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Q96PK6 (RBM14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding protein 14
Alternative name(s):
Paraspeckle protein 2
Short name=PSP2
RNA-binding motif protein 14
RRM-containing coactivator activator/modulator
Synaptotagmin-interacting protein
Short name=SYT-interacting protein
Gene names
Name:RBM14
Synonyms:SIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length669 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, functions as a transcriptional repressor, modulating transcriptional activities of coactivators including isoform 1, NCOA6 and CITED1.

Subunit structure

Isoform 1 interacts with NCOA6, CITED1 and XRCC5/KU86. Isoform 1 interacts with SS18 isoform 1. Isoform 1 interacts with SS18 isoform 2. Ref.1 Ref.13

Subcellular location

Nucleus. Nucleusnucleolus. Note: In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Ref.11 Ref.26

Tissue specificity

Expressed in all tissues tested, including brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood lymphocytes.

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Non-traceable author statement Ref.1. Source: UniProtKB

DNA repair

Non-traceable author statement Ref.1. Source: UniProtKB

DNA replication

Non-traceable author statement Ref.1. Source: UniProtKB

glucocorticoid receptor signaling pathway

Non-traceable author statement Ref.1. Source: UniProtKB

histone deacetylation

Inferred from physical interaction Ref.1. Source: UniProtKB

intracellular estrogen receptor signaling pathway

Non-traceable author statement Ref.1. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1Ref.13. Source: UniProtKB

response to hormone

Traceable author statement Ref.1. Source: UniProtKB

transcription from RNA polymerase II promoter

Non-traceable author statement Ref.1. Source: GOC

   Cellular_componentmediator complex

Non-traceable author statement Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

ribonucleoprotein complex

Traceable author statement Ref.1. Source: UniProtKB

transcription factor complex

Inferred from physical interaction Ref.1. Source: UniProtKB

   Molecular_functionRNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

RNA polymerase II transcription cofactor activity

Non-traceable author statement Ref.1. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from physical interaction Ref.1. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding, bridging

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96PK6-1)

Also known as: CoAA;

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.
Isoform 2 (identifier: Q96PK6-2)

Also known as: CoAM;

The sequence of this isoform differs from the canonical sequence as follows:
     151-156: QKKGPG → MVPTGV
     157-669: Missing.
Isoform 3 (identifier: Q96PK6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     113-118: DYAFVH → GGMCVG
     119-669: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q96PK6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     113-119: DYAFVHM → GMVPTGV
     120-669: Missing.
Isoform 5 (identifier: Q96PK6-5)

The sequence of this isoform differs from the canonical sequence as follows:
     112-339: KDYAFVHMEK...SYGAQGSSLA → KGKRMHVQLS...YADRARYSAF
     340-669: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 669669RNA-binding protein 14
PRO_0000081774

Regions

Domain1 – 7373RRM 1
Domain79 – 14971RRM 2
Region307 – 35448TRBP-interacting domain
Compositional bias224 – 569346Ala-rich

Amino acid modifications

Modified residue1611Phosphoserine Ref.23
Modified residue1641N6-acetyllysine By similarity
Modified residue2061Phosphothreonine Ref.12 Ref.14 Ref.18 Ref.21 Ref.23 Ref.25
Modified residue2201Phosphoserine Ref.25
Modified residue2561Phosphoserine Ref.19
Modified residue5621Phosphoserine Ref.15
Modified residue5721Phosphothreonine Ref.22
Modified residue6181Phosphoserine Ref.19 Ref.23

Natural variations

Alternative sequence112 – 339228KDYAF…GSSLA → KGKRMHVQLSTSRLRTAPGM GDQSGCYRCGKEGHWSKECP IDRSGRVADLTEQYNEQYGA VRTPYTMSYGDSLYYNNAYG ALDAYYKRCRAARSYEAVAA AAASVYNYAEQTLSQLPQVQ NTAMASHLTSTSLDPYDRHL LPTSGAAATAAAAAAAAAAV TAASTSYYGRDRSPLRRATA PVPTVGEGYGYGHESELSQA SAAARNSLYDMARYEREQYA DRARYSAF in isoform 5.
VSP_047494
Alternative sequence113 – 1197DYAFVHM → GMVPTGV in isoform 4.
VSP_047109
Alternative sequence113 – 1186DYAFVH → GGMCVG in isoform 3.
VSP_044641
Alternative sequence119 – 669551Missing in isoform 3.
VSP_044642
Alternative sequence120 – 669550Missing in isoform 4.
VSP_047110
Alternative sequence151 – 1566QKKGPG → MVPTGV in isoform 2.
VSP_015078
Alternative sequence157 – 669513Missing in isoform 2.
VSP_015079
Alternative sequence340 – 669330Missing in isoform 5.
VSP_047495

Experimental info

Sequence conflict5601S → T in AAK77961. Ref.1
Sequence conflict6091A → V in BAD96550. Ref.6

Secondary structure

............. 669
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CoAA) [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 565C5EF51B6881FD

FASTA66969,492
        10         20         30         40         50         60 
MKIFVGNVDG ADTTPEELAA LFAPYGTVMS CAVMKQFAFV HMRENAGALR AIEALHGHEL 

        70         80         90        100        110        120 
RPGRALVVEM SRPRPLNTWK IFVGNVSAAC TSQELRSLFE RRGRVIECDV VKDYAFVHME 

       130        140        150        160        170        180 
KEADAKAAIA QLNGKEVKGK RINVELSTKG QKKGPGLAVQ SGDKTKKPGA GDTAFPGTGG 

       190        200        210        220        230        240 
FSATFDYQQA FGNSTGGFDG QARQPTPPFF GRDRSPLRRS PPRASYVAPL TAQPATYRAQ 

       250        260        270        280        290        300 
PSVSLGAAYR AQPSASLGVG YRTQPMTAQA ASYRAQPSVS LGAPYRGQLA SPSSQSAAAS 

       310        320        330        340        350        360 
SLGPYGGAQP SASALSSYGG QAAAASSLNS YGAQGSSLAS YGNQPSSYGA QAASSYGVRA 

       370        380        390        400        410        420 
AASSYNTQGA ASSLGSYGAQ AASYGAQSAA SSLAYGAQAA SYNAQPSASY NAQSAPYAAQ 

       430        440        450        460        470        480 
QAASYSSQPA AYVAQPATAA AYASQPAAYA AQATTPMAGS YGAQPVVQTQ LNSYGAQASM 

       490        500        510        520        530        540 
GLSGSYGAQS AAAATGSYGA AAAYGAQPSA TLAAPYRTQS SASLAASYAA QQHPQAAASY 

       550        560        570        580        590        600 
RGQPGNAYDG AGQPSAAYLS MSQGAVANAN STPPPYERTR LSPPRASYDD PYKKAVAMSK 

       610        620        630        640        650        660 
RYGSDRRLAE LSDYRRLSES QLSFRRSPTK SSLDYRRLPD AHSDYARYSG SYNDYLRAAQ 


MHSGYQRRM 

« Hide

Isoform 2 (CoAM) [UniParc].

Checksum: BCD4C7DA01982D64
Show »

FASTA15617,117
Isoform 3 [UniParc].

Checksum: CDC3102FDFAF75A5
Show »

FASTA11812,894
Isoform 4 [UniParc].

Checksum: 9B1DC069EB814F75
Show »

FASTA11913,031
Isoform 5 [UniParc].

Checksum: 3618E2DA670C7E21
Show »

FASTA33937,035

References

« Hide 'large scale' references
[1]"Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM)."
Iwasaki T., Chin W.W., Ko L.
J. Biol. Chem. 276:33375-33383(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, INTERACTION WITH CITED1; NCOA6 AND XRCC5.
[2]"Switched alternative splicing of oncogene CoAA during embryonal carcinoma stem cell differentiation."
Yang Z., Sui Y., Xiong S., Liour S.S., Phillips A.C., Ko L.
Nucleic Acids Res. 35:1919-1932(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]"Functional pre- mRNA trans-splicing of coactivator CoAA and corepressor RBM4 during stem/progenitor cell differentiation."
Brooks Y.S., Wang G., Yang Z., Smith K.K., Bieberich E., Ko L.
J. Biol. Chem. 284:18033-18046(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[4]"SIP, a novel protein interacting with SYT."
Antonson P., Goodwin G.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Synovial sarcoma.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Embryo.
[6]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 1).
Tissue: Liver.
[7]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] (ISOFORMS 1 AND 3).
Tissue: Leiomyosarcoma and Lung.
[10]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 601-669.
Tissue: Liver.
[11]"Paraspeckles: a novel nuclear domain."
Fox A.H., Lam Y.W., Leung A.K.L., Lyon C.E., Andersen J., Mann M., Lamond A.I.
Curr. Biol. 12:13-25(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Synovial sarcoma translocation (SYT) encodes a nuclear receptor coactivator."
Iwasaki T., Koibuchi N., Chin W.W.
Endocrinology 146:3892-3899(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SS18.
[14]"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-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[16]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[18]"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-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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].
[21]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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-572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"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-161; THR-206 AND SER-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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 THR-206 AND SER-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[27]"Solution structure of RNA binding domain 2 in RNA-binding protein 14."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 77-153.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF315632 mRNA. Translation: AAK77961.1.
AF315633 mRNA. Translation: AAK77962.1.
DQ294957 mRNA. Translation: ABB99396.1.
EU287938 mRNA. Translation: ABY74511.1.
AF080561 mRNA. Translation: AAC64058.1.
AK021768 mRNA. Translation: BAG51046.1.
AK222830 mRNA. Translation: BAD96550.1.
AP001157 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74552.1.
BC000488 mRNA. Translation: AAH00488.1.
BE885635 mRNA. No translation available.
CR749306 mRNA. Translation: CAH18161.1.
RefSeqNP_001185765.1. NM_001198836.1.
NP_001185766.1. NM_001198837.1.
NP_001185774.1. NM_001198845.1.
NP_001185775.1. NM_001198846.1.
NP_006319.1. NM_006328.3.
UniGeneHs.523822.
Hs.533712.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DNPNMR-A77-153[»]
ProteinModelPortalQ96PK6.
SMRQ96PK6. Positions 2-155.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115700. 84 interactions.
IntActQ96PK6. 17 interactions.
MINTMINT-2798129.
STRING9606.ENSP00000311747.

PTM databases

PhosphoSiteQ96PK6.

Polymorphism databases

DMDM73913750.

Proteomic databases

PaxDbQ96PK6.
PRIDEQ96PK6.

Protocols and materials databases

DNASU10432.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310137; ENSP00000311747; ENSG00000239306. [Q96PK6-1]
ENST00000393979; ENSP00000377548; ENSG00000239306. [Q96PK6-2]
ENST00000409738; ENSP00000386995; ENSG00000239306. [Q96PK6-4]
GeneID100526737.
10432.
KEGGhsa:100526737.
hsa:10432.
UCSCuc001oit.3. human. [Q96PK6-1]
uc009yri.3. human. [Q96PK6-2]

Organism-specific databases

CTD100526737.
10432.
GeneCardsGC11P066384.
HGNCHGNC:14219. RBM14.
HPAHPA006628.
MIM612409. gene.
neXtProtNX_Q96PK6.
PharmGKBPA34263.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000065673.
HOVERGENHBG053180.
InParanoidQ96PK6.
KOK13189.
OMASDYAFVH.
OrthoDBEOG7SFJ0M.
PhylomeDBQ96PK6.
TreeFamTF320661.

Gene expression databases

ArrayExpressQ96PK6.
BgeeQ96PK6.
GenevestigatorQ96PK6.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBM14. human.
RBM14-RBM4. human.
EvolutionaryTraceQ96PK6.
GeneWikiRBM14.
NextBio34054915.
PROQ96PK6.
SOURCESearch...

Entry information

Entry nameRBM14_HUMAN
AccessionPrimary (citable) accession number: Q96PK6
Secondary accession number(s): B0LM41 expand/collapse secondary AC list , B3KMN4, D6RGD8, O75932, Q2PYN1, Q53GV1, Q68DQ9, Q96PK5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM