Q96PK6 (RBM14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RBM14
Synonyms:	SIP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	669 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
Subcellular location	Nucleus. Nucleus › nucleolus. Note: In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Ref.9 Ref.23
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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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.11. Source: UniProtKB response to hormone stimulus Traceable author statement Ref.1. Source: UniProtKB
Cellular_component	mediator complex Non-traceable author statement Ref.1. Source: UniProtKB ribonucleoprotein complex Traceable author statement Ref.1. Source: UniProtKB transcription factor complex Inferred from physical interaction Ref.1. Source: UniProtKB
Molecular_function	RNA 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 protein binding, bridging Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 669

669

RNA-binding protein 14

PRO_0000081774

Regions

Domain

1 – 73

73

RRM 1

Domain

79 – 149

71

RRM 2

Region

307 – 354

48

TRBP-interacting domain

Compositional bias

224 – 569

346

Ala-rich

Amino acid modifications

Modified residue

161

1

Phosphoserine Ref.20

Modified residue

206

1

Phosphothreonine Ref.10 Ref.12 Ref.16 Ref.18 Ref.20 Ref.22

Modified residue

220

1

Phosphoserine Ref.22

Modified residue

256

1

Phosphoserine Ref.17

Modified residue

520

1

Phosphoserine By similarity

Modified residue

562

1

Phosphoserine Ref.13

Modified residue

572

1

Phosphothreonine Ref.19

Modified residue

582

1

Phosphoserine By similarity

Modified residue

618

1

Phosphoserine Ref.17 Ref.20

Modified residue

629

1

Phosphothreonine By similarity

Modified residue

632

1

Phosphoserine By similarity

Natural variations

Alternative sequence

113 – 118

6

DYAFVH → GGMCVG in isoform 3.

VSP_044641

Alternative sequence

119 – 669

551

Missing in isoform 3.

VSP_044642

Alternative sequence

151 – 156

6

QKKGPG → MVPTGV in isoform 2.

VSP_015078

Alternative sequence

157 – 669

513

Missing in isoform 2.

VSP_015079

Experimental info

Sequence conflict

560

1

S → T in AAK77961. Ref.1

Sequence conflict

609

1

A → V in BAD96550. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

669

Helix Strand Turn

Details...

Beta strand

81 – 85

5

Helix

92 – 102

11

Beta strand

105 – 110

6

Beta strand

115 – 120

6

Helix

122 – 132

11

Beta strand

143 – 147

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CoAA) [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 565C5EF51B6881FD	FASTA	669	69,492
	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
	Isoform 2 (CoAM) [UniParc]. Checksum: BCD4C7DA01982D64	FASTA	156	17,117
	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 KEADAKAAIA QLNGKEVKGK RINVELSTKG MVPTGV
	Isoform 3 [UniParc]. Checksum: CDC3102FDFAF75A5	FASTA	118	12,894
	10 20 30 40 50 60 MKIFVGNVDG ADTTPEELAA LFAPYGTVMS CAVMKQFAFV HMRENAGALR AIEALHGHEL 70 80 90 100 110 RPGRALVVEM SRPRPLNTWK IFVGNVSAAC TSQELRSLFE RRGRVIECDV VKGGMCVG

References

	« Hide 'large scale' referencesShow '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]	"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.
[3]	"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.
[4]	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.
[5]	"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. , 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].
[6]	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. , 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].
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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.
[12]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"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.
[15]	"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.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY.
[19]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"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, MASS SPECTROMETRY.
[23]	"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].
[24]	"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.
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.

IPI

IPI00013174.
IPI00644837.
IPI01009009.

RefSeq

NP_001185765.1. NM_001198836.1.
NP_001185775.1. NM_001198846.1.
NP_006319.1. NM_006328.3.

UniGene

Hs.533712.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DNP	NMR	-	A	77-153	[»]

ProteinModelPortal

Q96PK6.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96PK6. 8 interactions.

MINT

MINT-2798129.

STRING

9606.ENSP00000311747.

PTM databases

PhosphoSite

Q96PK6.

Polymorphism databases

DMDM

73913750.

Proteomic databases

PaxDb

Q96PK6.

PRIDE

Q96PK6.

Protocols and materials databases

DNASU

10432.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310137; ENSP00000311747; ENSG00000239306.
ENST00000393979; ENSP00000377548; ENSG00000239306.

GeneID

100526737.
10432.

KEGG

hsa:100526737.
hsa:10432.

UCSC

uc001oit.3. human.
uc009yri.3. human.

Organism-specific databases

CTD

100526737.
10432.

GeneCards

GC11P066384.

HGNC

HGNC:14219. RBM14.

HPA

HPA006628.

MIM

612409. gene.

neXtProt

NX_Q96PK6.

PharmGKB

PA34263.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOGENOM

HOG000065673.

HOVERGEN

HBG053180.

InParanoid

Q96PK6.

KO

K13189.

OMA

SLTSYGA.

OrthoDB

EOG45X7XS.

PhylomeDB

Q96PK6.

Gene expression databases

ArrayExpress

Q96PK6.

Bgee

Q96PK6.

Genevestigator

Q96PK6.

GermOnline

ENSG00000173959. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 2 hits.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RBM14. human.
RBM14-RBM4. human.

EvolutionaryTrace

Q96PK6.

GenomeRNAi

10432.

NextBio

34054915.

SOURCE

Search...

Entry information

Entry name

RBM14_HUMAN

Accession

Primary (citable) accession number: Q96PK6
Secondary accession number(s): B3KMN4 , D6RGD8, O75932, Q53GV1, Q68DQ9, Q96PK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	August 30, 2005
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.