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Q9BXP5

- SRRT_HUMAN

UniProt

Q9BXP5 - SRRT_HUMAN

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9BXP5.
ExpressionAtlasiQ9BXP5. baseline and differential.
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. 48 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.
GeneTreeiENSGT00390000005492.
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

        10         20         30         40         50
MGDSDDEYDR RRRDKFRRER SDYDRSRERD ERRRGDDWND REWDRGRERR
60 70 80 90 100
SRGEYRDYDR NRRERFSPPR HELSPPQKRM RRDWDEHSSD PYHSGYEMPY
110 120 130 140 150
AGGGGGPTYG PPQPWGHPDV HIMQHHVLPI QARLGSIAEI DLGVPPPVMK
160 170 180 190 200
TFKEFLLSLD DSVDETEAVK RYNDYKLDFR RQQMQDFFLA HKDEEWFRSK
210 220 230 240 250
YHPDEVGKRR QEARGALQNR LRVFLSLMET GWFDNLLLDI DKADAIVKML
260 270 280 290 300
DAAVIKMEGG TENDLRILEQ EEEEEQAGKP GEPSKKEEGR AGAGLGDGER
310 320 330 340 350
KTNDKDEKKE DGKQAENDSS NDDKTKKSEG DGDKEEKKED SEKEAKKSSK
360 370 380 390 400
KRNRKHSGDD SFDEGSVSES ESESESGQAE EEKEEAEEAL KEKEKPKEEE
410 420 430 440 450
WEKPKDAAGL ECKPRPLHKT CSLFMRNIAP NISRAEIISL CKRYPGFMRV
460 470 480 490 500
ALSEPQPERR FFRRGWVTFD RSVNIKEICW NLQNIRLREC ELSPGVNRDL
510 520 530 540 550
TRRVRNINGI TQHKQIVRND IKLAAKLIHT LDDRTQLWAS EPGTPPLPTS
560 570 580 590 600
LPSQNPILKN ITDYLIEEVS AEEEELLGSS GGAPPEEPPK EGNPAEINVE
610 620 630 640 650
RDEKLIKVLD KLLLYLRIVH SLDYYNTCEY PNEDEMPNRC GIIHVRGPMP
660 670 680 690 700
PNRISHGEVL EWQKTFEEKL TPLLSVRESL SEEEAQKMGR KDPEQEVEKF
710 720 730 740 750
VTSNTQELGK DKWLCPLSGK KFKGPEFVRK HIFNKHAEKI EEVKKEVAFF
760 770 780 790 800
NNFLTDAKRP ALPEIKPAQP PGPAQILPPG LTPGLPYPHQ TPQGLMPYGQ
810 820 830 840 850
PRPPILGYGA GAVRPAVPTG GPPYPHAPYG AGRGNYDAFR GQGGYPGKPR
860 870
NRMVRGDPRA IVEYRDLDAP DDVDFF
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 AAD17774.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAM00189.1 differs from that shown. Reason: Frameshift at position 102. Curated
The sequence BAG58876.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAL23816.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000611405; ENSP00000480421; ENSG00000087087. [Q9BXP5-1]
ENST00000614484; ENSP00000481173; ENSG00000087087. [Q9BXP5-3]
ENST00000618262; ENSP00000478341; ENSG00000087087. [Q9BXP5-2]
ENST00000618411; ENSP00000483556; ENSG00000087087. [Q9BXP5-4]
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:
EMBLi
GenBanki
DDBJi
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. 48 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 ENST00000611405 ; ENSP00000480421 ; ENSG00000087087 . [Q9BXP5-1 ]
ENST00000614484 ; ENSP00000481173 ; ENSG00000087087 . [Q9BXP5-3 ]
ENST00000618262 ; ENSP00000478341 ; ENSG00000087087 . [Q9BXP5-2 ]
ENST00000618411 ; ENSP00000483556 ; ENSG00000087087 . [Q9BXP5-4 ]
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.
GeneTreei ENSGT00390000005492.
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

Bgeei Q9BXP5.
ExpressionAtlasi Q9BXP5. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 113 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