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Q96PK6

- RBM14_HUMAN

UniProt

Q96PK6 - RBM14_HUMAN

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Protein

RNA-binding protein 14

Gene

RBM14

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

Functioni

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.

GO - Molecular functioni

  1. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding, bridging Source: UniProtKB
  5. RNA binding Source: UniProtKB
  6. RNA polymerase II transcription cofactor activity Source: UniProtKB

GO - Biological processi

  1. DNA recombination Source: UniProtKB
  2. DNA repair Source: UniProtKB
  3. DNA replication Source: UniProtKB
  4. glucocorticoid receptor signaling pathway Source: UniProtKB
  5. histone deacetylation Source: UniProtKB
  6. intracellular estrogen receptor signaling pathway Source: UniProtKB
  7. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  8. response to hormone Source: UniProtKB
  9. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RBM14
Synonyms:SIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:14219. RBM14.

Subcellular locationi

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

GO - Cellular componenti

  1. mediator complex Source: UniProtKB
  2. nucleus Source: HPA
  3. ribonucleoprotein complex Source: UniProtKB
  4. transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34263.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 669669RNA-binding protein 14PRO_0000081774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611Phosphoserine1 Publication
Modified residuei164 – 1641N6-acetyllysineBy similarity
Modified residuei206 – 2061Phosphothreonine6 Publications
Modified residuei220 – 2201Phosphoserine1 Publication
Modified residuei256 – 2561Phosphoserine1 Publication
Modified residuei562 – 5621Phosphoserine1 Publication
Modified residuei572 – 5721Phosphothreonine1 Publication
Modified residuei618 – 6181Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96PK6.
PaxDbiQ96PK6.
PRIDEiQ96PK6.

PTM databases

PhosphoSiteiQ96PK6.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ96PK6.
ExpressionAtlasiQ96PK6. baseline and differential.
GenevestigatoriQ96PK6.

Organism-specific databases

HPAiHPA006628.

Interactioni

Subunit structurei

Isoform 1 interacts with NCOA6, CITED1 and XRCC5/KU86. Isoform 1 interacts with SS18 isoform 1. Isoform 1 interacts with SS18 isoform 2.2 Publications

Protein-protein interaction databases

BioGridi115700. 96 interactions.
IntActiQ96PK6. 17 interactions.
MINTiMINT-2798129.
STRINGi9606.ENSP00000311747.

Structurei

Secondary structure

1
669
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi81 – 855
Helixi92 – 10211
Beta strandi105 – 1106
Beta strandi115 – 1206
Helixi122 – 13211
Beta strandi143 – 1475

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DNPNMR-A77-153[»]
ProteinModelPortaliQ96PK6.
SMRiQ96PK6. Positions 2-155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96PK6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7373RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini79 – 14971RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni307 – 35448TRBP-interacting domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi224 – 569346Ala-richAdd
BLAST

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00390000020883.
HOGENOMiHOG000065673.
HOVERGENiHBG053180.
InParanoidiQ96PK6.
KOiK13189.
OMAiGSYSEYL.
OrthoDBiEOG7SFJ0M.
PhylomeDBiQ96PK6.
TreeFamiTF320661.

Family and domain databases

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

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96PK6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MKIFVGNVDG ADTTPEELAA LFAPYGTVMS CAVMKQFAFV HMRENAGALR
60 70 80 90 100
AIEALHGHEL RPGRALVVEM SRPRPLNTWK IFVGNVSAAC TSQELRSLFE
110 120 130 140 150
RRGRVIECDV VKDYAFVHME KEADAKAAIA QLNGKEVKGK RINVELSTKG
160 170 180 190 200
QKKGPGLAVQ SGDKTKKPGA GDTAFPGTGG FSATFDYQQA FGNSTGGFDG
210 220 230 240 250
QARQPTPPFF GRDRSPLRRS PPRASYVAPL TAQPATYRAQ PSVSLGAAYR
260 270 280 290 300
AQPSASLGVG YRTQPMTAQA ASYRAQPSVS LGAPYRGQLA SPSSQSAAAS
310 320 330 340 350
SLGPYGGAQP SASALSSYGG QAAAASSLNS YGAQGSSLAS YGNQPSSYGA
360 370 380 390 400
QAASSYGVRA AASSYNTQGA ASSLGSYGAQ AASYGAQSAA SSLAYGAQAA
410 420 430 440 450
SYNAQPSASY NAQSAPYAAQ QAASYSSQPA AYVAQPATAA AYASQPAAYA
460 470 480 490 500
AQATTPMAGS YGAQPVVQTQ LNSYGAQASM GLSGSYGAQS AAAATGSYGA
510 520 530 540 550
AAAYGAQPSA TLAAPYRTQS SASLAASYAA QQHPQAAASY RGQPGNAYDG
560 570 580 590 600
AGQPSAAYLS MSQGAVANAN STPPPYERTR LSPPRASYDD PYKKAVAMSK
610 620 630 640 650
RYGSDRRLAE LSDYRRLSES QLSFRRSPTK SSLDYRRLPD AHSDYARYSG
660
SYNDYLRAAQ MHSGYQRRM
Length:669
Mass (Da):69,492
Last modified:August 30, 2005 - v2
Checksum:i565C5EF51B6881FD
GO
Isoform 2 (identifier: Q96PK6-2) [UniParc]FASTAAdd to Basket

Also known as: CoAM

The sequence of this isoform differs from the canonical sequence as follows:
     151-156: QKKGPG → MVPTGV
     157-669: Missing.

Show »
Length:156
Mass (Da):17,117
Checksum:iBCD4C7DA01982D64
GO
Isoform 3 (identifier: Q96PK6-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-118: DYAFVH → GGMCVG
     119-669: Missing.

Note: No experimental confirmation available.

Show »
Length:118
Mass (Da):12,894
Checksum:iCDC3102FDFAF75A5
GO
Isoform 4 (identifier: Q96PK6-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-119: DYAFVHM → GMVPTGV
     120-669: Missing.

Show »
Length:119
Mass (Da):13,031
Checksum:i9B1DC069EB814F75
GO
Isoform 5 (identifier: Q96PK6-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:339
Mass (Da):37,035
Checksum:i3618E2DA670C7E21
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti560 – 5601S → T in AAK77961. (PubMed:11443112)Curated
Sequence conflicti609 – 6091A → V in BAD96550. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei112 – 339228KDYAF…GSSLA → KGKRMHVQLSTSRLRTAPGM GDQSGCYRCGKEGHWSKECP IDRSGRVADLTEQYNEQYGA VRTPYTMSYGDSLYYNNAYG ALDAYYKRCRAARSYEAVAA AAASVYNYAEQTLSQLPQVQ NTAMASHLTSTSLDPYDRHL LPTSGAAATAAAAAAAAAAV TAASTSYYGRDRSPLRRATA PVPTVGEGYGYGHESELSQA SAAARNSLYDMARYEREQYA DRARYSAF in isoform 5. 1 PublicationVSP_047494Add
BLAST
Alternative sequencei113 – 1197DYAFVHM → GMVPTGV in isoform 4. CuratedVSP_047109
Alternative sequencei113 – 1186DYAFVH → GGMCVG in isoform 3. 2 PublicationsVSP_044641
Alternative sequencei119 – 669551Missing in isoform 3. 2 PublicationsVSP_044642Add
BLAST
Alternative sequencei120 – 669550Missing in isoform 4. CuratedVSP_047110Add
BLAST
Alternative sequencei151 – 1566QKKGPG → MVPTGV in isoform 2. 1 PublicationVSP_015078
Alternative sequencei157 – 669513Missing in isoform 2. 1 PublicationVSP_015079Add
BLAST
Alternative sequencei340 – 669330Missing in isoform 5. 1 PublicationVSP_047495Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS55772.1. [Q96PK6-2]
CCDS55773.1. [Q96PK6-4]
CCDS8147.1. [Q96PK6-1]
RefSeqiNP_001185765.1. NM_001198836.1. [Q96PK6-2]
NP_001185766.1. NM_001198837.1. [Q96PK6-4]
NP_001185774.1. NM_001198845.1. [Q96PK6-5]
NP_001185775.1. NM_001198846.1. [Q96PK6-3]
NP_006319.1. NM_006328.3. [Q96PK6-1]
UniGeneiHs.523822.
Hs.533712.

Genome annotation databases

EnsembliENST00000310137; ENSP00000311747; ENSG00000239306. [Q96PK6-1]
ENST00000393979; ENSP00000377548; ENSG00000239306. [Q96PK6-2]
ENST00000409738; ENSP00000386995; ENSG00000239306. [Q96PK6-4]
GeneIDi100526737.
10432.
KEGGihsa:100526737.
hsa:10432.
UCSCiuc001oit.3. human. [Q96PK6-1]
uc009yri.3. human. [Q96PK6-2]

Polymorphism databases

DMDMi73913750.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS55772.1. [Q96PK6-2 ]
CCDS55773.1. [Q96PK6-4 ]
CCDS8147.1. [Q96PK6-1 ]
RefSeqi NP_001185765.1. NM_001198836.1. [Q96PK6-2 ]
NP_001185766.1. NM_001198837.1. [Q96PK6-4 ]
NP_001185774.1. NM_001198845.1. [Q96PK6-5 ]
NP_001185775.1. NM_001198846.1. [Q96PK6-3 ]
NP_006319.1. NM_006328.3. [Q96PK6-1 ]
UniGenei Hs.523822.
Hs.533712.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DNP NMR - A 77-153 [» ]
ProteinModelPortali Q96PK6.
SMRi Q96PK6. Positions 2-155.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115700. 96 interactions.
IntActi Q96PK6. 17 interactions.
MINTi MINT-2798129.
STRINGi 9606.ENSP00000311747.

PTM databases

PhosphoSitei Q96PK6.

Polymorphism databases

DMDMi 73913750.

Proteomic databases

MaxQBi Q96PK6.
PaxDbi Q96PK6.
PRIDEi Q96PK6.

Protocols and materials databases

DNASUi 10432.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310137 ; ENSP00000311747 ; ENSG00000239306 . [Q96PK6-1 ]
ENST00000393979 ; ENSP00000377548 ; ENSG00000239306 . [Q96PK6-2 ]
ENST00000409738 ; ENSP00000386995 ; ENSG00000239306 . [Q96PK6-4 ]
GeneIDi 100526737.
10432.
KEGGi hsa:100526737.
hsa:10432.
UCSCi uc001oit.3. human. [Q96PK6-1 ]
uc009yri.3. human. [Q96PK6-2 ]

Organism-specific databases

CTDi 100526737.
10432.
GeneCardsi GC11P066384.
HGNCi HGNC:14219. RBM14.
HPAi HPA006628.
MIMi 612409. gene.
neXtProti NX_Q96PK6.
PharmGKBi PA34263.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
GeneTreei ENSGT00390000020883.
HOGENOMi HOG000065673.
HOVERGENi HBG053180.
InParanoidi Q96PK6.
KOi K13189.
OMAi GSYSEYL.
OrthoDBi EOG7SFJ0M.
PhylomeDBi Q96PK6.
TreeFami TF320661.

Miscellaneous databases

ChiTaRSi RBM14. human.
RBM14-RBM4. human.
EvolutionaryTracei Q96PK6.
GeneWikii RBM14.
NextBioi 34054915.
PROi Q96PK6.
SOURCEi Search...

Gene expression databases

Bgeei Q96PK6.
ExpressionAtlasi Q96PK6. baseline and differential.
Genevestigatori Q96PK6.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 601-669.
    Tissue: Liver.
  11. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiRBM14_HUMAN
AccessioniPrimary (citable) accession number: Q96PK6
Secondary accession number(s): B0LM41
, B3KMN4, D6RGD8, O75932, Q2PYN1, Q53GV1, Q68DQ9, Q96PK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: October 29, 2014
This is version 127 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 11
    Human chromosome 11: 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

External Data

Dasty 3