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Protein

RNA-binding protein 27

Gene

RBM27

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

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri273 – 30129C3H1-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein 27
Alternative name(s):
RNA-binding motif protein 27
Gene namesi
Name:RBM27
Synonyms:KIAA1311
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:29243. RBM27.

Subcellular locationi

  • Cytoplasm
  • Nucleus speckle

  • Note: Incorporated into the nuclear speckles and to speckles proximal to the nuclear periphery. Also localizes to punctate structures in the cytoplasm termed cytospeckles (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134925458.

Polymorphism and mutation databases

BioMutaiRBM27.
DMDMi124021005.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10601060RNA-binding protein 27PRO_0000273044Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei447 – 4471PhosphothreonineCombined sources
Cross-linki653 – 653Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei927 – 9271PhosphoserineBy similarity
Modified residuei1012 – 10121PhosphoserineCombined sources
Modified residuei1020 – 10201PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9P2N5.
MaxQBiQ9P2N5.
PaxDbiQ9P2N5.
PeptideAtlasiQ9P2N5.
PRIDEiQ9P2N5.

PTM databases

iPTMnetiQ9P2N5.
PhosphoSiteiQ9P2N5.

Miscellaneous databases

PMAP-CutDBQ9P2N5.

Expressioni

Gene expression databases

BgeeiQ9P2N5.
CleanExiHS_RBM27.
GenevisibleiQ9P2N5. HS.

Organism-specific databases

HPAiHPA035944.
HPA036422.

Interactioni

Protein-protein interaction databases

BioGridi119955. 39 interactions.
IntActiQ9P2N5. 11 interactions.
MINTiMINT-2820712.
STRINGi9606.ENSP00000265271.

Structurei

3D structure databases

ProteinModelPortaliQ9P2N5.
SMRiQ9P2N5. Positions 599-676.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini600 – 67475RRMPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili809 – 88678Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi131 – 20171Arg-richAdd
BLAST
Compositional biasi311 – 417107Pro-richAdd
BLAST
Compositional biasi678 – 71841Gln-richAdd
BLAST

Domaini

The RRM domain mediates integration into cytospeckles.By similarity

Sequence similaritiesi

Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri273 – 30129C3H1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2135. Eukaryota.
ENOG410Y2TW. LUCA.
GeneTreeiENSGT00510000046929.
HOGENOMiHOG000067963.
HOVERGENiHBG057372.
InParanoidiQ9P2N5.
KOiK13193.
OMAiGPGHSMR.
OrthoDBiEOG7TJ3HB.
PhylomeDBiQ9P2N5.
TreeFamiTF319253.

Family and domain databases

Gene3Di1.20.1390.10. 1 hit.
3.30.70.330. 1 hit.
4.10.1000.10. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR002483. PWI_dom.
IPR000504. RRM_dom.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF01480. PWI. 1 hit.
PF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P2N5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIEDVDALK SWLAKLLEPI CDADPSALAN YVVALVKKDK PEKELKAFCA
60 70 80 90 100
DQLDVFLQKE TSGFVDKLFE SLYTKNYLPL LEPVKPEPKP LVQEKEEIKE
110 120 130 140 150
EVFQEPAEEE RDGRKKKYPS PQKTRSESSE RRTREKKRED GKWRDYDRYY
160 170 180 190 200
ERNELYREKY DWRRGRSKSR SKSRGLSRSR SRSRGRSKDR DPNRNVEHRE
210 220 230 240 250
RSKFKSERND LESSYVPVSA PPPNSSEQYS SGAQSIPSTV TVIAPAHHSE
260 270 280 290 300
NTTESWSNYY NNHSSSNSFG RNLPPKRRCR DYDERGFCVL GDLCQFDHGN
310 320 330 340 350
DPLVVDEVAL PSMIPFPPPP PGLPPPPPPG MLMPPMPGPG PGPGPGPGPG
360 370 380 390 400
PGPGPGPGHS MRLPVPQGHG QPPPSVVLPI PRPPITQSSL INSRDQPGTS
410 420 430 440 450
AVPNLASVGT RLPPPLPQNL LYTVSERQPM YSREHGAAAS ERLQLGTPPP
460 470 480 490 500
LLAARLVPPR NLMGSSIGYH TSVSSPTPLV PDTYEPDGYN PEAPSITSSG
510 520 530 540 550
RSQYRQFFSR TQTQRPNLIG LTSGDMDVNP RAANIVIQTE PPVPVSINSN
560 570 580 590 600
ITRVVLEPDS RKRAMSGLEG PLTKKPWLGK QGNNNQNKPG FLRKNQYTNT
610 620 630 640 650
KLEVKKIPQE LNNITKLNEH FSKFGTIVNI QVAFKGDPEA ALIQYLTNEE
660 670 680 690 700
ARKAISSTEA VLNNRFIRVL WHRENNEQPT LQSSAQLLLQ QQQTLSHLSQ
710 720 730 740 750
QHHHLPQHLH QQQVLVAQSA PSTVHGGIQK MMSKPQTSGA YVLNKVPVKH
760 770 780 790 800
RLGHAGGNQS DASHLLNQSG GAGEDCQIFS TPGHPKMIYS SSNLKTPSKL
810 820 830 840 850
CSGSKSHDVQ EVLKKKQEAM KLQQDMRKKR QEVLEKQIEC QKMLISKLEK
860 870 880 890 900
NKNMKPEERA NIMKTLKELG EKISQLKDEL KTSSAVSTPS KVKTKTEAQK
910 920 930 940 950
ELLDTELDLH KRLSSGEDTT ELRKKLSQLQ VEAARLGILP VGRGKTMSSQ
960 970 980 990 1000
GRGRGRGRGG RGRGSLNHMV VDHRPKALTV GGFIEEEKED LLQHFSTANQ
1010 1020 1030 1040 1050
GPKFKDRRLQ ISWHKPKVPS ISTETEEEEV KEEETETSDL FLPDDDDEDE
1060
DEYESRSWRR
Length:1,060
Mass (Da):118,718
Last modified:January 23, 2007 - v2
Checksum:i9DACF8B155187456
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC091959 Genomic DNA. No translation available.
AB037732 mRNA. Translation: BAA92549.1.
BC033524 mRNA. Translation: AAH33524.1.
CCDSiCCDS43378.1.
RefSeqiNP_061862.1. NM_018989.1.
UniGeneiHs.61441.

Genome annotation databases

EnsembliENST00000265271; ENSP00000265271; ENSG00000091009.
GeneIDi54439.
KEGGihsa:54439.
UCSCiuc003lnz.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC091959 Genomic DNA. No translation available.
AB037732 mRNA. Translation: BAA92549.1.
BC033524 mRNA. Translation: AAH33524.1.
CCDSiCCDS43378.1.
RefSeqiNP_061862.1. NM_018989.1.
UniGeneiHs.61441.

3D structure databases

ProteinModelPortaliQ9P2N5.
SMRiQ9P2N5. Positions 599-676.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119955. 39 interactions.
IntActiQ9P2N5. 11 interactions.
MINTiMINT-2820712.
STRINGi9606.ENSP00000265271.

PTM databases

iPTMnetiQ9P2N5.
PhosphoSiteiQ9P2N5.

Polymorphism and mutation databases

BioMutaiRBM27.
DMDMi124021005.

Proteomic databases

EPDiQ9P2N5.
MaxQBiQ9P2N5.
PaxDbiQ9P2N5.
PeptideAtlasiQ9P2N5.
PRIDEiQ9P2N5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265271; ENSP00000265271; ENSG00000091009.
GeneIDi54439.
KEGGihsa:54439.
UCSCiuc003lnz.5. human.

Organism-specific databases

CTDi54439.
GeneCardsiRBM27.
H-InvDBHIX0005281.
HGNCiHGNC:29243. RBM27.
HPAiHPA035944.
HPA036422.
neXtProtiNX_Q9P2N5.
PharmGKBiPA134925458.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2135. Eukaryota.
ENOG410Y2TW. LUCA.
GeneTreeiENSGT00510000046929.
HOGENOMiHOG000067963.
HOVERGENiHBG057372.
InParanoidiQ9P2N5.
KOiK13193.
OMAiGPGHSMR.
OrthoDBiEOG7TJ3HB.
PhylomeDBiQ9P2N5.
TreeFamiTF319253.

Miscellaneous databases

ChiTaRSiRBM27. human.
GenomeRNAii54439.
PMAP-CutDBQ9P2N5.
PROiQ9P2N5.

Gene expression databases

BgeeiQ9P2N5.
CleanExiHS_RBM27.
GenevisibleiQ9P2N5. HS.

Family and domain databases

Gene3Di1.20.1390.10. 1 hit.
3.30.70.330. 1 hit.
4.10.1000.10. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR002483. PWI_dom.
IPR000504. RRM_dom.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF01480. PWI. 1 hit.
PF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] OF 172-1060.
    Tissue: Brain.
  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] OF 665-1060.
    Tissue: Cervix.
  4. "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-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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 THR-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1020, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells."
    Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.
    Proteomics 8:2885-2896(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-653.
    Tissue: Cervix carcinoma.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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 THR-447 AND SER-1012, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  13. "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-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRBM27_HUMAN
AccessioniPrimary (citable) accession number: Q9P2N5
Secondary accession number(s): Q8IYW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 124 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  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.