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O95218

- ZRAB2_HUMAN

UniProt

O95218 - ZRAB2_HUMAN

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Protein

Zinc finger Ran-binding domain-containing protein 2

Gene

ZRANB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Splice factor required for alternative splicing of TRA2B/SFRS10 transcripts. May interfere with constitutive 5'-splice site selection.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri9 – 4032RanBP2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri65 – 9430RanBP2-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. RNA binding Source: ProtInc
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: GOC
  3. RNA splicing Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger Ran-binding domain-containing protein 2
Alternative name(s):
Zinc finger protein 265
Zinc finger, splicing
Gene namesi
Name:ZRANB2
Synonyms:ZIS, ZNF265
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:13058. ZRANB2.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37636.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Zinc finger Ran-binding domain-containing protein 2PRO_0000066585Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine1 Publication
Modified residuei18 – 181N6-acetyllysineBy similarity
Modified residuei54 – 541N6-acetyllysine1 Publication
Modified residuei92 – 921N6-acetyllysineBy similarity
Modified residuei120 – 1201Phosphoserine7 Publications
Modified residuei153 – 1531Phosphoserine5 Publications
Modified residuei181 – 1811Phosphoserine4 Publications
Modified residuei188 – 1881Phosphoserine5 Publications
Modified residuei193 – 1931Phosphoserine3 Publications

Post-translational modificationi

Isoform 2 is phosphorylated on Ser-310 upon DNA damage, probably by ATM or ATR.7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95218.
PaxDbiO95218.
PRIDEiO95218.

PTM databases

PhosphoSiteiO95218.

Expressioni

Gene expression databases

BgeeiO95218.
CleanExiHS_ZRANB2.
ExpressionAtlasiO95218. baseline and differential.
GenevestigatoriO95218.

Organism-specific databases

HPAiHPA053960.
HPA063298.

Interactioni

Subunit structurei

Interacts with the C-terminal half of SNRNP70, the Arg/Ser-rich domain of AKAP17A as well as with U2AF1 and CLK1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKAP17AQ020404EBI-1051583,EBI-1042725
ARRB1P494074EBI-1051583,EBI-743313
ARRB2P321214EBI-1051583,EBI-714559

Protein-protein interaction databases

BioGridi114802. 71 interactions.
IntActiO95218. 12 interactions.
STRINGi9606.ENSP00000359958.

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123Combined sources
Turni18 – 203Combined sources
Beta strandi32 – 343Combined sources
Beta strandi65 – 684Combined sources
Turni72 – 743Combined sources
Turni86 – 883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N0ZNMR-A1-40[»]
2K1PNMR-A65-95[»]
3G9YX-ray1.40A65-95[»]
ProteinModelPortaliO95218.
SMRiO95218. Positions 1-40, 67-95.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95218.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 324174Required for nuclear targetingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi198 – 26265Arg/Ser-richAdd
BLAST

Domaini

The RanBP2-type zinc fingers mediate binding to RNA.

Sequence similaritiesi

Belongs to the ZRANB2 family.Curated
Contains 2 RanBP2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri9 – 4032RanBP2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri65 – 9430RanBP2-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG275779.
GeneTreeiENSGT00730000111078.
HOVERGENiHBG066285.
InParanoidiO95218.
OMAiRSPERHH.
OrthoDBiEOG7ZD1XK.
PhylomeDBiO95218.
TreeFamiTF105996.

Family and domain databases

Gene3Di4.10.1060.10. 2 hits.
InterProiIPR017337. UCP037956_Znf_RanB2.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF00641. zf-RanBP. 2 hits.
[Graphical view]
PIRSFiPIRSF037956. UCP037956_ZnF_Ran. 1 hit.
SMARTiSM00547. ZnF_RBZ. 2 hits.
[Graphical view]
PROSITEiPS01358. ZF_RANBP2_1. 2 hits.
PS50199. ZF_RANBP2_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95218-1) [UniParc]FASTAAdd to Basket

Also known as: ZIS-1

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
MSTKNFRVSD GDWICPDKKC GNVNFARRTS CNRCGREKTT EAKMMKAGGT
60 70 80 90 100
EIGKTLAEKS RGLFSANDWQ CKTCSNVNWA RRSECNMCNT PKYAKLEERT
110 120 130 140 150
GYGGGFNERE NVEYIEREES DGEYDEFGRK KKKYRGKAVG PASILKEVED
160 170 180 190 200
KESEGEEEDE DEDLSKYKLD EDEDEDDADL SKYNLDASEE EDSNKKKSNR
210 220 230 240 250
RSRSKSRSSH SRSSSRSSSP SSSRSRSRSR SRSSSSSQSR SRSSSRERSR
260 270 280 290 300
SRGSKSRSSS RSHRGSSSPR KRSYSSSSSS PERNRKRSRS RSSSSGDRKK
310 320 330
RRTRSRSPER RHRSSSGSSH SGSRSSSKKK
Length:330
Mass (Da):37,404
Last modified:May 1, 2007 - v2
Checksum:i99BE2D12EBE0FF8E
GO
Isoform 2 (identifier: O95218-2) [UniParc]FASTAAdd to Basket

Also known as: ZIS-2

The sequence of this isoform differs from the canonical sequence as follows:
     310-330: RRHRSSSGSSHSGSRSSSKKK → SQVIGENTKQP

Note: Contains a phosphoserine at position 305. Contains a phosphoserine at position 307. Contains a phosphoserine at position 310. Contains a phosphothreonine at position 303.

Show »
Length:320
Mass (Da):36,318
Checksum:i15F1DFB7CD6CF611
GO

Sequence cautioni

The sequence AAD09746.1 differs from that shown. Reason: Frameshift at position 236. Curated
The sequence AAD09747.1 differs from that shown. Reason: Frameshift at position 236. Curated
The sequence BAD92805.1 differs from that shown. Reason: Intron retention.Curated
The sequence CAB66879.1 differs from that shown. Reason: Frameshift at position 236. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411E → G in BAD96578. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071R → G.2 Publications
Corresponds to variant rs11583800 [ dbSNP | Ensembl ].
VAR_030783

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei310 – 33021RRHRS…SSKKK → SQVIGENTKQP in isoform 2. 5 PublicationsVSP_024945Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF065391 mRNA. Translation: AAD09746.1. Frameshift.
AF065392 mRNA. Translation: AAD09747.1. Frameshift.
AL136945 mRNA. Translation: CAB66879.1. Frameshift.
AB209568 mRNA. Translation: BAD92805.1. Sequence problems.
AK222858 mRNA. Translation: BAD96578.1.
AL512443 Genomic DNA. Translation: CAH70058.1.
AL512443 Genomic DNA. Translation: CAH70059.1.
CH471059 Genomic DNA. Translation: EAX06433.1.
CH471059 Genomic DNA. Translation: EAX06435.1.
BC039814 mRNA. Translation: AAH39814.1.
CCDSiCCDS659.1. [O95218-1]
CCDS660.1. [O95218-2]
RefSeqiNP_005446.2. NM_005455.4. [O95218-2]
NP_976225.1. NM_203350.2. [O95218-1]
UniGeneiHs.194718.

Genome annotation databases

EnsembliENST00000254821; ENSP00000254821; ENSG00000132485. [O95218-2]
ENST00000370920; ENSP00000359958; ENSG00000132485. [O95218-1]
ENST00000610633; ENSP00000480576; ENSG00000132485.
ENST00000611683; ENSP00000482026; ENSG00000132485. [O95218-2]
GeneIDi9406.
KEGGihsa:9406.
UCSCiuc001dfs.3. human. [O95218-2]
uc001dft.3. human. [O95218-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF065391 mRNA. Translation: AAD09746.1 . Frameshift.
AF065392 mRNA. Translation: AAD09747.1 . Frameshift.
AL136945 mRNA. Translation: CAB66879.1 . Frameshift.
AB209568 mRNA. Translation: BAD92805.1 . Sequence problems.
AK222858 mRNA. Translation: BAD96578.1 .
AL512443 Genomic DNA. Translation: CAH70058.1 .
AL512443 Genomic DNA. Translation: CAH70059.1 .
CH471059 Genomic DNA. Translation: EAX06433.1 .
CH471059 Genomic DNA. Translation: EAX06435.1 .
BC039814 mRNA. Translation: AAH39814.1 .
CCDSi CCDS659.1. [O95218-1 ]
CCDS660.1. [O95218-2 ]
RefSeqi NP_005446.2. NM_005455.4. [O95218-2 ]
NP_976225.1. NM_203350.2. [O95218-1 ]
UniGenei Hs.194718.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N0Z NMR - A 1-40 [» ]
2K1P NMR - A 65-95 [» ]
3G9Y X-ray 1.40 A 65-95 [» ]
ProteinModelPortali O95218.
SMRi O95218. Positions 1-40, 67-95.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114802. 71 interactions.
IntActi O95218. 12 interactions.
STRINGi 9606.ENSP00000359958.

PTM databases

PhosphoSitei O95218.

Proteomic databases

MaxQBi O95218.
PaxDbi O95218.
PRIDEi O95218.

Protocols and materials databases

DNASUi 9406.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000254821 ; ENSP00000254821 ; ENSG00000132485 . [O95218-2 ]
ENST00000370920 ; ENSP00000359958 ; ENSG00000132485 . [O95218-1 ]
ENST00000610633 ; ENSP00000480576 ; ENSG00000132485 .
ENST00000611683 ; ENSP00000482026 ; ENSG00000132485 . [O95218-2 ]
GeneIDi 9406.
KEGGi hsa:9406.
UCSCi uc001dfs.3. human. [O95218-2 ]
uc001dft.3. human. [O95218-1 ]

Organism-specific databases

CTDi 9406.
GeneCardsi GC01M071528.
HGNCi HGNC:13058. ZRANB2.
HPAi HPA053960.
HPA063298.
MIMi 604347. gene.
neXtProti NX_O95218.
PharmGKBi PA37636.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG275779.
GeneTreei ENSGT00730000111078.
HOVERGENi HBG066285.
InParanoidi O95218.
OMAi RSPERHH.
OrthoDBi EOG7ZD1XK.
PhylomeDBi O95218.
TreeFami TF105996.

Miscellaneous databases

EvolutionaryTracei O95218.
GeneWikii ZRANB2.
GenomeRNAii 9406.
NextBioi 35236.
PROi O95218.
SOURCEi Search...

Gene expression databases

Bgeei O95218.
CleanExi HS_ZRANB2.
ExpressionAtlasi O95218. baseline and differential.
Genevestigatori O95218.

Family and domain databases

Gene3Di 4.10.1060.10. 2 hits.
InterProi IPR017337. UCP037956_Znf_RanB2.
IPR001876. Znf_RanBP2.
[Graphical view ]
Pfami PF00641. zf-RanBP. 2 hits.
[Graphical view ]
PIRSFi PIRSF037956. UCP037956_ZnF_Ran. 1 hit.
SMARTi SM00547. ZnF_RBZ. 2 hits.
[Graphical view ]
PROSITEi PS01358. ZF_RANBP2_1. 2 hits.
PS50199. ZF_RANBP2_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, characterization and mapping of the human ZIS (zinc-finger, splicing) gene."
    Nakano M., Yoshiura K., Oikawa M., Miyoshi O., Yamada K., Kondo S., Miwa N., Soeda E., Jinno Y., Fujii T., Niikawa N.
    Gene 225:59-65(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Fetal brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Uterus.
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-207.
  7. "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 2), VARIANT GLY-207.
    Tissue: Skin.
  8. "ZNF265 -- a novel spliceosomal protein able to induce alternative splicing."
    Adams D.J., van der Weyden L., Mayeda A., Stamm S., Morris B.J., Rasko J.E.J.
    J. Cell Biol. 154:25-32(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNRNP70; U2AF1 AND CLK1.
  9. "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-120; SER-153; SER-181; SER-188 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "XE7: a novel splicing factor that interacts with ASF/SF2 and ZNF265."
    Mangs A.H., Speirs H.J.L., Goy C., Adams D.J., Markus M.A., Morris B.J.
    Nucleic Acids Res. 34:4976-4986(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKAP17A.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305; SER-307 AND SER-310 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-153; SER-181 AND SER-188, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303; SER-305; SER-307 AND SER-310 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-120 AND SER-188, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-307 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-9; SER-120; SER-153; SER-181; SER-188 AND SER-193, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305; SER-307 AND SER-310 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-120; SER-153; SER-181; SER-188 AND SER-193, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303; SER-305 AND SER-307 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: STRUCTURE BY NMR OF 1-40, RNA-BINDING.

Entry informationi

Entry nameiZRAB2_HUMAN
AccessioniPrimary (citable) accession number: O95218
Secondary accession number(s): D3DQ75
, Q53GS3, Q59F92, Q5VV33, Q5VV34, Q8IXN6, Q9UP63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2007
Last modified: November 26, 2014
This is version 134 of the entry and version 2 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

3D-structure, 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3