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Q9BXP5 (SRRT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Serrate RNA effector molecule homolog
Alternative name(s):
Arsenite-resistance protein 2
Gene names
Name:SRRT
Synonyms:ARS2, ASR2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length876 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Ref.19

Subunit structure

Interacts with NCBP1 and DROSHA By similarity. Interacts with CASP8AP2 and ERBB4. Ref.20 Ref.22

Subcellular location

Nucleusnucleoplasm By similarity. Cytoplasm By similarity. Note: Predominantly nuclear. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent way By similarity. Ref.22

Tissue specificity

Ubiquitously expressed. Ref.17

Sequence similarities

Belongs to the ARS2 family.

Sequence caution

The sequence AAD17774.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAM00189.1 differs from that shown. Reason: Frameshift at position 102.

The sequence BAG58876.1 differs from that shown. Reason: Erroneous initiation.

The sequence EAL23816.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RNPS1Q152871EBI-712721,EBI-395959

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BXP5-1)

Also known as: A;

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: Q9BXP5-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     776-780: ILPPG → S
Isoform 3 (identifier: Q9BXP5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     388-388: Missing.
Isoform 4 (identifier: Q9BXP5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     388-388: Missing.
     776-780: ILPPG → S
Isoform 5 (identifier: Q9BXP5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     196-231: Missing.
     387-387: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 876876Serrate RNA effector molecule homolog
PRO_0000220965

Regions

Compositional bias10 – 8273Arg-rich
Compositional bias258 – 402145Glu-rich
Compositional bias760 – 82869Pro-rich

Amino acid modifications

Modified residue81Phosphotyrosine Ref.11
Modified residue671Phosphoserine Ref.11
Modified residue741Phosphoserine Ref.11
Modified residue1361Phosphoserine Ref.18 Ref.21
Modified residue4931Phosphoserine Ref.11 Ref.16 Ref.18
Modified residue5401Phosphoserine Ref.13 Ref.18 Ref.21
Modified residue5441Phosphothreonine Ref.10 Ref.11 Ref.14 Ref.15 Ref.18 Ref.21
Modified residue6241Phosphotyrosine Ref.12
Modified residue6251Phosphotyrosine Ref.12

Natural variations

Alternative sequence196 – 23136Missing in isoform 5.
VSP_038122
Alternative sequence3871Missing in isoform 5.
VSP_038123
Alternative sequence3881Missing in isoform 3 and isoform 4.
VSP_032502
Alternative sequence776 – 7805ILPPG → S in isoform 2 and isoform 4.
VSP_000324

Experimental info

Sequence conflict1061G → GG in CAB46374. Ref.3
Sequence conflict1191D → E in AAM00189. Ref.2
Sequence conflict3031N → Y in AAM00189. Ref.2
Sequence conflict3111D → Y in BAG64018. Ref.4
Sequence conflict4431R → K in BAG64018. Ref.4
Sequence conflict4981R → W in CAB46374. Ref.3
Sequence conflict7281V → A in CAB46374. Ref.3
Sequence conflict7441K → R in CAB46374. Ref.3

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: EB3ABD1325EA98D9

FASTA876100,666
        10         20         30         40         50         60 
MGDSDDEYDR RRRDKFRRER SDYDRSRERD ERRRGDDWND REWDRGRERR SRGEYRDYDR 

        70         80         90        100        110        120 
NRRERFSPPR HELSPPQKRM RRDWDEHSSD PYHSGYEMPY AGGGGGPTYG PPQPWGHPDV 

       130        140        150        160        170        180 
HIMQHHVLPI QARLGSIAEI DLGVPPPVMK TFKEFLLSLD DSVDETEAVK RYNDYKLDFR 

       190        200        210        220        230        240 
RQQMQDFFLA HKDEEWFRSK YHPDEVGKRR QEARGALQNR LRVFLSLMET GWFDNLLLDI 

       250        260        270        280        290        300 
DKADAIVKML DAAVIKMEGG TENDLRILEQ EEEEEQAGKP GEPSKKEEGR AGAGLGDGER 

       310        320        330        340        350        360 
KTNDKDEKKE DGKQAENDSS NDDKTKKSEG DGDKEEKKED SEKEAKKSSK KRNRKHSGDD 

       370        380        390        400        410        420 
SFDEGSVSES ESESESGQAE EEKEEAEEAL KEKEKPKEEE WEKPKDAAGL ECKPRPLHKT 

       430        440        450        460        470        480 
CSLFMRNIAP NISRAEIISL CKRYPGFMRV ALSEPQPERR FFRRGWVTFD RSVNIKEICW 

       490        500        510        520        530        540 
NLQNIRLREC ELSPGVNRDL TRRVRNINGI TQHKQIVRND IKLAAKLIHT LDDRTQLWAS 

       550        560        570        580        590        600 
EPGTPPLPTS LPSQNPILKN ITDYLIEEVS AEEEELLGSS GGAPPEEPPK EGNPAEINVE 

       610        620        630        640        650        660 
RDEKLIKVLD KLLLYLRIVH SLDYYNTCEY PNEDEMPNRC GIIHVRGPMP PNRISHGEVL 

       670        680        690        700        710        720 
EWQKTFEEKL TPLLSVRESL SEEEAQKMGR KDPEQEVEKF VTSNTQELGK DKWLCPLSGK 

       730        740        750        760        770        780 
KFKGPEFVRK HIFNKHAEKI EEVKKEVAFF NNFLTDAKRP ALPEIKPAQP PGPAQILPPG 

       790        800        810        820        830        840 
LTPGLPYPHQ TPQGLMPYGQ PRPPILGYGA GAVRPAVPTG GPPYPHAPYG AGRGNYDAFR 

       850        860        870 
GQGGYPGKPR NRMVRGDPRA IVEYRDLDAP DDVDFF 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 371E6A555F1AADBB
Show »

FASTA872100,276
Isoform 3 [UniParc].

Checksum: DC5CB52638E5A1E4
Show »

FASTA875100,537
Isoform 4 [UniParc].

Checksum: 2A1153687E90090B
Show »

FASTA871100,147
Isoform 5 [UniParc].

Checksum: DD73F667E8ADFB67
Show »

FASTA83996,222

References

« Hide 'large scale' references
[1]"Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5."
Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W., Koop B.F.
Nucleic Acids Res. 29:1352-1365(2001) [PubMed: 11239002] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
[2]"Cloning and bioinformatic characterization of the full length human homologous asr2 gene."
Yang L., Huang J., Ying K., Pan Z.M., Gu Y.Q., Wang G.Q., Lin S., Wu H., Yang Q.S., Xie Y., Mao Y.M.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[4]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Testis and Thalamus.
[5]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed: 12690205] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-876 (ISOFORM 1).
Tissue: Brain and Kidney.
[9]Hu G.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 443-876 (ISOFORMS 2/3).
[10]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-8; SER-67; SER-74; SER-493 AND THR-544, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling."
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z.
EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-624 AND TYR-625, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[14]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, MASS SPECTROMETRY.
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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[17]"ARS2 is a conserved eukaryotic gene essential for early mammalian development."
Wilson M.D., Wang D., Wagner R., Breyssens H., Gertsenstein M., Lobe C., Lu X., Nagy A., Burke R.D., Koop B.F., Howard P.L.
Mol. Cell. Biol. 28:1503-1514(2008) [PubMed: 18086880] [Abstract]
Cited for: TISSUE SPECIFICITY.
[18]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-493; SER-540 AND THR-544, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[19]"Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation."
Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M., Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N., Dreyfuss G., Thompson C.B.
Cell 138:328-339(2009) [PubMed: 19632182] [Abstract]
Cited for: FUNCTION.
[20]"Interaction of FLASH with arsenite resistance protein 2 is involved in cell cycle progression at S phase."
Kiriyama M., Kobayashi Y., Saito M., Ishikawa F., Yonehara S.
Mol. Cell. Biol. 29:4729-4741(2009) [PubMed: 19546234] [Abstract]
Cited for: INTERACTION WITH CASP8AP2.
[21]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-540 AND THR-544, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[22]"Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways."
Gilmore-Hebert M., Ramabhadran R., Stern D.F.
Mol. Cancer Res. 8:1388-1398(2010) [PubMed: 20858735] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
[23]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF312032 Genomic DNA. Translation: AAK21005.1.
AF312032 Genomic DNA. Translation: AAK21006.1.
AF248955 mRNA. Translation: AAM00189.1. Frameshift.
AL096723 mRNA. Translation: CAB46374.2.
AK296131 mRNA. Translation: BAG58876.1. Different initiation.
AK302820 mRNA. Translation: BAG64018.1.
AC011895 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23815.1.
CH236956 Genomic DNA. Translation: EAL23816.1. Sequence problems.
CH471091 Genomic DNA. Translation: EAW76467.1.
BC000082 mRNA. Translation: AAH00082.2.
BC069249 mRNA. Translation: AAH69249.1.
BC109117 mRNA. Translation: AAI09118.1.
AF082871 mRNA. Translation: AAD17774.1. Different initiation.
IPIIPI00220038.
IPI00375144.
IPI00888085.
IPI00888510.
IPI00927582.
PIRT12455.
RefSeqNP_001122324.1. NM_001128852.1.
NP_001122325.1. NM_001128853.1.
NP_001122326.1. NM_001128854.1.
NP_056992.4. NM_015908.5.
UniGeneHs.111801.

3D structure databases

ProteinModelPortalQ9BXP5.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9BXP5. 12 interactions.
MINTMINT-1373887.
STRINGQ9BXP5.

PTM databases

PhosphoSiteQ9BXP5.

Polymorphism databases

DMDM20137457.

Proteomic databases

PRIDEQ9BXP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347433; ENSP00000314491; ENSG00000087087.
ENST00000388793; ENSP00000373445; ENSG00000087087.
ENST00000457580; ENSP00000416553; ENSG00000087087.
GeneID51593.
KEGGhsa:51593.
UCSCuc003uwy.2. human.
uc003uwz.2. human.
uc003uxa.2. human.

Organism-specific databases

CTD51593.
GeneCardsGC07P100472.
HGNCHGNC:24101. SRRT.
neXtProtNX_Q9BXP5.
PharmGKBPA164726295.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05613.
GeneTreeENSGT00390000005492.
InParanoidQ9BXP5.
OMAIRKHIFN.
OrthoDBEOG4N30NP.
PhylomeDBQ9BXP5.

Gene expression databases

ArrayExpressQ9BXP5.
BgeeQ9BXP5.
GenevestigatorQ9BXP5.
GermOnlineENSG00000087087. Homo sapiens.

Family and domain databases

InterProIPR007042. Arsenite-R_2.
IPR021933. DUF3546.
[Graphical view]
PfamPF04959. ARS2. 1 hit.
PF12066. DUF3546. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio55439.

Entry information

Entry nameSRRT_HUMAN
AccessionPrimary (citable) accession number: Q9BXP5
Secondary accession number(s): A4D2E5 expand/collapse secondary AC list , A4D2E6, A6NK22, B4DJL4, B4DZA6, O95808, Q32MI4, Q6NT74, Q8TDQ5, Q9BWP6, Q9BXP4, Q9Y4S4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 87 of the entry and version 1 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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

SIMILARITY comments

Index of protein domains and families