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Protein

Ribonucleoprotein PTB-binding 1

Gene

RAVER1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA (By similarity).By similarity

GO - Molecular functioni

  • nucleic acid binding Source: GO_Central
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoprotein PTB-binding 1
Alternative name(s):
Protein raver-1
Gene namesi
Name:RAVER1
Synonyms:KIAA1978
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:30296. RAVER1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Nuclear, in perinucleolar structures. Shuttles between nucleus and cytoplasm. Cytoplasm, at focal contacts and cell-cell contacts. Associated with myotubes during muscle differentiation (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA144596390.

Polymorphism and mutation databases

BioMutaiRAVER1.
DMDMi74759693.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 606605Ribonucleoprotein PTB-binding 1PRO_0000081487Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei6 – 61PhosphoserineCombined sources
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei463 – 4631PhosphothreonineCombined sources
Modified residuei474 – 4741PhosphoserineCombined sources
Modified residuei562 – 5621PhosphoserineBy similarity
Isoform 2 (identifier: Q8IY67-2)
Modified residuei488 – 4881PhosphothreonineCombined sources
Modified residuei567 – 5671PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8IY67.
MaxQBiQ8IY67.
PaxDbiQ8IY67.
PeptideAtlasiQ8IY67.
PRIDEiQ8IY67.

PTM databases

iPTMnetiQ8IY67.

Expressioni

Gene expression databases

CleanExiHS_RAVER1.
ExpressionAtlasiQ8IY67. baseline and differential.
GenevisibleiQ8IY67. HS.

Organism-specific databases

HPAiHPA043575.
HPA049457.

Interactioni

Subunit structurei

Interacts with PTBP1, RAVER2, VCL and ACTN1. Part of a complex containing RAVER1, VCL and ACTN1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi125936. 57 interactions.
DIPiDIP-46973N.
IntActiQ8IY67. 5 interactions.
MINTiMINT-2812331.
STRINGi9606.ENSP00000293677.

Structurei

Secondary structure

1
606
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi41 – 5616Combined sources
Beta strandi60 – 645Combined sources
Helixi72 – 787Combined sources
Turni79 – 813Combined sources
Beta strandi84 – 907Combined sources
Turni91 – 944Combined sources
Beta strandi95 – 1028Combined sources
Helixi103 – 11311Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi133 – 1386Combined sources
Helixi145 – 1528Combined sources
Helixi153 – 1553Combined sources
Beta strandi158 – 1658Combined sources
Turni167 – 1693Combined sources
Beta strandi172 – 18211Combined sources
Helixi183 – 19311Combined sources
Beta strandi204 – 2074Combined sources
Helixi210 – 2123Combined sources
Turni215 – 2184Combined sources
Beta strandi221 – 2266Combined sources
Helixi235 – 2417Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi249 – 2557Combined sources
Beta strandi261 – 2688Combined sources
Helixi272 – 28211Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi299 – 3013Combined sources
Helixi303 – 31311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H2UX-ray2.75B/D39-321[»]
3H2VX-ray2.90E/F/G/H59-130[»]
3SMZX-ray1.99A39-320[»]
3VF0X-ray2.54B39-321[»]
ProteinModelPortaliQ8IY67.
SMRiQ8IY67. Positions 39-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IY67.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 13072RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini132 – 21079RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini221 – 29979RRM 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni307 – 39589Interaction with PTBP1By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 6016Nuclear localization signalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi406 – 46863Pro-richAdd
BLAST

Sequence similaritiesi

Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IJBP. Eukaryota.
ENOG410ZP6I. LUCA.
GeneTreeiENSGT00390000006046.
HOGENOMiHOG000253941.
HOVERGENiHBG059515.
InParanoidiQ8IY67.
PhylomeDBiQ8IY67.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: Q8IY67-1) [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
MAADVSVTHR PPLSPKSGAE VEAGDAAERR APEEELPPLD PEEIRKRLEH
60 70 80 90 100
TERQFRNRRK ILIRGLPGDV TNQEVHDLLS DYELKYCFVD KYKGTAFVTL
110 120 130 140 150
LNGEQAEAAI NAFHQSRLRE RELSVQLQPT DALLCVANLP PSLTQQQFEE
160 170 180 190 200
LVRPFGSLER CFLVYSERTG QSKGYGFAEY MKKDSAARAK SDLLGKPLGP
210 220 230 240 250
RTLYVHWTDA GQLTPALLHS RCLCVDRLPP GFNDVDALCR ALSAVHSPTF
260 270 280 290 300
CQLACGQDGQ LKGFAVLEYE TAEMAEEAQQ QADGLSLGGS HLRVSFCAPG
310 320 330 340 350
PPGRSMLAAL IAAQATALNR GKGLLPEPNI LQLLNNLGPS ASLQLLLNPL
360 370 380 390 400
LHGSAGGKQG LLGAPPAMPL LNGPALSTAL LQLALQTQGQ KKPGILGDSP
410 420 430 440 450
LGALQPGAQP ANPLLGELPA GGGLPPELPP RRGKPPPLLP SVLGPAGGDR
460 470 480 490 500
EALGLGPPAA QLTPPPAPVG LRGSGLRGPL SHFYSGSPTS YFTSGLQAGL
510 520 530 540 550
KQSHLSKAIG SSPLGSGEGL LGLSPGPNGH SHLLKVRAGG GDMQGWEAPA
560 570 580 590 600
PQRPLTRPAL PSVSRPHWAA RNAALPTCCP RPSPAQKAAM WASTPRASAA

TTRTPT
Length:606
Mass (Da):63,877
Last modified:March 1, 2003 - v1
Checksum:i09FA9935A6281B42
GO
Isoform 2 (identifier: Q8IY67-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     477-477: R → RGLQKDSGPL...GERSSGGSGG
     536-606: VRAGGGDMQG...ASAATTRTPT → TPLGGQKRSF...DSYLKRKRIF

Show »
Length:739
Mass (Da):77,860
Checksum:i62EAC25B58B730C8
GO
Isoform 3 (identifier: Q8IY67-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-75: EV → PS
     76-606: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:75
Mass (Da):8,419
Checksum:i5FDDB0267473DDDC
GO

Sequence cautioni

The sequence AAH37565.1 differs from that shown.Probable cloning artifact.Curated
The sequence BAB85564.1 differs from that shown.Intron retention.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei74 – 752EV → PS in isoform 3. 1 PublicationVSP_040968
Alternative sequencei76 – 606531Missing in isoform 3. 1 PublicationVSP_040969Add
BLAST
Alternative sequencei477 – 4771R → RGLQKDSGPLPTPPGVSLLG EPPKDYRIPLNPYLNLHSLL PASNLAGKEARGWGGAGRSR RPAEGPLTNPPAPGGGSSSS KAFQLKSRLLSPLSSARLPP EPGLSDSYSFDYPSDMGPRR LFSHPREPALGPHGPSRHKM SPPPSGFGERSSGGSGG in isoform 2. 1 PublicationVSP_017035
Alternative sequencei536 – 60671VRAGG…TRTPT → TPLGGQKRSFAHLLPSPEPS PEGSYVGQHSQGLGGHYADS YLKRKRIF in isoform 2. 1 PublicationVSP_017036Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB075858 mRNA. Translation: BAB85564.1. Sequence problems.
AC011511 Genomic DNA. No translation available.
BC037428 mRNA. No translation available.
BC037565 mRNA. Translation: AAH37565.1. Sequence problems.
RefSeqiNP_597709.2. NM_133452.2.
UniGeneiHs.744952.

Genome annotation databases

EnsembliENST00000615032; ENSP00000479520; ENSG00000161847. [Q8IY67-1]
GeneIDi125950.
KEGGihsa:125950.
UCSCiuc060tgw.1. human. [Q8IY67-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB075858 mRNA. Translation: BAB85564.1. Sequence problems.
AC011511 Genomic DNA. No translation available.
BC037428 mRNA. No translation available.
BC037565 mRNA. Translation: AAH37565.1. Sequence problems.
RefSeqiNP_597709.2. NM_133452.2.
UniGeneiHs.744952.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H2UX-ray2.75B/D39-321[»]
3H2VX-ray2.90E/F/G/H59-130[»]
3SMZX-ray1.99A39-320[»]
3VF0X-ray2.54B39-321[»]
ProteinModelPortaliQ8IY67.
SMRiQ8IY67. Positions 39-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125936. 57 interactions.
DIPiDIP-46973N.
IntActiQ8IY67. 5 interactions.
MINTiMINT-2812331.
STRINGi9606.ENSP00000293677.

PTM databases

iPTMnetiQ8IY67.

Polymorphism and mutation databases

BioMutaiRAVER1.
DMDMi74759693.

Proteomic databases

EPDiQ8IY67.
MaxQBiQ8IY67.
PaxDbiQ8IY67.
PeptideAtlasiQ8IY67.
PRIDEiQ8IY67.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000615032; ENSP00000479520; ENSG00000161847. [Q8IY67-1]
GeneIDi125950.
KEGGihsa:125950.
UCSCiuc060tgw.1. human. [Q8IY67-1]

Organism-specific databases

CTDi125950.
GeneCardsiRAVER1.
H-InvDBHIX0202703.
HGNCiHGNC:30296. RAVER1.
HPAiHPA043575.
HPA049457.
MIMi609950. gene.
neXtProtiNX_Q8IY67.
PharmGKBiPA144596390.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJBP. Eukaryota.
ENOG410ZP6I. LUCA.
GeneTreeiENSGT00390000006046.
HOGENOMiHOG000253941.
HOVERGENiHBG059515.
InParanoidiQ8IY67.
PhylomeDBiQ8IY67.

Miscellaneous databases

ChiTaRSiRAVER1. human.
EvolutionaryTraceiQ8IY67.
GeneWikiiRAVER1.
GenomeRNAii125950.
PROiQ8IY67.
SOURCEiSearch...

Gene expression databases

CleanExiHS_RAVER1.
ExpressionAtlasiQ8IY67. baseline and differential.
GenevisibleiQ8IY67. HS.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 182-606 (ISOFORM 2).
    Tissue: Cervix and Uterus.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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 THR-463, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-488 AND SER-567 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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 THR-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-463 AND SER-474, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-488 AND SER-567 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND THR-463, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-14 AND THR-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRAVR1_HUMAN
AccessioniPrimary (citable) accession number: Q8IY67
Secondary accession number(s): A6NMU4, Q8IY60, Q8TF24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 131 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.