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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

  • nuclease activity Source: InterPro
  • 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

BRENDAi3.1.31.1. 2681.

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

  • 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

PharmGKBiPA162404053.

Polymorphism and mutation databases

BioMutaiSND1.
DMDMi60415926.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 910909Staphylococcal nuclease domain-containing protein 1PRO_0000183180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei103 – 1031PhosphothreonineCombined sources
Modified residuei193 – 1931N6-acetyllysineCombined sources
Modified residuei240 – 2401PhosphothreonineCombined sources
Modified residuei426 – 4261PhosphoserineCombined sources
Modified residuei641 – 6411N6-acetyllysineCombined sources
Modified residuei645 – 6451PhosphoserineCombined sources
Modified residuei779 – 7791PhosphothreonineCombined sources
Modified residuei781 – 7811PhosphoserineCombined sources
Modified residuei785 – 7851PhosphoserineCombined sources
Modified residuei909 – 9091PhosphoserineCombined sources

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.
PhosphoSiteiQ7KZF4.
SwissPalmiQ7KZF4.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ7KZF4.
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

Protein-protein interaction databases

BioGridi117974. 88 interactions.
DIPiDIP-29613N.
IntActiQ7KZF4. 25 interactions.
MINTiMINT-4828459.
STRINGi9606.ENSP00000346762.

Structurei

Secondary structure

1
910
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 278Combined sources
Helixi29 – 313Combined sources
Beta strandi33 – 364Combined sources
Beta strandi40 – 434Combined sources
Beta strandi46 – 516Combined sources
Beta strandi54 – 563Combined sources
Helixi79 – 9012Combined sources
Beta strandi94 – 1029Combined sources
Beta strandi108 – 11710Combined sources
Beta strandi120 – 1223Combined sources
Helixi123 – 1297Combined sources
Beta strandi132 – 1354Combined sources
Helixi144 – 15916Combined sources
Helixi162 – 1643Combined sources
Beta strandi165 – 1673Combined sources
Helixi170 – 1723Combined sources
Beta strandi177 – 1793Combined sources
Helixi183 – 1886Combined sources
Turni189 – 1924Combined sources
Beta strandi195 – 20410Combined sources
Beta strandi207 – 2126Combined sources
Turni213 – 2164Combined sources
Beta strandi217 – 2237Combined sources
Helixi245 – 25612Combined sources
Beta strandi260 – 26910Combined sources
Beta strandi272 – 2787Combined sources
Helixi284 – 2907Combined sources
Turni298 – 3003Combined sources
Helixi301 – 3033Combined sources
Helixi308 – 32013Combined sources
Helixi324 – 3263Combined sources
Beta strandi341 – 35111Combined sources
Turni352 – 3543Combined sources
Beta strandi355 – 3595Combined sources
Beta strandi365 – 3706Combined sources
Helixi384 – 3863Combined sources
Turni387 – 3893Combined sources
Helixi392 – 3954Combined sources
Helixi399 – 41012Combined sources
Beta strandi414 – 42512Combined sources
Beta strandi432 – 4354Combined sources
Beta strandi438 – 4458Combined sources
Helixi450 – 4567Combined sources
Beta strandi459 – 4624Combined sources
Helixi476 – 48813Combined sources
Helixi492 – 4943Combined sources
Helixi511 – 52313Combined sources
Beta strandi526 – 54419Combined sources
Turni545 – 5484Combined sources
Beta strandi549 – 55911Combined sources
Beta strandi565 – 5673Combined sources
Beta strandi570 – 5723Combined sources
Helixi578 – 58912Combined sources
Beta strandi593 – 6019Combined sources
Beta strandi607 – 6137Combined sources
Helixi618 – 6247Combined sources
Beta strandi627 – 6304Combined sources
Helixi632 – 6343Combined sources
Helixi640 – 65314Combined sources
Helixi656 – 6583Combined sources
Beta strandi683 – 6908Combined sources
Beta strandi694 – 7007Combined sources
Helixi701 – 7033Combined sources
Helixi706 – 72015Combined sources
Turni725 – 7273Combined sources
Beta strandi735 – 7395Combined sources
Turni741 – 7433Combined sources
Beta strandi745 – 75511Combined sources
Beta strandi758 – 7636Combined sources
Turni764 – 7663Combined sources
Beta strandi769 – 7724Combined sources
Helixi774 – 7763Combined sources
Helixi782 – 7843Combined sources
Turni786 – 7883Combined sources
Beta strandi793 – 7986Combined sources
Helixi807 – 82115Combined sources
Beta strandi824 – 8329Combined sources
Beta strandi835 – 8373Combined sources
Beta strandi839 – 8446Combined sources
Turni845 – 8473Combined sources
Helixi851 – 8577Combined sources
Beta strandi860 – 8634Combined sources
Helixi869 – 8713Combined sources
Helixi872 – 88716Combined sources
Helixi891 – 8933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 17-332, 340-897.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7KZF4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 166149TNase-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini193 – 328136TNase-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini341 – 496156TNase-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini525 – 660136TNase-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini729 – 78759TudorPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi321 – 3255Nuclear localization signalSequence analysis
Motifi388 – 3925Nuclear 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.
InParanoidiQ7KZF4.
KOiK15979.
OMAiIQVPQDD.
OrthoDBiEOG7FJGZT.
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 AAA80488.1 differs from that shown. Reason: Frameshift at position 5. The frameshift leads to wrong initiation.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741L → V in AAA80488 (PubMed:7651391).Curated
Sequence conflicti707 – 7082LE → FQ in AAA80488 (PubMed:7651391).Curated

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_014390.2.
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_014390.2.
UniGeneiHs.122523.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 17-332, 340-897.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117974. 88 interactions.
DIPiDIP-29613N.
IntActiQ7KZF4. 25 interactions.
MINTiMINT-4828459.
STRINGi9606.ENSP00000346762.

PTM databases

iPTMnetiQ7KZF4.
PhosphoSiteiQ7KZF4.
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.
GeneCardsiSND1.
HGNCiHGNC:30646. SND1.
HPAiCAB019323.
HPA002529.
HPA002632.
MIMi602181. gene.
neXtProtiNX_Q7KZF4.
PharmGKBiPA162404053.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2039. Eukaryota.
COG1525. LUCA.
GeneTreeiENSGT00510000047270.
HOVERGENiHBG057234.
InParanoidiQ7KZF4.
KOiK15979.
OMAiIQVPQDD.
OrthoDBiEOG7FJGZT.
PhylomeDBiQ7KZF4.
TreeFamiTF300615.

Enzyme and pathway databases

BRENDAi3.1.31.1. 2681.

Miscellaneous databases

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

Gene expression databases

BgeeiQ7KZF4.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE."
    Tong X., Drapkin R., Yalamanchili R., Mosialos G., Kieff E.
    Mol. Cell. Biol. 15:4735-4744(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 234-249; 567-586; 642-651; 679-704 AND 788-818, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH EBNA2; GTF2E1 AND GTF2E2.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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: Lymph.
  4. Bienvenut W.V., Zebisch A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-21; 48-55; 72-83; 108-136; 178-184; 328-339; 347-359; 516-523; 527-539; 642-651; 716-731; 777-787; 811-819 AND 874-886, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  5. "Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II."
    Yang J., Aittomaeki S., Pesu M., Carter K., Saarinen J., Kalkkinen N., Kieff E., Silvennoinen O.
    EMBO J. 21:4950-4958(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STAT6 AND POLR2A.
  6. Cited for: INTERACTION WITH PIM1, PHOSPHORYLATION BY PIM1.
  7. "Equine arteritis virus non-structural protein 1, an essential factor for viral subgenomic mRNA synthesis, interacts with the cellular transcription co-factor p100."
    Tijms M.A., Snijder E.J.
    J. Gen. Virol. 84:2317-2322(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EAV NSP1.
  8. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 SER-909, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-193 AND LYS-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103; THR-240; SER-426; SER-645; THR-779; SER-781; SER-785 AND SER-909, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426; THR-779; SER-781 AND SER-909, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Solution structure of the Tudor domain of staphylococcal nuclease domain-containing protein 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 704-800.

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: July 6, 2016
This is version 137 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.