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Protein

Staphylococcal nuclease domain-containing protein 1

Gene

Snd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Plays a role in cell viability. Functions as a transcriptional coactivator for STAT5. Plays a role in cell viability (By similarity).By similarity

GO - Molecular functioni

  • nuclease activity Source: InterPro
  • poly(A) RNA binding Source: Ensembl
  • transcription coactivator activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Staphylococcal nuclease domain-containing protein 1
Alternative name(s):
100 kDa coactivator
SND p102
p100 co-activator
p105 coactivator
Gene namesi
Name:Snd1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi631340. Snd1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Melanosome By similarity

  • Note: In IL-4 stimulated cells colocalizes with STAT6 in the nucleus.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 909909Staphylococcal nuclease domain-containing protein 1PRO_0000183182Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921N6-acetyllysineBy similarity
Modified residuei234 – 2341PhosphothreonineBy similarity
Modified residuei425 – 4251PhosphoserineBy similarity
Modified residuei640 – 6401N6-acetyllysineBy similarity
Modified residuei908 – 9081PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by PIM1 in vitro.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ66X93.
PRIDEiQ66X93.

PTM databases

iPTMnetiQ66X93.
PhosphoSiteiQ66X93.

Expressioni

Gene expression databases

ExpressionAtlasiQ66X93. baseline and differential.
GenevisibleiQ66X93. RN.

Interactioni

Subunit structurei

Interacts with GTF2E1 and GTF2E2. Forms a ternary complex with STAT6 and POLR2A. Interacts with STAT5 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ66X93. 3 interactions.
STRINGi10116.ENSRNOP00000041531.

Structurei

3D structure databases

ProteinModelPortaliQ66X93.
SMRiQ66X93. Positions 678-894.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 165149TNase-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini192 – 327136TNase-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini340 – 495156TNase-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini524 – 659136TNase-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini728 – 78659TudorPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi320 – 3245Nuclear localization signalSequence analysis
Motifi387 – 3915Nuclear localization signalSequence analysis

Sequence similaritiesi

Contains 4 TNase-like domains.PROSITE-ProRule annotation
Contains 1 Tudor domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2039. Eukaryota.
COG1525. LUCA.
GeneTreeiENSGT00510000047270.
HOVERGENiHBG057234.
InParanoidiQ66X93.
KOiK15979.
OMAiIQVPQDD.
OrthoDBiEOG7FJGZT.
PhylomeDBiQ66X93.

Family and domain databases

Gene3Di2.40.50.90. 5 hits.
InterProiIPR016685. Silence_cplx_Nase-comp_TudorSN.
IPR016071. Staphylococal_nuclease_OB-fold.
IPR002071. Thermonucl_AS.
IPR002999. Tudor.
[Graphical view]
PfamiPF00565. SNase. 5 hits.
PF00567. TUDOR. 1 hit.
[Graphical view]
PIRSFiPIRSF017179. RISC-Tudor-SN. 1 hit.
SMARTiSM00318. SNc. 4 hits.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMiSSF50199. SSF50199. 6 hits.
PROSITEiPS01284. TNASE_2. 1 hit.
PS50830. TNASE_3. 4 hits.
PS50304. TUDOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q66X93-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASAQSSGSS GGPAVPTVQR GIVKMVLSGC AIIVRGQPRG GPPPERQINL
60 70 80 90 100
SNIRAGNLAR RAAATQPDGK DTPDEPWAFP AREFLRKKLI GKEVCFTIEN
110 120 130 140 150
KTPQGREYGM IYLGKDTNGE NIAESLVAEG LASRREGMRA NNPEQNRLSE
160 170 180 190 200
CEEQAKASKK GMWSEGNGSH TIRDLKYTIE NPRHFVDSHH QKPVNAIIEH
210 220 230 240 250
VRDGSVVRAL LLPDHYLVTV MLSGIKCPTF RRETDGSETP EPFAAEAKFF
260 270 280 290 300
TESRLLQRDV QIILESCHNQ NILGTILHPN GNITELLLKE GFARCVDWSI
310 320 330 340 350
AVYTRGAEKL RAAERFAKER RLRIWRDYVP PTANLDQKDK QFVAKVMQVL
360 370 380 390 400
NADAIVVKLN SGDYKTIHLS SIRPPRLEGD NIQDKNKKLR PLYDIPYMFE
410 420 430 440 450
AREFLRKKLI GKKVSVTVDY IRPASPATET VPAFSERTCA TVTIGGINIA
460 470 480 490 500
EALVSKGLAT VIRYRQDDDQ RSSHYDELLA AEARAIKNGK GLHSKKEVPI
510 520 530 540 550
HRVADISGDT QKAKQFLPFL QRAGRSEAVV EYVFSGSRLK LYLPKETCLI
560 570 580 590 600
TFLLAGIECP RGARNLPGLV QEGEPFSEEA TLFTKELVLQ REVEVEVESM
610 620 630 640 650
DKAGNFIGWL HMDGANLSVL LVEHALSKVH FTAERSAYYK PLLSAEEAAK
660 670 680 690 700
QRKEKVWAHY EEQPVEEVMP VLEEKERSAS YKPVFVTEIT DDLHFYVQDV
710 720 730 740 750
ETGTQLEKLM ENMRSDISSH PPVEGAYAPR RGEFCIAKFV DGEWYRARVE
760 770 780 790 800
KVESPAKVHV FYIDYGNREI LPSTRLGALP PAFSTRVLPA QATEYAFAFI
810 820 830 840 850
QVPQDEDART DAVDSVVRDI QNTQCLLNVE HLSASCPHVT LQFADSKGDV
860 870 880 890 900
GLGLVKEGLV MVEVRKEKQF QKVITEYLNA QESAKSARLN LWRYGDFRAD

DADEFGYSR
Length:909
Mass (Da):101,952
Last modified:October 11, 2004 - v1
Checksum:iCD032114A1051784
GO

Sequence cautioni

The sequence AAB41439.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321I → M in AAB41439 (Ref. 3) Curated
Sequence conflicti37 – 371Q → L in AAB41439 (Ref. 3) Curated
Sequence conflicti41 – 433GPP → TA in AAB41439 (Ref. 3) Curated
Sequence conflicti59 – 591A → DT in AAB41439 (Ref. 3) Curated
Sequence conflicti62 – 621A → R in AAB41439 (Ref. 3) Curated
Sequence conflicti133 – 1375SRREG → PGES in AAB41439 (Ref. 3) Curated
Sequence conflicti167 – 1737NGSHTIR → TGHTHP in AAB41439 (Ref. 3) Curated
Sequence conflicti360 – 3601N → S in AAB41439 (Ref. 3) Curated
Sequence conflicti450 – 4501A → T in AAB41439 (Ref. 3) Curated
Sequence conflicti637 – 6371A → G in AAB41439 (Ref. 3) Curated
Sequence conflicti726 – 7283AYA → LR in AAB41439 (Ref. 3) Curated
Sequence conflicti752 – 7521V → E in AAB41439 (Ref. 3) Curated
Sequence conflicti777 – 7771Missing in AAB41439 (Ref. 3) Curated
Sequence conflicti802 – 8021V → W in AAB41439 (Ref. 3) Curated
Sequence conflicti814 – 8185DSVVR → TVCA in AAB41439 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY697864 mRNA. Translation: AAU05374.1.
BC072471 mRNA. Translation: AAH72471.2.
U83883 mRNA. Translation: AAB41439.1. Different initiation.
RefSeqiNP_073185.2. NM_022694.2.
UniGeneiRn.36148.

Genome annotation databases

EnsembliENSRNOT00000047698; ENSRNOP00000041531; ENSRNOG00000031173.
GeneIDi64635.
KEGGirno:64635.
UCSCiRGD:631340. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY697864 mRNA. Translation: AAU05374.1.
BC072471 mRNA. Translation: AAH72471.2.
U83883 mRNA. Translation: AAB41439.1. Different initiation.
RefSeqiNP_073185.2. NM_022694.2.
UniGeneiRn.36148.

3D structure databases

ProteinModelPortaliQ66X93.
SMRiQ66X93. Positions 678-894.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ66X93. 3 interactions.
STRINGi10116.ENSRNOP00000041531.

PTM databases

iPTMnetiQ66X93.
PhosphoSiteiQ66X93.

Proteomic databases

PaxDbiQ66X93.
PRIDEiQ66X93.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000047698; ENSRNOP00000041531; ENSRNOG00000031173.
GeneIDi64635.
KEGGirno:64635.
UCSCiRGD:631340. rat.

Organism-specific databases

CTDi27044.
RGDi631340. Snd1.

Phylogenomic databases

eggNOGiKOG2039. Eukaryota.
COG1525. LUCA.
GeneTreeiENSGT00510000047270.
HOVERGENiHBG057234.
InParanoidiQ66X93.
KOiK15979.
OMAiIQVPQDD.
OrthoDBiEOG7FJGZT.
PhylomeDBiQ66X93.

Miscellaneous databases

PROiQ66X93.

Gene expression databases

ExpressionAtlasiQ66X93. baseline and differential.
GenevisibleiQ66X93. RN.

Family and domain databases

Gene3Di2.40.50.90. 5 hits.
InterProiIPR016685. Silence_cplx_Nase-comp_TudorSN.
IPR016071. Staphylococal_nuclease_OB-fold.
IPR002071. Thermonucl_AS.
IPR002999. Tudor.
[Graphical view]
PfamiPF00565. SNase. 5 hits.
PF00567. TUDOR. 1 hit.
[Graphical view]
PIRSFiPIRSF017179. RISC-Tudor-SN. 1 hit.
SMARTiSM00318. SNc. 4 hits.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMiSSF50199. SSF50199. 6 hits.
PROSITEiPS01284. TNASE_2. 1 hit.
PS50830. TNASE_3. 4 hits.
PS50304. TUDOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cellular localization of cloned StaphylocoCCal nuclease domain containing rat p102."
    Palacios L., Fresnedo O., Ochoa B.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "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].
    Tissue: Lung.
  3. "Rat p105 homologous to human B-cell p100 co-activator."
    Kassessinoff T., Amouzadeh H., Accili D., Beaven M.A., Sagi-Eisenberg R.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-909.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSND1_RAT
AccessioniPrimary (citable) accession number: Q66X93
Secondary accession number(s): P97693, Q6IN40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 11, 2004
Last modified: June 8, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.