MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Staphylococcal nuclease domain-containing protein 1; AltName: Full=100 kDa coactivator; AltName: Full=p100 co-activator; |
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| MyHits synonyms | SND1_PONAB , Q5REU4 , 7A5CD7C056D54B42 |
 Legends: 1, INIT_MET Removed. {ECO:0000250|UniProtKB:Q7KZF4}; 2, N-acetylalanine. {ECO:0000250|UniProtKB:Q7KZF4}; 3, Phosphothreonine. {ECO:0000250|UniProtKB:Q7KZF4}; 4, N6-acetyllysine. {ECO:0000250|UniProtKB:Q7KZF4}; 5, Phosphoserine. {ECO:0000250|UniProtKB:Q7KZF4}; 6, TNase-like 1. {ECO:0000255|PROSITE- ProRule:PRU00272}; 7, TNase-like 2. {ECO:0000255|PROSITE- ProRule:PRU00272}; 8, TNase-like 3. {ECO:0000255|PROSITE- ProRule:PRU00272}; 9, TNase-like 4. {ECO:0000255|PROSITE- ProRule:PRU00272}; 10, Tudor. {ECO:0000255|PROSITE- ProRule:PRU00211}; 11, MOTIF Nuclear localization signal. {ECO:0000255}; 12, ipfam:TUDOR [T]; 13, ipat:TNASE_2 [T]; 14, ipfam:SNase [T]; 15, ismart:TUDOR [T]; 16, iprf:TUDOR [T].
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ID SND1_PONAB Reviewed; 910 AA.
AC Q5REU4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 05-OCT-2016, entry version 70.
DE RecName: Full=Staphylococcal nuclease domain-containing protein 1;
DE AltName: Full=100 kDa coactivator;
DE AltName: Full=p100 co-activator;
GN Name=SND1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a bridging factor between STAT6 and the
CC basal transcription factor. Plays a role in PIM1 regulation of MYB
CC activity. Plays a role in cell viability. Functions as a
CC transcriptional coactivator for STAT5 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GTF2E1 and GTF2E2. Forms a ternary complex
CC with STAT6 and POLR2A. Interacts with STAT5 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}. Melanosome {ECO:0000250}. Note=In IL-4 stimulated
CC cells colocalizes with STAT6 in the nucleus. {ECO:0000250}.
CC -!- PTM: Phosphorylated by PIM1 in vitro. {ECO:0000250}.
CC -!- SIMILARITY: Contains 4 TNase-like domains. {ECO:0000255|PROSITE-
CC ProRule:PRU00272}.
CC -!- SIMILARITY: Contains 1 Tudor domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00211}.
DR EMBL; CR857422; CAH89713.1; -; mRNA.
DR ProteinModelPortal; Q5REU4; -.
DR STRING; 9601.ENSPPYP00000020159; -.
DR PRIDE; Q5REU4; -.
DR eggNOG; KOG2039; Eukaryota.
DR eggNOG; COG1525; LUCA.
DR HOVERGEN; HBG057234; -.
DR InParanoid; Q5REU4; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; IEA:InterPro.
DR GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.90; -; 5.
DR InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002071; Thermonucl_AS.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00565; SNase; 5.
DR Pfam; PF00567; TUDOR; 1.
DR PIRSF; PIRSF017179; RISC-Tudor-SN; 1.
DR SMART; SM00318; SNc; 4.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF50199; SSF50199; 6.
DR PROSITE; PS01284; TNASE_2; 1.
DR PROSITE; PS50830; TNASE_3; 4.
DR PROSITE; PS50304; TUDOR; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q7KZF4}.
FT CHAIN 2 910 Staphylococcal nuclease domain-containing
FT protein 1.
FT /FTId=PRO_0000292280.
FT DOMAIN 18 166 TNase-like 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00272}.
FT DOMAIN 193 328 TNase-like 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00272}.
FT DOMAIN 341 496 TNase-like 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00272}.
FT DOMAIN 525 660 TNase-like 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00272}.
FT DOMAIN 729 787 Tudor. {ECO:0000255|PROSITE-
FT ProRule:PRU00211}.
FT MOTIF 321 325 Nuclear localization signal.
FT {ECO:0000255}.
FT MOTIF 388 392 Nuclear localization signal.
FT {ECO:0000255}.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000250|UniProtKB:Q7KZF4}.
FT MOD_RES 103 103 Phosphothreonine.
FT {ECO:0000250|UniProtKB:Q7KZF4}.
FT MOD_RES 193 193 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:Q7KZF4}.
FT MOD_RES 240 240 Phosphothreonine.
FT {ECO:0000250|UniProtKB:Q7KZF4}.
FT MOD_RES 426 426 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q7KZF4}.
FT MOD_RES 641 641 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:Q7KZF4}.
FT MOD_RES 645 645 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q7KZF4}.
FT MOD_RES 779 779 Phosphothreonine.
FT {ECO:0000250|UniProtKB:Q7KZF4}.
FT MOD_RES 785 785 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q7KZF4}.
FT MOD_RES 909 909 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q7KZF4}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 679 797 ipfam:TUDOR [T]
FT MYHIT 341 496 ismart:SNc [T]
FT MYHIT 525 660 iprf:TNASE_3 [T]
FT MYHIT 103 113 ipat:TNASE_2 [T]
FT MYHIT 193 328 iprf:TNASE_3 [T]
FT MYHIT 220 327 ipfam:SNase [T]
FT MYHIT 368 495 ipfam:SNase [T]
FT MYHIT 18 166 iprf:TNASE_3 [T]
FT MYHIT 728 785 ismart:TUDOR [T]
FT MYHIT 525 660 ismart:SNc [T]
FT MYHIT 18 166 ismart:SNc [T]
FT MYHIT 341 496 iprf:TNASE_3 [T]
FT MYHIT 50 166 ipfam:SNase [T]
FT MYHIT 729 787 iprf:TUDOR [T]
FT MYHIT 848 894 ipfam:SNase [T]
FT MYHIT 553 659 ipfam:SNase [T]
FT MYHIT 193 328 ismart:SNc [T]
SQ SEQUENCE 910 AA; 101993 MW; 7A5CD7C056D54B42 CRC64;
MASSAQSGGS SGGPAVPTVQ RGIVKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGNLA
RRAAATQPDA KDTPDEPWAF PAREFLRKKL IGKEVCFTIE NKTPQGREYG MIYLGKDTNG
ENIAESLVAE GLATRREGMR ANNPEQNRLS ECEEQAKAAK KGMWSEGNGS HTIRDLKYTI
ENPRHFVDSH HQKPVNAIIE HVRDGSVVRA LLLPDYYLVT VMLSGIKCPT FRREADGSET
PEPFAAEAKF FTESRLLQRD VQIILESCHN QNILGTILHP NGNITELLLK EGFARCVDWS
IAVYTRGAEK LRAAERFAKE RRLRIWRDYV APTANLDQKD KQFVAKVMQV LNADAIVVKL
NSGDYKTIHL SSIRPPRLEG ENTQDKNKKL RPLYDIPYMF EAREFLRKKL IGKKVNVTVD
YIRPASPATE TVPAFSERTC ATVTIGGINI AEALVSKGLA TVIRYRQDDD QRSSHYDELL
AAEARAIKNG KGLHSKKEVP IHRVADISGD TQKAKQFLPF LQRAGRSEAV VEYVFSGSRL
KLYLPKETCL ITFLLAGIEC PRGARNLPGL VQEGEPFSEE ATLFTKELVL QREVEVEVES
MDKAGNFIGW LHIDGANLSV LLVEHALSKV HFTAERSSYY KSLLSAEEAA KQKKEKVWAH
YEEQPVEEVM PVLEEKERSA SYKPVFVTEI TDDLHFYVQD VETGTQLEKL MENMRNDIAS
HPPVEGSYAP RRGEFCIAKF VDGEWYRARV EKVESPAKIH VFYIDYGNRE VLPSTRLGTL
PPAFSTRVLP AQATEYAFAF IQVPQDDDAR TDAVDSVVRD IQNTQCLLNV EHLSAGCPHV
TLQFADSKGD VGLGLVKEGL VMVEVRKEKQ FQKVITEYLN AQESAKSARL NLWRYGDFRA
DDADEFGYSR
//
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