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snRNA-activating protein complex subunit 4 (SNAPc subunit 4) (Proximal sequence element-binding transcription factor subunit alpha) (PSE-binding factor subunit alpha) (PTF subunit alpha) (snRNA-activating protein complex 190 kDa subunit) (SNAPc 190 kDa subunit)

 SNPC4_HUMAN             Reviewed;        1469 AA.
Q5SXM2; Q9Y6P7;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
10-OCT-2018, entry version 138.
RecName: Full=snRNA-activating protein complex subunit 4;
Short=SNAPc subunit 4;
AltName: Full=Proximal sequence element-binding transcription factor subunit alpha;
Short=PSE-binding factor subunit alpha;
Short=PTF subunit alpha;
AltName: Full=snRNA-activating protein complex 190 kDa subunit;
Short=SNAPc 190 kDa subunit;
Name=SNAPC4 {ECO:0000312|EMBL:CAI13935.1,
ECO:0000312|HGNC:HGNC:11137};
Synonyms=SNAP190 {ECO:0000312|EMBL:AAC02972.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC02972.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH SNAPC2.
TISSUE=Teratocarcinoma {ECO:0000312|EMBL:AAC02972.1};
PubMed=9418884; DOI=10.1128/MCB.18.1.368;
Wong M.W., Henry R.W., Ma B., Kobayashi R., Klages N., Matthias P.,
Strubin M., Hernandez N.;
"The large subunit of basal transcription factor SNAPc is a Myb domain
protein that interacts with Oct-1.";
Mol. Cell. Biol. 18:368-377(1998).
[2] {ECO:0000312|EMBL:CAI13935.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3] {ECO:0000305}
INTERACTION WITH SNAPC1; SNAPC2 AND SNAPC5, AND MUTAGENESIS OF GLN-94;
GLN-115; LEU-1314; LEU-1355; LEU-1362; LEU-1364 AND LEU-1369.
PubMed=11056176; DOI=10.1074/jbc.M009301200;
Ma B., Hernandez N.;
"A map of protein-protein contacts within the small nuclear RNA-
activating protein complex SNAPc.";
J. Biol. Chem. 276:5027-5035(2001).
[4] {ECO:0000305}
FUNCTION, AND INTERACTION WITH TBP AND BRF2.
PubMed=12621023; DOI=10.1074/jbc.M204247200;
Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W.;
"The small nuclear RNA-activating protein 190 Myb DNA binding domain
stimulates TATA box-binding protein-TATA box recognition.";
J. Biol. Chem. 278:18649-18657(2003).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1157, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1398 AND SER-1400, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-599; SER-626 AND
SER-1224, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Part of the SNAPc complex required for the transcription
of both RNA polymerase II and III small-nuclear RNA genes. Binds
to the proximal sequence element (PSE), a non-TATA-box basal
promoter element common to these 2 types of genes. Recruits TBP
and BRF2 to the U6 snRNA TATA box. {ECO:0000269|PubMed:12621023,
ECO:0000269|PubMed:9418884}.
-!- SUBUNIT: Part of the SNAPc complex composed of 5 subunits: SNAPC1,
SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC4 interacts with SNAPC1,
SNAPC2, SNAPC5, BRF2 and TBP. {ECO:0000269|PubMed:11056176,
ECO:0000269|PubMed:12621023, ECO:0000269|PubMed:9418884}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00625}.
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EMBL; AF032387; AAC02972.1; -; mRNA.
EMBL; AL592301; CAI13935.1; -; Genomic_DNA.
CCDS; CCDS6998.1; -.
PIR; T09219; T09219.
RefSeq; NP_003077.2; NM_003086.3.
RefSeq; XP_005266153.1; XM_005266096.2.
RefSeq; XP_006717304.1; XM_006717241.2.
RefSeq; XP_006717305.1; XM_006717242.3.
UniGene; Hs.113265; -.
ProteinModelPortal; Q5SXM2; -.
SMR; Q5SXM2; -.
BioGrid; 112505; 16.
CORUM; Q5SXM2; -.
IntAct; Q5SXM2; 18.
MINT; Q5SXM2; -.
STRING; 9606.ENSP00000298532; -.
iPTMnet; Q5SXM2; -.
PhosphoSitePlus; Q5SXM2; -.
BioMuta; SNAPC4; -.
DMDM; 74762223; -.
EPD; Q5SXM2; -.
MaxQB; Q5SXM2; -.
PaxDb; Q5SXM2; -.
PeptideAtlas; Q5SXM2; -.
PRIDE; Q5SXM2; -.
ProteomicsDB; 63996; -.
DNASU; 6621; -.
Ensembl; ENST00000298532; ENSP00000298532; ENSG00000165684.
GeneID; 6621; -.
KEGG; hsa:6621; -.
UCSC; uc004chh.4; human.
CTD; 6621; -.
DisGeNET; 6621; -.
EuPathDB; HostDB:ENSG00000165684.3; -.
GeneCards; SNAPC4; -.
H-InvDB; HIX0008543; -.
H-InvDB; HIX0201404; -.
HGNC; HGNC:11137; SNAPC4.
HPA; HPA046627; -.
HPA; HPA073243; -.
MIM; 602777; gene.
neXtProt; NX_Q5SXM2; -.
OpenTargets; ENSG00000165684; -.
PharmGKB; PA35985; -.
eggNOG; KOG0048; Eukaryota.
eggNOG; COG5147; LUCA.
GeneTree; ENSGT00390000001038; -.
HOGENOM; HOG000231537; -.
HOVERGEN; HBG080315; -.
InParanoid; Q5SXM2; -.
KO; K09453; -.
OMA; PVTWVLT; -.
OrthoDB; EOG091G02PC; -.
PhylomeDB; Q5SXM2; -.
TreeFam; TF313064; -.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
ChiTaRS; SNAPC4; human.
GeneWiki; SNAPC4; -.
GenomeRNAi; 6621; -.
PRO; PR:Q5SXM2; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165684; Expressed in 200 organ(s), highest expression level in epithelium of bronchus.
CleanEx; HS_SNAPC4; -.
ExpressionAtlas; Q5SXM2; baseline and differential.
Genevisible; Q5SXM2; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0019185; C:snRNA-activating protein complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0001135; F:RNA polymerase II transcription factor recruiting activity; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0009301; P:snRNA transcription; TAS:ProtInc.
GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0042796; P:snRNA transcription by RNA polymerase III; IDA:UniProtKB.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0006383; P:transcription by RNA polymerase III; TAS:ProtInc.
CDD; cd00167; SANT; 2.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR017877; Myb-like_dom.
InterPro; IPR017930; Myb_dom.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR031282; SNAPC4.
PANTHER; PTHR10641:SF944; PTHR10641:SF944; 1.
Pfam; PF00249; Myb_DNA-binding; 2.
SMART; SM00717; SANT; 5.
SUPFAM; SSF46689; SSF46689; 3.
PROSITE; PS51294; HTH_MYB; 3.
PROSITE; PS50090; MYB_LIKE; 1.
1: Evidence at protein level;
Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation.
CHAIN 1 1469 snRNA-activating protein complex subunit
4.
/FTId=PRO_0000197120.
DOMAIN 250 288 Myb-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00133}.
DOMAIN 289 343 HTH myb-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DOMAIN 344 395 Myb-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00133}.
DOMAIN 396 451 HTH myb-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DOMAIN 452 503 HTH myb-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DNA_BIND 317 341 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DNA_BIND 424 447 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DNA_BIND 476 499 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
REGION 84 133 SNAPC5-binding.
{ECO:0000269|PubMed:11056176}.
REGION 1281 1393 SNAPC2-binding.
{ECO:0000269|PubMed:11056176}.
COMPBIAS 931 1264 Pro-rich. {ECO:0000255}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 599 599 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 626 626 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1157 1157 Phosphothreonine.
{ECO:0000244|PubMed:18220336}.
MOD_RES 1224 1224 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1398 1398 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1400 1400 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1440 1440 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BP86}.
VARIANT 44 44 D -> N (in dbSNP:rs7031489).
/FTId=VAR_059455.
VARIANT 799 799 H -> Q (in dbSNP:rs3812571).
/FTId=VAR_050193.
VARIANT 1448 1448 P -> S (in dbSNP:rs3812561).
/FTId=VAR_050194.
MUTAGEN 94 94 Q->A: Abolishes SNAPC5 binding in the
absence of SNAPC1. Minimal effect on
SNAPC5 binding in the presence of SNAPC1.
{ECO:0000269|PubMed:11056176}.
MUTAGEN 94 94 Q->L: Abolishes SNAPC5 binding in the
absence of SNAPC1. Minimal effect on
SNAPC5 binding in the presence of SNAPC1.
{ECO:0000269|PubMed:11056176}.
MUTAGEN 115 115 Q->L: Abolishes SNAPC5 binding in the
absence of SNAPC1. Minimal effect on
SNAPC5 binding in the presence of SNAPC1.
{ECO:0000269|PubMed:11056176}.
MUTAGEN 1314 1314 L->A: Abolishes SNAPC2-binding.
{ECO:0000269|PubMed:11056176}.
MUTAGEN 1355 1355 L->A: Abolishes SNAPC2-binding.
{ECO:0000269|PubMed:11056176}.
MUTAGEN 1362 1362 L->A: Abolishes SNAPC2-binding.
{ECO:0000269|PubMed:11056176}.
MUTAGEN 1364 1364 L->A: Abolishes SNAPC2-binding.
{ECO:0000269|PubMed:11056176}.
MUTAGEN 1369 1369 L->A: Decreased binding to SNAPC2.
{ECO:0000269|PubMed:11056176}.
CONFLICT 1046 1046 A -> G (in Ref. 1; AAC02972).
{ECO:0000305}.
SEQUENCE 1469 AA; 159433 MW; 78CBCFB1887E106C CRC64;
MDVDAEREKI TQEIKELERI LDPGSSGSHV EISESSLESD SEADSLPSED LDPADPPISE
EERWGEASND EDDPKDKTLP EDPETCLQLN MVYQEVIQEK LAEANLLLAQ NREQQEELMR
DLAGSKGTKV KDGKSLPPST YMGHFMKPYF KDKVTGVGPP ANEDTREKAA QGIKAFEELL
VTKWKNWEKA LLRKSVVSDR LQRLLQPKLL KLEYLHQKQS KVSSELERQA LEKQGREAEK
EIQDINQLPE EALLGNRLDS HDWEKISNIN FEGSRSAEEI RKFWQNSEHP SINKQEWSRE
EEERLQAIAA AHGHLEWQKI AEELGTSRSA FQCLQKFQQH NKALKRKEWT EEEDRMLTQL
VQEMRVGSHI PYRRIVYYME GRDSMQLIYR WTKSLDPGLK KGYWAPEEDA KLLQAVAKYG
EQDWFKIREE VPGRSDAQCR DRYLRRLHFS LKKGRWNLKE EEQLIELIEK YGVGHWAKIA
SELPHRSGSQ CLSKWKIMMG KKQGLRRRRR RARHSVRWSS TSSSGSSSGS SGGSSSSSSS
SSEEDEPEQA QAGEGDRALL SPQYMVPDMD LWVPARQSTS QPWRGGAGAW LGGPAASLSP
PKGSSASQGG SKEASTTAAA PGEETSPVQV PARAHGPVPR SAQASHSADT RPAGAEKQAL
EGGRRLLTVP VETVLRVLRA NTAARSCTQK EQLRQPPLPT SSPGVSSGDS VARSHVQWLR
HRATQSGQRR WRHALHRRLL NRRLLLAVTP WVGDVVVPCT QASQRPAVVQ TQADGLREQL
QQARLASTPV FTLFTQLFHI DTAGCLEVVR ERKALPPRLP QAGARDPPVH LLQASSSAQS
TPGHLFPNVP AQEASKSASH KGSRRLASSR VERTLPQASL LASTGPRPKP KTVSELLQEK
RLQEARAREA TRGPVVLPSQ LLVSSSVILQ PPLPHTPHGR PAPGPTVLNV PLSGPGAPAA
AKPGTSGSWQ EAGTSAKDKR LSTMQALPLA PVFSEAEGTA PAASQAPALG PGQISVSCPE
SGLGQSQAPA ASRKQGLPEA PPFLPAAPSP TPLPVQPLSL THIGGPHVAT SVPLPVTWVL
TAQGLLPVPV PAVVSLPRPA GTPGPAGLLA TLLPPLTETR AAQGPRAPAL SSSWQPPANM
NREPEPSCRT DTPAPPTHAL SQSPAEADGS VAFVPGEAQV AREIPEPRTS SHADPPEAEP
PWSGRLPAFG GVIPATEPRG TPGSPSGTQE PRGPLGLEKL PLRQPGPEKG ALDLEKPPLP
QPGPEKGALD LGLLSQEGEA ATQQWLGGQR GVRVPLLGSR LPYQPPALCS LRALSGLLLH
KKALEHKATS LVVGGEAERP AGALQASLGL VRGQLQDNPA YLLLRARFLA AFTLPALLAT
LAPQGVRTTL SVPSRVGSES EDEDLLSELE LADRDGQPGC TTATCPIQGA PDSGKCSASS
CLDTSNDPDD LDVLRTRHAR HTRKRRRLV


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EIAAB27106 CAAT box DNA-binding protein subunit A,CBF-B,CCAAT-binding transcription factor subunit B,Nfya,NF-YA,Nuclear transcription factor Y subunit A,Nuclear transcription factor Y subunit alpha,Rat,Rattus no
31-227 GABPB2 is the GA-binding protein transcription factor, beta subunit. It forms a tetrameric complex with the alpha subunit, and stimulates transcription of target genes. The encoded protein may be invo 0.05 mg
31-228 GABPB2 encodes the GA-binding protein transcription factor, beta subunit. This protein forms a tetrameric complex with the alpha subunit, and stimulates transcription of target genes. The encoded prot 0.1 mg
27-111 GABPB2 is the GA-binding protein transcription factor, beta subunit. This protein forms a tetrameric complex with the alpha subunit, and stimulates transcription of target genes. The protein may be in 0.05 mg
U0526p CLIA LIS1,LIS-1,Lissencephaly-1 protein,PAF acetylhydrolase 45 kDa subunit,PAF-AH 45 kDa subunit,PAFAH alpha,PAF-AH alpha,PAFAH1B1,PAFAHA,Pig,Platelet-activating factor acetylhydrolase IB subunit alph 96T


 

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