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Q9BXP5

- SRRT_HUMAN

UniProt

Q9BXP5 - SRRT_HUMAN

Protein

Serrate RNA effector molecule homolog

Gene

SRRT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. neuronal stem cell maintenance Source: UniProtKB
    3. primary miRNA processing Source: UniProtKB
    4. regulation of transcription, DNA-templated Source: UniProtKB
    5. response to arsenic-containing substance Source: UniProtKB
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    RNA-mediated gene silencing, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serrate RNA effector molecule homolog
    Alternative name(s):
    Arsenite-resistance protein 2
    Gene namesi
    Name:SRRT
    Synonyms:ARS2, ASR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:24101. SRRT.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164726295.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 876875Serrate RNA effector molecule homologPRO_0000220965Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine2 Publications
    Modified residuei4 – 41Phosphoserine2 Publications
    Modified residuei8 – 81Phosphotyrosine1 Publication
    Modified residuei74 – 741Phosphoserine1 Publication
    Modified residuei493 – 4931Phosphoserine3 Publications
    Modified residuei540 – 5401Phosphoserine2 Publications
    Modified residuei544 – 5441Phosphothreonine7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BXP5.
    PaxDbiQ9BXP5.
    PRIDEiQ9BXP5.

    PTM databases

    PhosphoSiteiQ9BXP5.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9BXP5.
    BgeeiQ9BXP5.
    GenevestigatoriQ9BXP5.

    Organism-specific databases

    HPAiHPA042858.

    Interactioni

    Subunit structurei

    Interacts with NCBP1 and DROSHA By similarity. Interacts with CASP8AP2 and ERBB4.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428583EBI-712721,EBI-466029

    Protein-protein interaction databases

    BioGridi119626. 43 interactions.
    IntActiQ9BXP5. 20 interactions.
    MINTiMINT-1373887.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BXP5.
    SMRiQ9BXP5. Positions 149-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 8273Arg-richAdd
    BLAST
    Compositional biasi258 – 402145Glu-richAdd
    BLAST
    Compositional biasi760 – 82869Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ARS2 family.Curated

    Phylogenomic databases

    eggNOGiNOG283007.
    InParanoidiQ9BXP5.
    OMAiIVHSVDY.
    OrthoDBiEOG70PBXD.
    PhylomeDBiQ9BXP5.
    TreeFamiTF317609.

    Family and domain databases

    InterProiIPR007042. Arsenite-R_2.
    IPR021933. DUF3546.
    [Graphical view]
    PfamiPF04959. ARS2. 1 hit.
    PF12066. DUF3546. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BXP5-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGDSDDEYDR RRRDKFRRER SDYDRSRERD ERRRGDDWND REWDRGRERR    50
    SRGEYRDYDR NRRERFSPPR HELSPPQKRM RRDWDEHSSD PYHSGYEMPY 100
    AGGGGGPTYG PPQPWGHPDV HIMQHHVLPI QARLGSIAEI DLGVPPPVMK 150
    TFKEFLLSLD DSVDETEAVK RYNDYKLDFR RQQMQDFFLA HKDEEWFRSK 200
    YHPDEVGKRR QEARGALQNR LRVFLSLMET GWFDNLLLDI DKADAIVKML 250
    DAAVIKMEGG TENDLRILEQ EEEEEQAGKP GEPSKKEEGR AGAGLGDGER 300
    KTNDKDEKKE DGKQAENDSS NDDKTKKSEG DGDKEEKKED SEKEAKKSSK 350
    KRNRKHSGDD SFDEGSVSES ESESESGQAE EEKEEAEEAL KEKEKPKEEE 400
    WEKPKDAAGL ECKPRPLHKT CSLFMRNIAP NISRAEIISL CKRYPGFMRV 450
    ALSEPQPERR FFRRGWVTFD RSVNIKEICW NLQNIRLREC ELSPGVNRDL 500
    TRRVRNINGI TQHKQIVRND IKLAAKLIHT LDDRTQLWAS EPGTPPLPTS 550
    LPSQNPILKN ITDYLIEEVS AEEEELLGSS GGAPPEEPPK EGNPAEINVE 600
    RDEKLIKVLD KLLLYLRIVH SLDYYNTCEY PNEDEMPNRC GIIHVRGPMP 650
    PNRISHGEVL EWQKTFEEKL TPLLSVRESL SEEEAQKMGR KDPEQEVEKF 700
    VTSNTQELGK DKWLCPLSGK KFKGPEFVRK HIFNKHAEKI EEVKKEVAFF 750
    NNFLTDAKRP ALPEIKPAQP PGPAQILPPG LTPGLPYPHQ TPQGLMPYGQ 800
    PRPPILGYGA GAVRPAVPTG GPPYPHAPYG AGRGNYDAFR GQGGYPGKPR 850
    NRMVRGDPRA IVEYRDLDAP DDVDFF 876
    Length:876
    Mass (Da):100,666
    Last modified:June 1, 2001 - v1
    Checksum:iEB3ABD1325EA98D9
    GO
    Isoform 2 (identifier: Q9BXP5-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         776-780: ILPPG → S

    Show »
    Length:872
    Mass (Da):100,276
    Checksum:i371E6A555F1AADBB
    GO
    Isoform 3 (identifier: Q9BXP5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         388-388: Missing.

    Show »
    Length:875
    Mass (Da):100,537
    Checksum:iDC5CB52638E5A1E4
    GO
    Isoform 4 (identifier: Q9BXP5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         388-388: Missing.
         776-780: ILPPG → S

    Show »
    Length:871
    Mass (Da):100,147
    Checksum:i2A1153687E90090B
    GO
    Isoform 5 (identifier: Q9BXP5-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         196-231: Missing.
         387-387: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:839
    Mass (Da):96,222
    Checksum:iDD73F667E8ADFB67
    GO

    Sequence cautioni

    The sequence AAM00189.1 differs from that shown. Reason: Frameshift at position 102.
    The sequence AAD17774.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061G → GG in CAB46374. (PubMed:11230166)Curated
    Sequence conflicti119 – 1191D → E in AAM00189. 1 PublicationCurated
    Sequence conflicti303 – 3031N → Y in AAM00189. 1 PublicationCurated
    Sequence conflicti311 – 3111D → Y in BAG64018. (PubMed:14702039)Curated
    Sequence conflicti443 – 4431R → K in BAG64018. (PubMed:14702039)Curated
    Sequence conflicti498 – 4981R → W in CAB46374. (PubMed:11230166)Curated
    Sequence conflicti728 – 7281V → A in CAB46374. (PubMed:11230166)Curated
    Sequence conflicti744 – 7441K → R in CAB46374. (PubMed:11230166)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei196 – 23136Missing in isoform 5. 1 PublicationVSP_038122Add
    BLAST
    Alternative sequencei387 – 3871Missing in isoform 5. 1 PublicationVSP_038123
    Alternative sequencei388 – 3881Missing in isoform 3 and isoform 4. 2 PublicationsVSP_032502
    Alternative sequencei776 – 7805ILPPG → S in isoform 2 and isoform 4. 2 PublicationsVSP_000324

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS34709.1. [Q9BXP5-1]
    CCDS47665.1. [Q9BXP5-2]
    CCDS47666.1. [Q9BXP5-3]
    CCDS47667.1. [Q9BXP5-4]
    PIRiT12455.
    RefSeqiNP_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]
    UniGeneiHs.111801.

    Genome annotation databases

    EnsembliENST00000347433; ENSP00000314491; ENSG00000087087. [Q9BXP5-1]
    ENST00000388793; ENSP00000373445; ENSG00000087087. [Q9BXP5-3]
    ENST00000432932; ENSP00000391852; ENSG00000087087. [Q9BXP5-4]
    ENST00000457580; ENSP00000416553; ENSG00000087087. [Q9BXP5-2]
    GeneIDi51593.
    KEGGihsa:51593.
    UCSCiuc003uwy.2. human. [Q9BXP5-1]
    uc003uwz.2. human. [Q9BXP5-2]
    uc003uxa.2. human. [Q9BXP5-4]
    uc010lhl.1. human. [Q9BXP5-3]

    Polymorphism databases

    DMDMi20137457.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS34709.1. [Q9BXP5-1 ]
    CCDS47665.1. [Q9BXP5-2 ]
    CCDS47666.1. [Q9BXP5-3 ]
    CCDS47667.1. [Q9BXP5-4 ]
    PIRi T12455.
    RefSeqi NP_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 ]
    UniGenei Hs.111801.

    3D structure databases

    ProteinModelPortali Q9BXP5.
    SMRi Q9BXP5. Positions 149-252.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119626. 43 interactions.
    IntActi Q9BXP5. 20 interactions.
    MINTi MINT-1373887.

    PTM databases

    PhosphoSitei Q9BXP5.

    Polymorphism databases

    DMDMi 20137457.

    Proteomic databases

    MaxQBi Q9BXP5.
    PaxDbi Q9BXP5.
    PRIDEi Q9BXP5.

    Protocols and materials databases

    DNASUi 51593.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000347433 ; ENSP00000314491 ; ENSG00000087087 . [Q9BXP5-1 ]
    ENST00000388793 ; ENSP00000373445 ; ENSG00000087087 . [Q9BXP5-3 ]
    ENST00000432932 ; ENSP00000391852 ; ENSG00000087087 . [Q9BXP5-4 ]
    ENST00000457580 ; ENSP00000416553 ; ENSG00000087087 . [Q9BXP5-2 ]
    GeneIDi 51593.
    KEGGi hsa:51593.
    UCSCi uc003uwy.2. human. [Q9BXP5-1 ]
    uc003uwz.2. human. [Q9BXP5-2 ]
    uc003uxa.2. human. [Q9BXP5-4 ]
    uc010lhl.1. human. [Q9BXP5-3 ]

    Organism-specific databases

    CTDi 51593.
    GeneCardsi GC07P100472.
    HGNCi HGNC:24101. SRRT.
    HPAi HPA042858.
    MIMi 614469. gene.
    neXtProti NX_Q9BXP5.
    PharmGKBi PA164726295.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283007.
    InParanoidi Q9BXP5.
    OMAi IVHSVDY.
    OrthoDBi EOG70PBXD.
    PhylomeDBi Q9BXP5.
    TreeFami TF317609.

    Miscellaneous databases

    ChiTaRSi SRRT. human.
    GeneWikii ARS2.
    GenomeRNAii 51593.
    NextBioi 55439.
    PROi Q9BXP5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BXP5.
    Bgeei Q9BXP5.
    Genevestigatori Q9BXP5.

    Family and domain databases

    InterProi IPR007042. Arsenite-R_2.
    IPR021933. DUF3546.
    [Graphical view ]
    Pfami PF04959. ARS2. 1 hit.
    PF12066. DUF3546. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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.
      , 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.
      , 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. 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. 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. 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].

    Entry informationi

    Entry nameiSRRT_HUMAN
    AccessioniPrimary (citable) accession number: Q9BXP5
    Secondary accession number(s): A4D2E5
    , A4D2E6, A6NK22, B4DJL4, B4DZA6, O95808, Q32MI4, Q6NT74, Q8TDQ5, Q9BWP6, Q9BXP4, Q9Y4S4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3