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Q9BXP5 (SRRT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length876 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription By similarity. Ref.18

Subunit structure

Interacts with NCBP1 and DROSHA By similarity. Interacts with CASP8AP2 and ERBB4. Ref.19 Ref.21

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.21

Tissue specificity

Ubiquitously expressed. Ref.15

Sequence similarities

Belongs to the ARS2 family.

Sequence caution

The sequence AAD17774.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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

The sequence BAG58876.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HTTP428583EBI-712721,EBI-466029

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

Initiator methionine11Removed Ref.22
Chain2 – 876875Serrate RNA effector molecule homolog
PRO_0000220965

Regions

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

Amino acid modifications

Modified residue21N-acetylglycine Ref.22 Ref.24
Modified residue41Phosphoserine Ref.22 Ref.24
Modified residue81Phosphotyrosine Ref.10
Modified residue741Phosphoserine Ref.22
Modified residue4931Phosphoserine Ref.10 Ref.14 Ref.22
Modified residue5401Phosphoserine Ref.11 Ref.16
Modified residue5441Phosphothreonine Ref.10 Ref.12 Ref.13 Ref.16 Ref.20 Ref.22 Ref.24

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]"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 TYR-8; SER-493 AND THR-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[16]"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-540 AND THR-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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].
[18]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CASP8AP2.
[20]"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-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
[22]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-74; SER-493 AND THR-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND THR-544, 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.
CCDSCCDS34709.1. [Q9BXP5-1]
CCDS47665.1. [Q9BXP5-2]
CCDS47666.1. [Q9BXP5-3]
CCDS47667.1. [Q9BXP5-4]
PIRT12455.
RefSeqNP_001122324.1. NM_001128852.1. [Q9BXP5-3]
NP_001122325.1. NM_001128853.1. [Q9BXP5-2]
NP_001122326.1. NM_001128854.1. [Q9BXP5-4]
NP_056992.4. NM_015908.5. [Q9BXP5-1]
UniGeneHs.111801.

3D structure databases

ProteinModelPortalQ9BXP5.
SMRQ9BXP5. Positions 149-252.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119626. 41 interactions.
IntActQ9BXP5. 20 interactions.
MINTMINT-1373887.

PTM databases

PhosphoSiteQ9BXP5.

Polymorphism databases

DMDM20137457.

Proteomic databases

MaxQBQ9BXP5.
PaxDbQ9BXP5.
PRIDEQ9BXP5.

Protocols and materials databases

DNASU51593.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347433; ENSP00000314491; ENSG00000087087. [Q9BXP5-1]
ENST00000388793; ENSP00000373445; ENSG00000087087. [Q9BXP5-3]
ENST00000432932; ENSP00000391852; ENSG00000087087. [Q9BXP5-4]
ENST00000457580; ENSP00000416553; ENSG00000087087. [Q9BXP5-2]
GeneID51593.
KEGGhsa:51593.
UCSCuc003uwy.2. human. [Q9BXP5-1]
uc003uwz.2. human. [Q9BXP5-2]
uc003uxa.2. human. [Q9BXP5-4]
uc010lhl.1. human. [Q9BXP5-3]

Organism-specific databases

CTD51593.
GeneCardsGC07P100472.
HGNCHGNC:24101. SRRT.
HPAHPA042858.
MIM614469. gene.
neXtProtNX_Q9BXP5.
PharmGKBPA164726295.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283007.
InParanoidQ9BXP5.
OMAIVHSVDY.
OrthoDBEOG70PBXD.
PhylomeDBQ9BXP5.
TreeFamTF317609.

Gene expression databases

ArrayExpressQ9BXP5.
BgeeQ9BXP5.
GenevestigatorQ9BXP5.

Family and domain databases

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

Other

ChiTaRSSRRT. human.
GeneWikiARS2.
GenomeRNAi51593.
NextBio55439.
PROQ9BXP5.
SOURCESearch...

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: July 9, 2014
This is version 110 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 7

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