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Protein

Staphylococcal nuclease domain-containing protein 1

Gene

SND1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2).1 Publication

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • nuclease activity Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB
  • transcription cofactor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:G66-33488-MONOMER.
BRENDAi3.1.31.1. 2681.
ReactomeiR-HSA-6802952. Signaling by BRAF and RAF fusions.

Names & Taxonomyi

Protein namesi
Recommended name:
Staphylococcal nuclease domain-containing protein 1
Alternative name(s):
100 kDa coactivator
EBNA2 coactivator p100
Tudor domain-containing protein 11
p100 co-activator
Gene namesi
Name:SND1
Synonyms:TDRD11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:30646. SND1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: HPA
  • dense body Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleus Source: ProtInc
  • RISC complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi27044.
OpenTargetsiENSG00000197157.
PharmGKBiPA162404053.

Polymorphism and mutation databases

BioMutaiSND1.
DMDMi60415926.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001831802 – 910Staphylococcal nuclease domain-containing protein 1Add BLAST909

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei103PhosphothreonineCombined sources1
Modified residuei193N6-acetyllysineCombined sources1
Modified residuei240PhosphothreonineCombined sources1
Modified residuei426PhosphoserineCombined sources1
Modified residuei641N6-acetyllysineCombined sources1
Modified residuei645PhosphoserineCombined sources1
Modified residuei779PhosphothreonineCombined sources1
Modified residuei781PhosphoserineCombined sources1
Modified residuei785PhosphoserineCombined sources1
Modified residuei909PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by PIM1 in vitro.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ7KZF4.
MaxQBiQ7KZF4.
PaxDbiQ7KZF4.
PeptideAtlasiQ7KZF4.
PRIDEiQ7KZF4.

2D gel databases

REPRODUCTION-2DPAGEIPI00140420.

PTM databases

iPTMnetiQ7KZF4.
PhosphoSitePlusiQ7KZF4.
SwissPalmiQ7KZF4.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000197157.
CleanExiHS_SND1.
ExpressionAtlasiQ7KZF4. baseline and differential.
GenevisibleiQ7KZF4. HS.

Organism-specific databases

HPAiCAB019323.
HPA002529.
HPA002632.

Interactioni

Subunit structurei

Binds to acidic transactivation domain of EBNA2. Interacts with EAV NSP1. Interacts with GTF2E1 and GTF2E2. Forms a ternary complex with STAT6 and POLR2A. Interacts with STAT5 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
G3BP1Q132833EBI-1044112,EBI-1047359
MTDHQ86UE44EBI-1044112,EBI-1046588

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi117974. 88 interactors.
DIPiDIP-29613N.
IntActiQ7KZF4. 26 interactors.
MINTiMINT-4828459.
STRINGi9606.ENSP00000346762.

Structurei

Secondary structure

1910
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 27Combined sources8
Helixi29 – 31Combined sources3
Beta strandi33 – 36Combined sources4
Beta strandi40 – 43Combined sources4
Beta strandi46 – 51Combined sources6
Beta strandi54 – 56Combined sources3
Helixi79 – 90Combined sources12
Beta strandi94 – 102Combined sources9
Beta strandi108 – 117Combined sources10
Beta strandi120 – 122Combined sources3
Helixi123 – 129Combined sources7
Beta strandi132 – 135Combined sources4
Helixi144 – 159Combined sources16
Helixi162 – 164Combined sources3
Beta strandi165 – 167Combined sources3
Helixi170 – 172Combined sources3
Beta strandi177 – 179Combined sources3
Helixi183 – 188Combined sources6
Turni189 – 192Combined sources4
Beta strandi195 – 204Combined sources10
Beta strandi207 – 212Combined sources6
Turni213 – 216Combined sources4
Beta strandi217 – 223Combined sources7
Helixi245 – 256Combined sources12
Beta strandi260 – 269Combined sources10
Beta strandi272 – 278Combined sources7
Helixi284 – 290Combined sources7
Turni298 – 300Combined sources3
Helixi301 – 303Combined sources3
Helixi308 – 320Combined sources13
Helixi324 – 326Combined sources3
Beta strandi341 – 351Combined sources11
Turni352 – 354Combined sources3
Beta strandi355 – 359Combined sources5
Beta strandi365 – 370Combined sources6
Helixi384 – 386Combined sources3
Turni387 – 389Combined sources3
Helixi392 – 395Combined sources4
Helixi399 – 410Combined sources12
Beta strandi414 – 425Combined sources12
Beta strandi432 – 435Combined sources4
Beta strandi438 – 445Combined sources8
Helixi450 – 456Combined sources7
Beta strandi459 – 462Combined sources4
Helixi476 – 488Combined sources13
Helixi492 – 494Combined sources3
Helixi511 – 523Combined sources13
Beta strandi526 – 544Combined sources19
Turni545 – 548Combined sources4
Beta strandi549 – 559Combined sources11
Beta strandi565 – 567Combined sources3
Beta strandi570 – 572Combined sources3
Helixi578 – 589Combined sources12
Beta strandi593 – 601Combined sources9
Beta strandi607 – 613Combined sources7
Helixi618 – 624Combined sources7
Beta strandi627 – 630Combined sources4
Helixi632 – 634Combined sources3
Helixi640 – 653Combined sources14
Helixi656 – 658Combined sources3
Beta strandi683 – 690Combined sources8
Beta strandi694 – 700Combined sources7
Helixi701 – 703Combined sources3
Helixi706 – 720Combined sources15
Turni725 – 727Combined sources3
Beta strandi735 – 739Combined sources5
Turni741 – 743Combined sources3
Beta strandi745 – 755Combined sources11
Beta strandi758 – 763Combined sources6
Turni764 – 766Combined sources3
Beta strandi769 – 772Combined sources4
Helixi774 – 776Combined sources3
Helixi782 – 784Combined sources3
Turni786 – 788Combined sources3
Beta strandi793 – 798Combined sources6
Helixi807 – 821Combined sources15
Beta strandi824 – 832Combined sources9
Beta strandi835 – 837Combined sources3
Beta strandi839 – 844Combined sources6
Turni845 – 847Combined sources3
Helixi851 – 857Combined sources7
Beta strandi860 – 863Combined sources4
Helixi869 – 871Combined sources3
Helixi872 – 887Combined sources16
Helixi891 – 893Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E6NNMR-A704-800[»]
2HQEX-ray2.00A/B665-910[»]
2HQXX-ray1.42A/B665-910[»]
2O4XX-ray2.00A679-895[»]
B705-795[»]
3BDLX-ray1.90A340-888[»]
3OMCX-ray1.77A/B650-910[»]
3OMGX-ray1.85A/B650-910[»]
4QMGX-ray2.70A/B/C/D/E16-339[»]
ProteinModelPortaliQ7KZF4.
SMRiQ7KZF4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7KZF4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 166TNase-like 1PROSITE-ProRule annotationAdd BLAST149
Domaini193 – 328TNase-like 2PROSITE-ProRule annotationAdd BLAST136
Domaini341 – 496TNase-like 3PROSITE-ProRule annotationAdd BLAST156
Domaini525 – 660TNase-like 4PROSITE-ProRule annotationAdd BLAST136
Domaini729 – 787TudorPROSITE-ProRule annotationAdd BLAST59

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi321 – 325Nuclear localization signalSequence analysis5
Motifi388 – 392Nuclear localization signalSequence analysis5

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.
InParanoidiQ7KZF4.
KOiK15979.
OMAiIQVPQDD.
OrthoDBiEOG091G027G.
PhylomeDBiQ7KZF4.
TreeFamiTF300615.

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.

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

Q7KZF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSAQSGGS SGGPAVPTVQ RGIIKMVLSG CAIIVRGQPR GGPPPERQIN
60 70 80 90 100
LSNIRAGNLA RRAAATQPDA KDTPDEPWAF PAREFLRKKL IGKEVCFTIE
110 120 130 140 150
NKTPQGREYG MIYLGKDTNG ENIAESLVAE GLATRREGMR ANNPEQNRLS
160 170 180 190 200
ECEEQAKAAK KGMWSEGNGS HTIRDLKYTI ENPRHFVDSH HQKPVNAIIE
210 220 230 240 250
HVRDGSVVRA LLLPDYYLVT VMLSGIKCPT FRREADGSET PEPFAAEAKF
260 270 280 290 300
FTESRLLQRD VQIILESCHN QNILGTILHP NGNITELLLK EGFARCVDWS
310 320 330 340 350
IAVYTRGAEK LRAAERFAKE RRLRIWRDYV APTANLDQKD KQFVAKVMQV
360 370 380 390 400
LNADAIVVKL NSGDYKTIHL SSIRPPRLEG ENTQDKNKKL RPLYDIPYMF
410 420 430 440 450
EAREFLRKKL IGKKVNVTVD YIRPASPATE TVPAFSERTC ATVTIGGINI
460 470 480 490 500
AEALVSKGLA TVIRYRQDDD QRSSHYDELL AAEARAIKNG KGLHSKKEVP
510 520 530 540 550
IHRVADISGD TQKAKQFLPF LQRAGRSEAV VEYVFSGSRL KLYLPKETCL
560 570 580 590 600
ITFLLAGIEC PRGARNLPGL VQEGEPFSEE ATLFTKELVL QREVEVEVES
610 620 630 640 650
MDKAGNFIGW LHIDGANLSV LLVEHALSKV HFTAERSSYY KSLLSAEEAA
660 670 680 690 700
KQKKEKVWAH YEEQPVEEVM PVLEEKERSA SYKPVFVTEI TDDLHFYVQD
710 720 730 740 750
VETGTQLEKL MENMRNDIAS HPPVEGSYAP RRGEFCIAKF VDGEWYRARV
760 770 780 790 800
EKVESPAKIH VFYIDYGNRE VLPSTRLGTL SPAFSTRVLP AQATEYAFAF
810 820 830 840 850
IQVPQDDDAR TDAVDSVVRD IQNTQCLLNV EHLSAGCPHV TLQFADSKGD
860 870 880 890 900
VGLGLVKEGL VMVEVRKEKQ FQKVITEYLN AQESAKSARL NLWRYGDFRA
910
DDADEFGYSR
Length:910
Mass (Da):101,997
Last modified:July 5, 2004 - v1
Checksum:iD58BF200F3F3D628
GO

Sequence cautioni

The sequence AAA80488 differs from that shown. Reason: Frameshift at position 5. The frameshift leads to wrong initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti274L → V in AAA80488 (PubMed:7651391).Curated1
Sequence conflicti707 – 708LE → FQ in AAA80488 (PubMed:7651391).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22055 mRNA. Translation: AAA80488.1. Sequence problems.
BT009785 mRNA. Translation: AAP88787.1.
BC017180 mRNA. Translation: AAH17180.3.
CCDSiCCDS34747.1.
PIRiI38968.
RefSeqiNP_055205.2. NM_014390.3.
UniGeneiHs.122523.

Genome annotation databases

EnsembliENST00000354725; ENSP00000346762; ENSG00000197157.
GeneIDi27044.
KEGGihsa:27044.
UCSCiuc003vmi.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22055 mRNA. Translation: AAA80488.1. Sequence problems.
BT009785 mRNA. Translation: AAP88787.1.
BC017180 mRNA. Translation: AAH17180.3.
CCDSiCCDS34747.1.
PIRiI38968.
RefSeqiNP_055205.2. NM_014390.3.
UniGeneiHs.122523.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E6NNMR-A704-800[»]
2HQEX-ray2.00A/B665-910[»]
2HQXX-ray1.42A/B665-910[»]
2O4XX-ray2.00A679-895[»]
B705-795[»]
3BDLX-ray1.90A340-888[»]
3OMCX-ray1.77A/B650-910[»]
3OMGX-ray1.85A/B650-910[»]
4QMGX-ray2.70A/B/C/D/E16-339[»]
ProteinModelPortaliQ7KZF4.
SMRiQ7KZF4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117974. 88 interactors.
DIPiDIP-29613N.
IntActiQ7KZF4. 26 interactors.
MINTiMINT-4828459.
STRINGi9606.ENSP00000346762.

PTM databases

iPTMnetiQ7KZF4.
PhosphoSitePlusiQ7KZF4.
SwissPalmiQ7KZF4.

Polymorphism and mutation databases

BioMutaiSND1.
DMDMi60415926.

2D gel databases

REPRODUCTION-2DPAGEIPI00140420.

Proteomic databases

EPDiQ7KZF4.
MaxQBiQ7KZF4.
PaxDbiQ7KZF4.
PeptideAtlasiQ7KZF4.
PRIDEiQ7KZF4.

Protocols and materials databases

DNASUi27044.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354725; ENSP00000346762; ENSG00000197157.
GeneIDi27044.
KEGGihsa:27044.
UCSCiuc003vmi.4. human.

Organism-specific databases

CTDi27044.
DisGeNETi27044.
GeneCardsiSND1.
HGNCiHGNC:30646. SND1.
HPAiCAB019323.
HPA002529.
HPA002632.
MIMi602181. gene.
neXtProtiNX_Q7KZF4.
OpenTargetsiENSG00000197157.
PharmGKBiPA162404053.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2039. Eukaryota.
COG1525. LUCA.
GeneTreeiENSGT00510000047270.
HOVERGENiHBG057234.
InParanoidiQ7KZF4.
KOiK15979.
OMAiIQVPQDD.
OrthoDBiEOG091G027G.
PhylomeDBiQ7KZF4.
TreeFamiTF300615.

Enzyme and pathway databases

BioCyciZFISH:G66-33488-MONOMER.
BRENDAi3.1.31.1. 2681.
ReactomeiR-HSA-6802952. Signaling by BRAF and RAF fusions.

Miscellaneous databases

ChiTaRSiSND1. human.
EvolutionaryTraceiQ7KZF4.
GeneWikiiSND1.
GenomeRNAii27044.
PROiQ7KZF4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197157.
CleanExiHS_SND1.
ExpressionAtlasiQ7KZF4. baseline and differential.
GenevisibleiQ7KZF4. HS.

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...

Entry informationi

Entry nameiSND1_HUMAN
AccessioniPrimary (citable) accession number: Q7KZF4
Secondary accession number(s): Q13122, Q96AG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 141 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

3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.