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P98175 (RBM10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding protein 10
Alternative name(s):
G patch domain-containing protein 9
RNA-binding motif protein 10
RNA-binding protein S1-1
Short name=S1-1
Gene names
Name:RBM10
Synonyms:DXS8237E, GPATC9, GPATCH9, KIAA0122
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length930 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in post-transcriptional processing, most probably in mRNA splicing. Binds to RNA homopolymers, with a preference for poly(G) and poly(U) and little for poly(A) By similarity. Ref.21

Subunit structure

Associates with the spliceosome. Component of a large chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5. Ref.20

Subcellular location

Nucleus. Note: In the extranucleolar nucleoplasm constitutes hundreds of nuclear domains, which dynamically change their structures in a reversible manner. Upon globally reducing RNA polymerase II transcription, the nuclear bodies enlarge and decrease in number. They occur closely adjacent to nuclear speckles or IGCs (interchromatin granule clusters) but coincide with TIDRs (transcription-inactivation-dependent RNA domains). Ref.21

Involvement in disease

TARP syndrome (TARPS) [MIM:311900]: A disorder characterized by the Robin sequence (micrognathia, glossoptosis and cleft palate), talipes equinovarus and cardiac defects.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

Contains 1 C2H2-type zinc finger.

Contains 1 G-patch domain.

Contains 1 RanBP2-type zinc finger.

Contains 2 RRM (RNA recognition motif) domains.

Sequence caution

The sequence AAB33572.1 differs from that shown. Reason: Frameshift at position 696.

The sequence BAA09471.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB70731.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB70731.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process3'-UTR-mediated mRNA stabilization

Inferred from electronic annotation. Source: Ensembl

RNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleus

Inferred from direct assay. Source: LIFEdb

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 22365833. Source: IntAct

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 22365833. Source: IntAct

protein complex binding

Inferred from direct assay Ref.20. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P98175-1)

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: P98175-2)

The sequence of this isoform differs from the canonical sequence as follows:
     354-354: Missing.
Isoform 3 (identifier: P98175-3)

The sequence of this isoform differs from the canonical sequence as follows:
     68-144: Missing.
Isoform 4 (identifier: P98175-4)

The sequence of this isoform differs from the canonical sequence as follows:
     68-144: Missing.
     354-354: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 930930RNA-binding protein 10
PRO_0000081767

Regions

Domain129 – 20981RRM 1
Domain300 – 38485RRM 2
Domain858 – 90447G-patch
Zinc finger212 – 24231RanBP2-type
Zinc finger759 – 78426C2H2-type; atypical
Compositional bias80 – 878Poly-Arg
Compositional bias113 – 12513Poly-Glu
Compositional bias561 – 60747Tyr-rich

Amino acid modifications

Modified residue611Phosphoserine Ref.12
Modified residue891Phosphoserine Ref.17
Modified residue3831N6-acetyllysine Ref.15
Modified residue7181Phosphoserine Ref.17 Ref.19
Modified residue7231Phosphoserine Ref.11 Ref.12 Ref.17 Ref.19
Modified residue7331Phosphoserine Ref.12 Ref.14
Modified residue7361Phosphoserine Ref.12 Ref.14 Ref.19
Modified residue7381Phosphoserine Ref.12 Ref.14 Ref.17
Modified residue7811Phosphoserine Ref.17
Modified residue7971Phosphoserine Ref.9 Ref.14 Ref.17 Ref.19

Natural variations

Alternative sequence68 – 14477Missing in isoform 3 and isoform 4.
VSP_036173
Alternative sequence3541Missing in isoform 2 and isoform 4.
VSP_036035
Natural variant3961R → H in a colorectal cancer sample; somatic mutation. Ref.22
VAR_035486

Experimental info

Sequence conflict4991A → P in BAA09471. Ref.1
Sequence conflict6721S → T in CAB70731. Ref.3

Secondary structure

................................ 930
Helix Strand Turn

Details...

Sequences

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

Last modified December 16, 2008. Version 3.
Checksum: 472E68F085CA5744

FASTA930103,533
        10         20         30         40         50         60 
MEYERRGGRG DRTGRYGATD RSQDDGGENR SRDHDYRDMD YRSYPREYGS QEGKHDYDDS 

        70         80         90        100        110        120 
SEEQSAEDSY EASPGSETQR RRRRRHRHSP TGPPGFPRDG DYRDQDYRTE QGEEEEEEED 

       130        140        150        160        170        180 
EEEEEKASNI VMLRMLPQAA TEDDIRGQLQ SHGVQAREVR LMRNKSSGQS RGFAFVEFSH 

       190        200        210        220        230        240 
LQDATRWMEA NQHSLNILGQ KVSMHYSDPK PKINEDWLCN KCGVQNFKRR EKCFKCGVPK 

       250        260        270        280        290        300 
SEAEQKLPLG TRLDQQTLPL GGRELSQGLL PLPQPYQAQG VLASQALSQG SEPSSENAND 

       310        320        330        340        350        360 
TIILRNLNPH STMDSILGAL APYAVLSSSN VRVIKDKQTQ LNRGFAFIQL STIVEAAQLL 

       370        380        390        400        410        420 
QILQALHPPL TIDGKTINVE FAKGSKRDMA SNEGSRISAA SVASTAIAAA QWAISQASQG 

       430        440        450        460        470        480 
GEGTWATSEE PPVDYSYYQQ DEGYGNSQGT ESSLYAHGYL KGTKGPGITG TKGDPTGAGP 

       490        500        510        520        530        540 
EASLEPGADS VSMQAFSRAQ PGAAPGIYQQ SAEASSSQGT AANSQSYTIM SPAVLKSELQ 

       550        560        570        580        590        600 
SPTHPSSALP PATSPTAQES YSQYPVPDVS TYQYDETSGY YYDPQTGLYY DPNSQYYYNA 

       610        620        630        640        650        660 
QSQQYLYWDG ERRTYVPALE QSADGHKETG APSKEGKEKK EKHKTKTAQQ IAKDMERWAR 

       670        680        690        700        710        720 
SLNKQKENFK NSFQPISSLR DDERRESATA DAGYAILEKK GALAERQHTS MDLPKLASDD 

       730        740        750        760        770        780 
RPSPPRGLVA AYSGESDSEE EQERGGPERE EKLTDWQKLA CLLCRRQFPS KEALIRHQQL 

       790        800        810        820        830        840 
SGLHKQNLEI HRRAHLSENE LEALEKNDME QMKYRDRAAE RREKYGIPEP PEPKRRKYGG 

       850        860        870        880        890        900 
ISTASVDFEQ PTRDGLGSDN IGSRMLQAMG WKEGSGLGRK KQGIVTPIEA QTRVRGSGLG 

       910        920        930 
ARGSSYGVTS TESYKETLHK TMVTRFNEAQ 

« Hide

Isoform 2 [UniParc].

Checksum: 43D8E086250E441B
Show »

FASTA929103,433
Isoform 3 [UniParc].

Checksum: BF5689F0C926EDA8
Show »

FASTA85394,469
Isoform 4 [UniParc].

Checksum: BB39E0CAC9B4A8A3
Show »

FASTA85294,370

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Bone marrow.
[2]"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 3).
Tissue: Liver.
[3]"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] (ISOFORM 1).
Tissue: Testis.
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[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] (ISOFORMS 1 AND 4).
Tissue: Brain, Lung, Muscle and Placenta.
[7]"A novel gene, DXS8237E, lies within 20 kb upstream of UBE1 in Xp11.23 and has a different X inactivation status."
Coleman M.P., Ambrose H.J., Carrel L., Nemeth A.H., Willard H.F., Davies K.E.
Genomics 31:135-138(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 544-930.
Tissue: Fetal brain.
[8]"Large-scale proteomic analysis of the human spliceosome."
Rappsilber J., Ryder U., Lamond A.I., Mann M.
Genome Res. 12:1231-1245(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH THE SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"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 SER-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"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-723, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-61; SER-723; SER-733; SER-736 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"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 SER-733; SER-736; SER-738 AND SER-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Massively parallel sequencing of exons on the X chromosome identifies RBM10 as the gene that causes a syndromic form of cleft palate."
Johnston J.J., Teer J.K., Cherukuri P.F., Hansen N.F., Loftus S.K., Chong K., Mullikin J.C., Biesecker L.G.
Am. J. Hum. Genet. 86:743-748(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN TARPS.
[17]"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-89; SER-718; SER-723; SER-738; SER-781 AND SER-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"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-718; SER-723; SER-736 AND SER-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation."
Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., Tempst P., Glass C.K., Rosenfeld M.G.
Mol. Cell 27:609-621(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
[21]"S1-1 nuclear domains: characterization and dynamics as a function of transcriptional activity."
Inoue A., Tsugawa K., Tokunaga K., Takahashi K.P., Uni S., Kimura M., Nishio K., Yamamoto N., Honda K., Watanabe T., Yamane H., Tani T.
Biol. Cell 100:523-535(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[22]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-396.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50912 mRNA. Translation: BAA09471.1. Different initiation.
AK292758 mRNA. Translation: BAF85447.1.
AL137421 mRNA. Translation: CAB70731.1. Sequence problems.
AL513366 Genomic DNA. Translation: CAI41700.1.
CH471164 Genomic DNA. Translation: EAW59284.1.
CH471164 Genomic DNA. Translation: EAW59285.1.
CH471164 Genomic DNA. Translation: EAW59287.1.
CH471164 Genomic DNA. Translation: EAW59283.1.
BC003089 mRNA. Translation: AAH03089.1.
BC004181 mRNA. Translation: AAH04181.1.
BC008733 mRNA. Translation: AAH08733.1.
BC024153 mRNA. Translation: AAH24153.1.
U35373 mRNA. Translation: AAB33572.1. Frameshift.
CCDSCCDS14274.1. [P98175-1]
CCDS55407.1. [P98175-4]
CCDS56600.1. [P98175-3]
RefSeqNP_001191395.1. NM_001204466.1. [P98175-3]
NP_001191396.1. NM_001204467.1. [P98175-2]
NP_005667.2. NM_005676.4. [P98175-1]
NP_690595.1. NM_152856.2. [P98175-4]
UniGeneHs.401509.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LXINMR-A128-218[»]
2M2BNMR-A277-408[»]
ProteinModelPortalP98175.
SMRP98175. Positions 128-218, 277-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113869. 52 interactions.
IntActP98175. 40 interactions.
MINTMINT-2864879.
STRING9606.ENSP00000366829.

PTM databases

PhosphoSiteP98175.

Polymorphism databases

DMDM218512116.

Proteomic databases

MaxQBP98175.
PaxDbP98175.
PRIDEP98175.

Protocols and materials databases

DNASU8241.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329236; ENSP00000328848; ENSG00000182872. [P98175-4]
ENST00000345781; ENSP00000329659; ENSG00000182872. [P98175-3]
ENST00000377604; ENSP00000366829; ENSG00000182872. [P98175-1]
ENST00000603045; ENSP00000474744; ENSG00000271352. [P98175-1]
ENST00000603922; ENSP00000475019; ENSG00000271352. [P98175-3]
ENST00000604931; ENSP00000474848; ENSG00000271352. [P98175-4]
GeneID8241.
KEGGhsa:8241.
UCSCuc004dhf.3. human. [P98175-1]
uc004dhg.3. human. [P98175-4]
uc004dhh.3. human. [P98175-2]
uc010nhq.3. human. [P98175-3]

Organism-specific databases

CTD8241.
GeneCardsGC0XP047004.
HGNCHGNC:9896. RBM10.
HPAHPA034972.
MIM300080. gene.
311900. phenotype.
neXtProtNX_P98175.
Orphanet2886. TARP syndrome.
PharmGKBPA34259.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290849.
HOVERGENHBG000318.
InParanoidP98175.
KOK13094.
OMAKGDPAGT.
OrthoDBEOG7NSB1M.
PhylomeDBP98175.
TreeFamTF315789.

Gene expression databases

BgeeP98175.
CleanExHS_RBM10.
GenevestigatorP98175.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
4.10.1060.10. 1 hit.
InterProIPR000467. G_patch_dom.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamPF01585. G-patch. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTSM00443. G_patch. 1 hit.
SM00360. RRM. 2 hits.
SM00355. ZnF_C2H2. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
PROSITEPS50174. G_PATCH. 1 hit.
PS50102. RRM. 2 hits.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBM10. human.
GeneWikiRBM10.
GenomeRNAi8241.
NextBio30996.
PROP98175.
SOURCESearch...

Entry information

Entry nameRBM10_HUMAN
AccessionPrimary (citable) accession number: P98175
Secondary accession number(s): C4AM81 expand/collapse secondary AC list , Q14136, Q5JRR2, Q9BTE4, Q9BTX0, Q9NTB1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 143 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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