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Protein

Ribosome-binding protein 1

Gene

RRBP1

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

Functioni

Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane.By similarity

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • receptor activity Source: ProtInc

GO - Biological processi

  • osteoblast differentiation Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • translation Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome-binding protein 1
Alternative name(s):
180 kDa ribosome receptor homolog
Short name:
RRp
ES/130-related protein
Ribosome receptor protein
Gene namesi
Name:RRBP1
Synonyms:KIAA1398
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:10448. RRBP1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77LumenalSequence analysis
Transmembranei8 – 2821HelicalSequence analysisAdd
BLAST
Topological domaini29 – 14101382CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: HPA
  • integral component of endoplasmic reticulum membrane Source: GO_Central
  • membrane Source: UniProtKB
  • ribosome Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34863.

Polymorphism and mutation databases

BioMutaiRRBP1.
DMDMi23822112.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14101410Ribosome-binding protein 1PRO_0000097441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei159 – 1591PhosphoserineBy similarity
Modified residuei165 – 1651PhosphoserineBy similarity
Modified residuei225 – 2251PhosphothreonineCombined sources
Modified residuei235 – 2351PhosphothreonineCombined sources
Modified residuei245 – 2451PhosphothreonineCombined sources
Modified residuei255 – 2551PhosphothreonineCombined sources
Modified residuei533 – 5331PhosphoserineCombined sources
Modified residuei573 – 5731PhosphoserineCombined sources
Modified residuei583 – 5831PhosphoserineCombined sources
Modified residuei615 – 6151PhosphoserineCombined sources
Modified residuei900 – 9001PhosphoserineCombined sources
Modified residuei932 – 9321N6-acetyllysineBy similarity
Modified residuei959 – 9591PhosphoserineCombined sources
Modified residuei978 – 9781PhosphoserineCombined sources
Modified residuei1276 – 12761PhosphoserineCombined sources
Modified residuei1277 – 12771PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9P2E9.
MaxQBiQ9P2E9.
PaxDbiQ9P2E9.
PRIDEiQ9P2E9.

PTM databases

iPTMnetiQ9P2E9.
PhosphoSiteiQ9P2E9.
SwissPalmiQ9P2E9.

Expressioni

Gene expression databases

BgeeiQ9P2E9.
ExpressionAtlasiQ9P2E9. baseline and differential.
GenevisibleiQ9P2E9. HS.

Organism-specific databases

HPAiHPA009026.
HPA011924.

Interactioni

Protein-protein interaction databases

BioGridi112152. 46 interactions.
IntActiQ9P2E9. 17 interactions.
MINTiMINT-5006662.
STRINGi9606.ENSP00000354045.

Structurei

3D structure databases

ProteinModelPortaliQ9P2E9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati197 – 206101
Repeati207 – 216102
Repeati217 – 226103
Repeati227 – 236104
Repeati237 – 246105
Repeati247 – 256106
Repeati257 – 266107
Repeati267 – 276108
Repeati277 – 286109
Repeati287 – 2961010
Repeati297 – 3061011
Repeati307 – 3161012
Repeati317 – 3261013
Repeati327 – 3361014
Repeati337 – 3461015
Repeati347 – 3561016
Repeati357 – 3661017
Repeati367 – 3761018
Repeati377 – 3861019
Repeati387 – 3961020
Repeati397 – 4061021
Repeati407 – 4161022
Repeati417 – 4261023
Repeati427 – 4361024
Repeati437 – 4461025
Repeati447 – 4561026
Repeati457 – 4661027
Repeati467 – 4761028
Repeati477 – 4861029
Repeati487 – 4961030
Repeati497 – 5061031
Repeati507 – 5161032
Repeati517 – 5261033
Repeati527 – 534834; approximate
Repeati535 – 5441035
Repeati545 – 5541036; approximate
Repeati555 – 5641037
Repeati565 – 5741038
Repeati575 – 5841039; approximate
Repeati585 – 5941040
Repeati595 – 6041041

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni197 – 60440841 X 10 AA approximate tandem repeats of [TN]-Q-[GSA]-[KRQT]-K-[ATGSV]-[ED]-[GTAS]-[ATIS]-[PQTAS]Add
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFNK. Eukaryota.
ENOG410XY8H. LUCA.
GeneTreeiENSGT00530000063895.
HOVERGENiHBG061483.
InParanoidiQ9P2E9.
KOiK14000.
OrthoDBiEOG7ZWD1D.
PhylomeDBiQ9P2E9.
TreeFamiTF333579.

Family and domain databases

InterProiIPR007794. Rib_rcpt_KP.
[Graphical view]
PfamiPF05104. Rib_recp_KP_reg. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Note: Additional isoforms seem to exist. Additional isoforms are probable deriving from alternative splicing in the repeat region.

Isoform 3 (identifier: Q9P2E9-1) [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
MDIYDTQTLG VVVFGGFMVV SAIGIFLVST FSMKETSYEE ALANQRKEMA
60 70 80 90 100
KTHHQKVEKK KKEKTVEKKG KTKKKEEKPN GKIPDHDPAP NVTVLLREPV
110 120 130 140 150
RAPAVAVAPT PVQPPIIVAP VATVPAMPQE KLASSPKDKK KKEKKVAKVE
160 170 180 190 200
PAVSSVVNSI QVLTSKAAIL ETAPKEVPMV VVPPVGAKGN TPATGTTQGK
210 220 230 240 250
KAEGTQNQSK KAEGAPNQGR KAEGTPNQGK KTEGTPNQGK KAEGTPNQGK
260 270 280 290 300
KAEGTPNQGK KAEGAQNQGK KVDTTPNQGK KVEGAPTQGR KAEGAQNQAK
310 320 330 340 350
KVEGAQNQGK KAEGAQNQGK KGEGAQNQGK KAEGAQNQGK KAEGAQNQGK
360 370 380 390 400
KAEGAQNQGK KAEGAQNQGK KAEGAQNQGK KSEGAQNQGK KVEGAQNQGK
410 420 430 440 450
KAEGAQNQGK KAEGAQNQGK KAEGAQNQGK KAEGAQNQGK KAEGAQNQGK
460 470 480 490 500
KAEGAQNQGK KAEGAQNQGK KVEGAQNQGK KAEGAQNQGK KAEGAQNQGK
510 520 530 540 550
KAEGAQNQGQ KGEGAQNQGK KTEGAQGKKA ERSPNQGKKG EGAPIQGKKA
560 570 580 590 600
DSVANQGTKV EGITNQGKKA EGSPSEGKKA EGSPNQGKKA DAAANQGKKT
610 620 630 640 650
ESASVQGRNT DVAQSPEAPK QEAPAKKKSG SKKKGEPGPP DADGPLYLPY
660 670 680 690 700
KTLVSTVGSM VFNEGEAQRL IEILSEKAGI IQDTWHKATQ KGDPVAILKR
710 720 730 740 750
QLEEKEKLLA TEQEDAAVAK SKLRELNKEM AAEKAKAAAG EAKVKKQLVA
760 770 780 790 800
REQEITAVQA RMQASYREHV KEVQQLQGKI RTLQEQLENG PNTQLARLQQ
810 820 830 840 850
ENSILRDALN QATSQVESKQ NAELAKLRQE LSKVSKELVE KSEAVRQDEQ
860 870 880 890 900
QRKALEAKAA AFEKQVLQLQ ASHRESEEAL QKRLDEVSRE LCHTQSSHAS
910 920 930 940 950
LRADAEKAQE QQQQMAELHS KLQSSEAEVR SKCEELSGLH GQLQEARAEN
960 970 980 990 1000
SQLTERIRSI EALLEAGQAR DAQDVQASQA EADQQQTRLK ELESQVSGLE
1010 1020 1030 1040 1050
KEAIELREAV EQQKVKNNDL REKNWKAMEA LATAEQACKE KLLSLTQAKE
1060 1070 1080 1090 1100
ESEKQLCLIE AQTMEALLAL LPELSVLAQQ NYTEWLQDLK EKGPTLLKHP
1110 1120 1130 1140 1150
PAPAEPSSDL ASKLREAEET QSTLQAECDQ YRSILAETEG MLRDLQKSVE
1160 1170 1180 1190 1200
EEEQVWRAKV GAAEEELQKS RVTVKHLEEI VEKLKGELES SDQVREHTSH
1210 1220 1230 1240 1250
LEAELEKHMA AASAECQNYA KEVAGLRQLL LESQSQLDAA KSEAQKQSDE
1260 1270 1280 1290 1300
LALVRQQLSE MKSHVEDGDI AGAPASSPEA PPAEQDPVQL KTQLEWTEAI
1310 1320 1330 1340 1350
LEDEQTQRQK LTAEFEEAQT SACRLQEELE KLRTAGPLES SETEEASQLK
1360 1370 1380 1390 1400
ERLEKEKKLT SDLGRAATRL QELLKTTQEQ LAREKDTVKK LQEQLEKAED
1410
GSSSKEGTSV
Length:1,410
Mass (Da):152,472
Last modified:October 10, 2002 - v4
Checksum:iB83FD15D002D366C
GO
Isoform 1 (identifier: Q9P2E9-2) [UniParc]FASTAAdd to basket

Also known as: p180

The sequence of this isoform differs from the canonical sequence as follows:
     635-637: Missing.

Show »
Length:1,407
Mass (Da):152,189
Checksum:i7A0FEF5AD86EF0E4
GO
Isoform 2 (identifier: Q9P2E9-3) [UniParc]FASTAAdd to basket

Also known as: ES130

The sequence of this isoform differs from the canonical sequence as follows:
     177-606: Missing.
     635-637: Missing.

Show »
Length:977
Mass (Da):108,632
Checksum:i63B7644AAA334537
GO

Sequence cautioni

The sequence BAA92636.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti322 – 3221G → A in AAC25978 (PubMed:9628588).Curated
Sequence conflicti345 – 3451A → G in AAC25978 (PubMed:9628588).Curated
Sequence conflicti350 – 3501K → KKTEEAQKQGKKAEGAQIQG KKNEGAQTQGKKAEGAQNQG KKNEGAQTQGKKAEGAQTQG KKADGAQNQGKKAEGAQNQG KKAEGAQNQGKKAEGAQNQG KKADGAQNQGKKAEGAQNQG KKAEGAQNQGT in AAC25978 (PubMed:9628588).Curated
Sequence conflicti382 – 3821S → A in AAC25978 (PubMed:9628588).Curated
Sequence conflicti382 – 3821S → A in BAA92636 (PubMed:10718198).Curated
Sequence conflicti392 – 3921V → A in AAC25978 (PubMed:9628588).Curated
Sequence conflicti448 – 4481Q → QDKKAEGAQNQGRKAEGAQN QGRKAEGAQNQGKKAEGAPN QGKKAEGAPNQGKKAEGTPN QGKKAEGTPNQGKKAEGTPN QGKKAEGAQNQGKKAEGAQN QGKKAEGTPNQGKKAEGAQN QGKKAEGAQNQGKKAEGAQN QGKKAEGAQNQ (PubMed:10718198).Curated
Sequence conflicti1043 – 10431L → H in AAC25977 (PubMed:9628588).Curated
Sequence conflicti1043 – 10431L → H (PubMed:10718198).Curated
Sequence conflicti1043 – 10431L → H (PubMed:17974005).Curated
Sequence conflicti1043 – 10431L → H in AAH00099 (PubMed:15489334).Curated
Sequence conflicti1199 – 11991S → L (PubMed:10718198).Curated
Sequence conflicti1199 – 11991S → L (PubMed:17974005).Curated
Sequence conflicti1199 – 11991S → L in AAH00099 (PubMed:15489334).Curated
Sequence conflicti1312 – 13121T → M in AAC25977 (PubMed:9628588).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1324 – 13241R → L.
Corresponds to variant rs1132274 [ dbSNP | Ensembl ].
VAR_056982

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei177 – 606430Missing in isoform 2. 1 PublicationVSP_003949Add
BLAST
Alternative sequencei635 – 6373Missing in isoform 1 and isoform 2. 1 PublicationVSP_003950

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006751 mRNA. Translation: AAC25977.1.
AF007575 mRNA. Translation: AAC25978.1.
AB037819 mRNA. Translation: BAA92636.2. Different initiation.
AL132765 Genomic DNA. Translation: CAC10587.1.
AL132765 Genomic DNA. Translation: CAH74034.1.
AL833822 mRNA. Translation: CAD38684.1.
BC000099 mRNA. Translation: AAH00099.4.
CCDSiCCDS13128.1. [Q9P2E9-3]
RefSeqiNP_001036041.1. NM_001042576.1.
NP_004578.2. NM_004587.2.
UniGeneiHs.472213.

Genome annotation databases

EnsembliENST00000360807; ENSP00000354045; ENSG00000125844. [Q9P2E9-3]
ENST00000377807; ENSP00000367038; ENSG00000125844. [Q9P2E9-3]
GeneIDi6238.
KEGGihsa:6238.
UCSCiuc002wpv.1. human. [Q9P2E9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006751 mRNA. Translation: AAC25977.1.
AF007575 mRNA. Translation: AAC25978.1.
AB037819 mRNA. Translation: BAA92636.2. Different initiation.
AL132765 Genomic DNA. Translation: CAC10587.1.
AL132765 Genomic DNA. Translation: CAH74034.1.
AL833822 mRNA. Translation: CAD38684.1.
BC000099 mRNA. Translation: AAH00099.4.
CCDSiCCDS13128.1. [Q9P2E9-3]
RefSeqiNP_001036041.1. NM_001042576.1.
NP_004578.2. NM_004587.2.
UniGeneiHs.472213.

3D structure databases

ProteinModelPortaliQ9P2E9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112152. 46 interactions.
IntActiQ9P2E9. 17 interactions.
MINTiMINT-5006662.
STRINGi9606.ENSP00000354045.

PTM databases

iPTMnetiQ9P2E9.
PhosphoSiteiQ9P2E9.
SwissPalmiQ9P2E9.

Polymorphism and mutation databases

BioMutaiRRBP1.
DMDMi23822112.

Proteomic databases

EPDiQ9P2E9.
MaxQBiQ9P2E9.
PaxDbiQ9P2E9.
PRIDEiQ9P2E9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360807; ENSP00000354045; ENSG00000125844. [Q9P2E9-3]
ENST00000377807; ENSP00000367038; ENSG00000125844. [Q9P2E9-3]
GeneIDi6238.
KEGGihsa:6238.
UCSCiuc002wpv.1. human. [Q9P2E9-1]

Organism-specific databases

CTDi6238.
GeneCardsiRRBP1.
HGNCiHGNC:10448. RRBP1.
HPAiHPA009026.
HPA011924.
MIMi601418. gene.
neXtProtiNX_Q9P2E9.
PharmGKBiPA34863.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFNK. Eukaryota.
ENOG410XY8H. LUCA.
GeneTreeiENSGT00530000063895.
HOVERGENiHBG061483.
InParanoidiQ9P2E9.
KOiK14000.
OrthoDBiEOG7ZWD1D.
PhylomeDBiQ9P2E9.
TreeFamiTF333579.

Miscellaneous databases

ChiTaRSiRRBP1. human.
GeneWikiiRRBP1.
GenomeRNAii6238.
NextBioi24219.
PROiQ9P2E9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P2E9.
ExpressionAtlasiQ9P2E9. baseline and differential.
GenevisibleiQ9P2E9. HS.

Family and domain databases

InterProiIPR007794. Rib_rcpt_KP.
[Graphical view]
PfamiPF05104. Rib_recp_KP_reg. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of multiple forms of 180-kDa ribosome receptor in human cells."
    Langley R., Leung E., Morris C., Berg R., McDonald M., Weaver A., Parry D., Ni J., Su J., Gentz R., Spurr N., Krissansen G.W.
    DNA Cell Biol. 17:449-460(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 413-1208 (ISOFORM 3).
    Tissue: Uterus.
  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] OF 756-1410.
    Tissue: Brain.
  7. "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 THR-225; THR-245; THR-255; SER-583 AND SER-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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 SER-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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 SER-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615; SER-1276 AND SER-1277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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 THR-225; THR-235; THR-245; THR-255; SER-533 AND SER-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-583; SER-615 AND SER-978, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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 SER-573; SER-615; SER-900; SER-959 AND SER-1277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRRBP1_HUMAN
AccessioniPrimary (citable) accession number: Q9P2E9
Secondary accession number(s): A2A2S6
, A6NCN6, O75300, O75301, Q5W165, Q96SB2, Q9BWP1, Q9H476
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 10, 2002
Last modified: April 13, 2016
This is version 144 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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

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.