnpa2b1.

Subcellular locationi

  • Nucleusnucleoplasm By similarity
  • Cytoplasmic granule By similarity
  • Secretedexosome By similarity

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Not found in the nucleolus. Found in exosomes follwong sumoylation.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Secreted, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353Heterogeneous nuclear ribonucleoproteins A2/B1PRO_0000081837Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei29 – 291PhosphoserineCombined sources
Modified residuei85 – 851PhosphoserineCombined sources
Modified residuei104 – 1041N6,N6-dimethyllysineBy similarity
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei149 – 1491PhosphoserineBy similarity
Modified residuei168 – 1681N6-acetyllysineBy similarity
Modified residuei173 – 1731N6-acetyllysineBy similarity
Cross-linki186 – 186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei203 – 2031Dimethylated arginine; alternateBy similarity
Modified residuei203 – 2031Omega-N-methylarginine; alternateBy similarity
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei213 – 2131Dimethylated arginine; alternateBy similarity
Modified residuei213 – 2131Omega-N-methylarginine; alternateBy similarity
Modified residuei225 – 2251PhosphoserineCombined sources
Modified residuei231 – 2311PhosphoserineBy similarity
Modified residuei236 – 2361PhosphoserineBy similarity
Modified residuei259 – 2591PhosphoserineCombined sources
Modified residuei266 – 2661Asymmetric dimethylarginineBy similarity
Modified residuei324 – 3241PhosphoserineBy similarity
Modified residuei331 – 3311PhosphotyrosineBy similarity
Modified residuei341 – 3411PhosphoserineCombined sources
Modified residuei344 – 3441PhosphoserineCombined sources
Modified residuei347 – 3471PhosphotyrosineBy similarity

Post-translational modificationi

Sumoylated in exosomes, promoting miRNAs-binding.By similarity
Asymmetric dimethylation at Arg-266 constitutes the major methylation site (By similarity). According to a report, methlytion affects subcellular location and promotes nuclear localization (By similarity). According to another report, methylation at Arg-266 does not influence nucleocytoplasmic shuttling (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO88569.
MaxQBiO88569.
PaxDbiO88569.
PRIDEiO88569.
TopDownProteomicsiO88569-1. [O88569-1]
O88569-2. [O88569-2]
O88569-3. [O88569-3]

2D gel databases

REPRODUCTION-2DPAGEIPI00405058.
O88569.
SWISS-2DPAGEO88569.

PTM databases

iPTMnetiO88569.
PhosphoSiteiO88569.
SwissPalmiO88569.

Expressioni

Gene expression databases

BgeeiO88569.
CleanExiMM_HNRNPA2B1.
ExpressionAtlasiO88569. baseline and differential.
GenevisibleiO88569. MM.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1. Interacts with C9orf72. Interacts with DGCR8. Interacts with TARDBP. Interacts with CKAP5.By similarity

Protein-protein interaction databases

BioGridi207301. 7 interactions.
IntActiO88569. 7 interactions.
MINTiMINT-1866167.
STRINGi10090.ENSMUSP00000087453.

Structurei

3D structure databases

ProteinModelPortaliO88569.
SMRiO88569. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 10484RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini112 – 19180RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 353161Low complexity (LC) regionBy similarityAdd
BLAST
Regioni308 – 34740Nuclear targeting sequenceBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 157Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi202 – 353152Gly-richAdd
BLAST

Domaini

The low complexity (LC) region is intrinsically disordered. When incubated at high concentration, it is able to polymerize into labile, amyloid-like fibers and form cross-beta polymerization structures, probably driving the formation of hydrogels. In contrast to irreversible, pathogenic amyloids, the fibers polymerized from LC regions disassemble upon dilution. A number of evidences suggest that formation of cross-beta structures by LC regions mediate the formation of RNA granules, liquid-like droplets, and hydrogels.By similarity

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00760000118873.
HOVERGENiHBG002295.
InParanoidiO88569.
KOiK13158.
OMAiRESDWRE.
OrthoDBiEOG715Q6V.
PhylomeDBiO88569.
TreeFamiTF351342.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O88569-1) [UniParc]FASTAAdd to basket

Also known as: B1

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
MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC
60 70 80 90 100
VVMRDPASKR SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE
110 120 130 140 150
ESGKPGAHVT VKKLFVGGIK EDTEEHHLRD YFEEYGKIDT IEIITDRQSG
160 170 180 190 200
KKRGFGFVTF DDHDPVDKIV LQKYHTINGH NAEVRKALSR QEMQEVQSSR
210 220 230 240 250
SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF GDGYNGYGGG
260 270 280 290 300
PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGSY
310 320 330 340 350
NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR

SRY
Length:353
Mass (Da):37,403
Last modified:January 23, 2007 - v2
Checksum:iEC387DA3D8E989E4
GO
Isoform 2 (identifier: O88569-2) [UniParc]FASTAAdd to basket

Also known as: A2

The sequence of this isoform differs from the canonical sequence as follows:
     3-14: Missing.

Show »
Length:341
Mass (Da):35,979
Checksum:i99F5B66ED874EEFA
GO
Isoform 3 (identifier: O88569-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     3-14: Missing.
     252-291: Missing.

Show »
Length:301
Mass (Da):32,460
Checksum:i3F0336701AAEBEED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731K → E in BAE23274 (PubMed:16141072).Curated
Sequence conflicti214 – 2141G → V in BAE23274 (PubMed:16141072).Curated
Sequence conflicti299 – 2991S → T in AAC26867 (PubMed:12546712).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3 – 1412Missing in isoform 2 and isoform 3. 4 PublicationsVSP_022595Add
BLAST
Alternative sequencei252 – 29140Missing in isoform 3. 2 PublicationsVSP_025012Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF406651 mRNA. Translation: AAK98601.2.
AF452567 Genomic DNA. Translation: AAN16352.1.
AF073990 Genomic DNA. Translation: AAD29846.1.
AF073993 mRNA. Translation: AAC26867.1.
AK089012 mRNA. Translation: BAC40700.1.
AK137214 mRNA. Translation: BAE23274.1.
BC059107 mRNA. Translation: AAH59107.1.
BC141253 mRNA. Translation: AAI41254.1.
CCDSiCCDS51773.1. [O88569-3]
CCDS51774.1. [O88569-2]
RefSeqiNP_058086.2. NM_016806.3. [O88569-2]
NP_872591.1. NM_182650.4. [O88569-3]
XP_006506436.2. XM_006506373.2. [O88569-1]
XP_006506437.2. XM_006506374.2. [O88569-1]
XP_006544818.1. XM_006544755.2. [O88569-2]
XP_006544819.1. XM_006544756.2. [O88569-3]
UniGeneiMm.155896.

Genome annotation databases

EnsembliENSMUST00000069949; ENSMUSP00000067491; ENSMUSG00000004980. [O88569-3]
ENSMUST00000090002; ENSMUSP00000087453; ENSMUSG00000004980. [O88569-2]
ENSMUST00000114459; ENSMUSP00000110103; ENSMUSG00000004980. [O88569-1]
ENSMUST00000203220; ENSMUSP00000145374; ENSMUSG00000004980. [O88569-2]
ENSMUST00000203954; ENSMUSP00000145028; ENSMUSG00000004980. [O88569-1]
ENSMUST00000204158; ENSMUSP00000145383; ENSMUSG00000004980. [O88569-3]
ENSMUST00000204188; ENSMUSP00000145245; ENSMUSG00000004980. [O88569-3]
GeneIDi102642938.
53379.
KEGGimmu:102642938.
mmu:53379.
UCSCiuc009bxm.2. mouse. [O88569-3]
uc009bxn.2. mouse. [O88569-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF406651 mRNA. Translation: AAK98601.2.
AF452567 Genomic DNA. Translation: AAN16352.1.
AF073990 Genomic DNA. Translation: AAD29846.1.
AF073993 mRNA. Translation: AAC26867.1.
AK089012 mRNA. Translation: BAC40700.1.
AK137214 mRNA. Translation: BAE23274.1.
BC059107 mRNA. Translation: AAH59107.1.
BC141253 mRNA. Translation: AAI41254.1.
CCDSiCCDS51773.1. [O88569-3]
CCDS51774.1. [O88569-2]
RefSeqiNP_058086.2. NM_016806.3. [O88569-2]
NP_872591.1. NM_182650.4. [O88569-3]
XP_006506436.2. XM_006506373.2. [O88569-1]
XP_006506437.2. XM_006506374.2. [O88569-1]
XP_006544818.1. XM_006544755.2. [O88569-2]
XP_006544819.1. XM_006544756.2. [O88569-3]
UniGeneiMm.155896.

3D structure databases

ProteinModelPortaliO88569.
SMRiO88569. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207301. 7 interactions.
IntActiO88569. 7 interactions.
MINTiMINT-1866167.
STRINGi10090.ENSMUSP00000087453.

PTM databases

iPTMnetiO88569.
PhosphoSiteiO88569.
SwissPalmiO88569.

2D gel databases

REPRODUCTION-2DPAGEIPI00405058.
O88569.
SWISS-2DPAGEO88569.

Proteomic databases

EPDiO88569.
MaxQBiO88569.
PaxDbiO88569.
PRIDEiO88569.
TopDownProteomicsiO88569-1. [O88569-1]
O88569-2. [O88569-2]
O88569-3. [O88569-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000069949; ENSMUSP00000067491; ENSMUSG00000004980. [O88569-3]
ENSMUST00000090002; ENSMUSP00000087453; ENSMUSG00000004980. [O88569-2]
ENSMUST00000114459; ENSMUSP00000110103; ENSMUSG00000004980. [O88569-1]
ENSMUST00000203220; ENSMUSP00000145374; ENSMUSG00000004980. [O88569-2]
ENSMUST00000203954; ENSMUSP00000145028; ENSMUSG00000004980. [O88569-1]
ENSMUST00000204158; ENSMUSP00000145383; ENSMUSG00000004980. [O88569-3]
ENSMUST00000204188; ENSMUSP00000145245; ENSMUSG00000004980. [O88569-3]
GeneIDi102642938.
53379.
KEGGimmu:102642938.
mmu:53379.
UCSCiuc009bxm.2. mouse. [O88569-3]
uc009bxn.2. mouse. [O88569-2]

Organism-specific databases

CTDi3181.
MGIiMGI:104819. Hnrnpa2b1.

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00760000118873.
HOVERGENiHBG002295.
InParanoidiO88569.
KOiK13158.
OMAiRESDWRE.
OrthoDBiEOG715Q6V.
PhylomeDBiO88569.
TreeFamiTF351342.

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiHnrnpa2b1. mouse.
PROiO88569.
SOURCEiSearch...

Gene expression databases

BgeeiO88569.
CleanExiMM_HNRNPA2B1.
ExpressionAtlasiO88569. baseline and differential.
GenevisibleiO88569. MM.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Intracellular trafficking of hnRNP A2 in oligodendrocytes."
    Brumwell C., Antolik C., Carson J.H., Barbarese E.
    Exp. Cell Res. 279:310-320(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C3Heb/FeJ.
    Tissue: Brain.
  2. "Characterization of the mouse hnRNP A2/B1/B0 gene and identification of processed pseudogenes."
    Hatfield J.T., Rothnagel J.A., Smith R.
    Gene 295:33-42(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    Strain: BALB/cJ.
  3. "Gene trap mutagenesis of hnRNP A2/B1: a cryptic 3' splice site in the neomycin resistance gene allows continued expression of the disrupted cellular gene."
    Roshon M., DeGregori J.V., Ruley H.E.
    BMC Genomics 4:2-2(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Strain: C57BL/6J and NOD.
    Tissue: Thymus and Urinary bladder.
  5. Lubec G., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 23-38; 47-54; 114-120; 138-147; 154-168; 174-185; 191-200 AND 204-228, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Brain and Hippocampus.
  6. "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 3).
    Strain: FVB/N.
    Tissue: Brain and Mammary tumor.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-85; SER-212; SER-225; SER-259; SER-341 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiROA2_MOUSE
AccessioniPrimary (citable) accession number: O88569
Secondary accession number(s): B9EJ02
, Q3UVJ5, Q6PCV9, Q8C2A0, Q8CJ71, Q91ZR9, Q9R204
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.