Q7KZ85 (SPT6H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription elongation factor SPT6
Short name=hSPT6

Alternative name(s):
Tat-cotransactivator 2 protein
Short name=Tat-CT2 protein

Gene names

Name:	SUPT6H
Synonyms:	KIAA0162, SPT6H

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1726 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts to stimulate transcriptional elongation by RNA polymerase II. Ref.6 Ref.7
Subunit structure	Interacts with RNA polymerase II and the DRB sensitivity-inducing factor complex (DSIF complex), which is composed of SUPT5H and SUPT4H1. Interacts with human cytomegalovirus/HHV-5 protein UL69. Ref.7 Ref.16
Subcellular location	Nucleus Probable.
Tissue specificity	Ubiquitously expressed.
Sequence similarities	Belongs to the SPT6 family. Contains 1 S1 motif domain. Contains 1 SH2 domain.
Sequence caution	The sequence AAB18949.1 differs from that shown. Reason: Frameshift at position 988. The sequence AAC50821.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH33074.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA11479.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin remodeling Non-traceable author statement Ref.1. Source: UniProtKB regulation of DNA-dependent transcription, elongation Inferred from electronic annotation. Source: InterPro regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: InterPro transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on ester bonds Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q7KZ85-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q7KZ85-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1181: Missing.
     1182-1211: ESYDQAIRNDETGLWQCPFCQQDNFPELSE → MPSRGTRPEDSSVLIPTDNSTPHKEDLSSK

Isoform 3 (identifier: Q7KZ85-3)

The sequence of this isoform differs from the canonical sequence as follows:
     617-1616: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.15
	Chain	2 – 1726	1725	Transcription elongation factor SPT6		PRO_0000072171
Regions
	Domain	1213 – 1282	70	S1 motif
	Domain	1325 – 1431	107	SH2
	Compositional bias	6 – 250	245	Asp/Glu-rich
	Compositional bias	1525 – 1528	4	Poly-Ser
	Compositional bias	1654 – 1657	4	Poly-Ser
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.15
	Modified residue	7	1	Phosphoserine Ref.15
	Modified residue	12	1	Phosphoserine Ref.15
	Modified residue	73	1	Phosphoserine Ref.11
	Modified residue	75	1	Phosphoserine Ref.11
	Modified residue	78	1	Phosphoserine Ref.11
	Modified residue	125	1	Phosphoserine Ref.8 Ref.13 Ref.15
	Modified residue	267	1	Phosphoserine Ref.10
	Modified residue	743	1	N6-acetyllysine Ref.12
	Modified residue	1523	1	Phosphothreonine Ref.10 Ref.13
	Modified residue	1532	1	Phosphothreonine Ref.11 Ref.13
	Modified residue	1535	1	Phosphoserine Ref.9 Ref.10 Ref.11 Ref.15
	Modified residue	1539	1	Phosphothreonine Ref.9 Ref.10 Ref.11
	Modified residue	1676	1	N6-acetyllysine Ref.12
	Modified residue	1697	1	Phosphothreonine Ref.11 Ref.13
	Modified residue	1701	1	Phosphoserine Ref.10 Ref.11 Ref.13
	Modified residue	1703	1	Phosphoserine Ref.10 Ref.11 Ref.13
	Modified residue	1718	1	Phosphothreonine Ref.9 Ref.10 Ref.11 Ref.13
Natural variations
	Alternative sequence	1 – 1181	1181	Missing in isoform 2.		VSP_011505
	Alternative sequence	617 – 1616	1000	Missing in isoform 3.		VSP_011507
	Alternative sequence	1182 – 1211	30	ESYDQ…PELSE → MPSRGTRPEDSSVLIPTDNS TPHKEDLSSK in isoform 2.		VSP_011506
Experimental info
	Sequence conflict	61 – 73	13	DDDED…EDEGS → ATAPGHPKLSEGR in AAC50821. Ref.1
	Sequence conflict	100 – 109	10	DFDLIEENLG → LEDDDFLLNE in AAH33074. Ref.4
	Sequence conflict	988 – 994	7	YVCGLGP → VCLWPGT Ref.1
	Sequence conflict	1545	1	L → P in AAH17105. Ref.4
	Sequence conflict	1627	1	S → I in AAH17105. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 31, 2004. Version 2. Checksum: F7EB22FA669EB030	FASTA	1,726	199,073
	10 20 30 40 50 60 MSDFVESEAE ESEEEYNDEG EVVPRVTKKF VEEEDDDEEE EEENLDDQDE QGNLKGFIND 70 80 90 100 110 120 DDDEDEGEED EGSDSGDSED DVGHKKRKRT SFDDRLEDDD FDLIEENLGV KVKRGQKYRR 130 140 150 160 170 180 VKKMSDDEDD DEEEYGKEEH EKEAIAEEIF QDGEGEEGQE AMEAPMAPPE EEEEDDEESD 190 200 210 220 230 240 IDDFIVDDDG QPLKKPKWRK KLPGYTDAAL QEAQEIFGVD FDYDEFEKYN EYDEELEEEY 250 260 270 280 290 300 EYEDDEAEGE IRVRPKKTTK KRVSRRSIFE MYEPSELESS HLTDQDNEIR ATDLPERFQL 310 320 330 340 350 360 RSIPVKGAED DELEEEADWI YRNAFATPTI SLQESCDYLD RGQPASSFSR KGPSTIQKIK 370 380 390 400 410 420 EALGFMRNQH FEVPFIAFYR KEYVEPELHI NDLWRVWQWD EKWTQLRIRK ENLTRLFEKM 430 440 450 460 470 480 QAYQYEQISA DPDKPLADGI RALDTTDMER LKDVQSMDEL KDVYNHFLLY YGRDIPKMQN 490 500 510 520 530 540 AAKASRKKLK RVREEGDEEG EGDEAEDEEQ RGPELKQASR RDMYTICQSA GLDGLAKKFG 550 560 570 580 590 600 LTPEQFGENL RDSYQRHETE QFPAEPLELA KDYVCSQFPT PEAVLEGARY MVALQIAREP 610 620 630 640 650 660 LVRQVLRQTF QERAKLNITP TKKGRKDVDE AHYAYSFKYL KNKPVKELRD DQFLKICLAE 670 680 690 700 710 720 DEGLLTTDIS IDLKGVEGYG NDQTYFEEIK QFYYRDEFSH QVQEWNRQRT MAIERALQQF 730 740 750 760 770 780 LYVQMAKELK NKLLAEAKEY VIKACSRKLY NWLRVAPYRP DQQVEEDDDF MDENQGKGIR 790 800 810 820 830 840 VLGIAFSSAR DHPVFCALVN GEGEVTDFLR LPHFTKRRTA WREEEREKKA QDIETLKKFL 850 860 870 880 890 900 LNKKPHVVTV AGENRDAQML IEDVKRIVHE LDQGQQLSSI GVELVDNELA ILYMNSKKSE 910 920 930 940 950 960 AEFRDYPPVL RQAVSLARRI QDPLIEFAQV CSSDEDILCL KFHPLQEHVV KEELLNALYC 970 980 990 1000 1010 1020 EFINRVNEVG VDVNRAIAHP YSQALIQYVC GLGPRKGTHL LKILKQNNTR LESRTQLVTM 1030 1040 1050 1060 1070 1080 CHMGPKVFMN CAGFLKIDTA SLGDSTDSYI EVLDGSRVHP ETYEWARKMA VDALEYDESA 1090 1100 1110 1120 1130 1140 EDANPAGALE EILENPERLK DLDLDAFAEE LERQGYGDKH ITLYDIRAEL SCRYKDLRTA 1150 1160 1170 1180 1190 1200 YRSPNTEEIF NMLTKETPET FYIGKLIICN VTGIAHRRPQ GESYDQAIRN DETGLWQCPF 1210 1220 1230 1240 1250 1260 CQQDNFPELS EVWNHFDSGS CPGQAIGVKT RLDNGVTGFI PTKFLSDKVV KRPEERVKVG 1270 1280 1290 1300 1310 1320 MTVHCRIMKI DIEKFSADLT CRTSDLMDRN NEWKLPKDTY YDFDAEAADH KQEEDMKRKQ 1330 1340 1350 1360 1370 1380 QRTTYIKRVI AHPSFHNINF KQAEKMMETM DQGDVIIRPS SKGENHLTVT WKVSDGIYQH 1390 1400 1410 1420 1430 1440 VDVREEGKEN AFSLGATLWI NSEEFEDLDE IVARYVQPMA SFARDLLNHK YYQDCSGGDR 1450 1460 1470 1480 1490 1500 KKLEELLIKT KKEKPTFIPY FICACKELPG KFLLGYQPRG KPRIEYVTVT PEGFRYRGQI 1510 1520 1530 1540 1550 1560 FPTVNGLFRW FKDHYQDPVP GITPSSSSRT RTPASINATP ANINLADLTR AVNALPQNMT 1570 1580 1590 1600 1610 1620 SQMFSAIAAV TGQGQNPNAT PAQWASSQYG YGGSGGGSSA YHVFPTPAQQ PVATPLMTPS 1630 1640 1650 1660 1670 1680 YSYTTPSQPI TTPQYHQLQA STTPQSAQAQ PQPSSSSRQR QQQPKSNSHA AIDWGKMAEQ 1690 1700 1710 1720 WLQEKEAERR KQKQRLTPRP SPSPMIESTP MSIAGDATPL LDEMDR
	Isoform 2 [UniParc]. Checksum: 4BD128B2327CECE4	FASTA	545	61,301
	10 20 30 40 50 60 MPSRGTRPED SSVLIPTDNS TPHKEDLSSK VWNHFDSGSC PGQAIGVKTR LDNGVTGFIP 70 80 90 100 110 120 TKFLSDKVVK RPEERVKVGM TVHCRIMKID IEKFSADLTC RTSDLMDRNN EWKLPKDTYY 130 140 150 160 170 180 DFDAEAADHK QEEDMKRKQQ RTTYIKRVIA HPSFHNINFK QAEKMMETMD QGDVIIRPSS 190 200 210 220 230 240 KGENHLTVTW KVSDGIYQHV DVREEGKENA FSLGATLWIN SEEFEDLDEI VARYVQPMAS 250 260 270 280 290 300 FARDLLNHKY YQDCSGGDRK KLEELLIKTK KEKPTFIPYF ICACKELPGK FLLGYQPRGK 310 320 330 340 350 360 PRIEYVTVTP EGFRYRGQIF PTVNGLFRWF KDHYQDPVPG ITPSSSSRTR TPASINATPA 370 380 390 400 410 420 NINLADLTRA VNALPQNMTS QMFSAIAAVT GQGQNPNATP AQWASSQYGY GGSGGGSSAY 430 440 450 460 470 480 HVFPTPAQQP VATPLMTPSY SYTTPSQPIT TPQYHQLQAS TTPQSAQAQP QPSSSSRQRQ 490 500 510 520 530 540 QQPKSNSHAA IDWGKMAEQW LQEKEAERRK QKQRLTPRPS PSPMIESTPM SIAGDATPLL DEMDR
	Isoform 3 [UniParc]. Checksum: BA3499B7CD6743BD	FASTA	726	84,632
	10 20 30 40 50 60 MSDFVESEAE ESEEEYNDEG EVVPRVTKKF VEEEDDDEEE EEENLDDQDE QGNLKGFIND 70 80 90 100 110 120 DDDEDEGEED EGSDSGDSED DVGHKKRKRT SFDDRLEDDD FDLIEENLGV KVKRGQKYRR 130 140 150 160 170 180 VKKMSDDEDD DEEEYGKEEH EKEAIAEEIF QDGEGEEGQE AMEAPMAPPE EEEEDDEESD 190 200 210 220 230 240 IDDFIVDDDG QPLKKPKWRK KLPGYTDAAL QEAQEIFGVD FDYDEFEKYN EYDEELEEEY 250 260 270 280 290 300 EYEDDEAEGE IRVRPKKTTK KRVSRRSIFE MYEPSELESS HLTDQDNEIR ATDLPERFQL 310 320 330 340 350 360 RSIPVKGAED DELEEEADWI YRNAFATPTI SLQESCDYLD RGQPASSFSR KGPSTIQKIK 370 380 390 400 410 420 EALGFMRNQH FEVPFIAFYR KEYVEPELHI NDLWRVWQWD EKWTQLRIRK ENLTRLFEKM 430 440 450 460 470 480 QAYQYEQISA DPDKPLADGI RALDTTDMER LKDVQSMDEL KDVYNHFLLY YGRDIPKMQN 490 500 510 520 530 540 AAKASRKKLK RVREEGDEEG EGDEAEDEEQ RGPELKQASR RDMYTICQSA GLDGLAKKFG 550 560 570 580 590 600 LTPEQFGENL RDSYQRHETE QFPAEPLELA KDYVCSQFPT PEAVLEGARY MVALQIAREP 610 620 630 640 650 660 LVRQVLRQTF QERAKLMTPS YSYTTPSQPI TTPQYHQLQA STTPQSAQAQ PQPSSSSRQR 670 680 690 700 710 720 QQQPKSNSHA AIDWGKMAEQ WLQEKEAERR KQKQRLTPRP SPSPMIESTP MSIAGDATPL LDEMDR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and analysis of the human and murine putative chromatin structure regulator SUPT6H and Supt6h." Chiang P.-W., Wang S., Smithivas P., Song W.-J., Ramamoorthy S., Hillman J., Puett S., Van Keuren M.L., Crombez E., Kumar A., Glover T.W., Miller D.E., Tsai C.-H., Blackburn C.C., Chen X.-N., Sun Z., Cheng J.-F., Korenberg J.R., Kurnit D.M. Genomics 34:328-333(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N. DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Bone marrow.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] (ISOFORMS 1; 2 AND 3). Tissue: Cervix, Lung, Melanoma, Placenta and Testis.
[5]	Yu W., Gibbs R.A. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1460-1726 (ISOFORMS 1/2). Tissue: Brain.
[6]	"Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation." Wu-Baer F., Lane W.S., Gaynor R.B. J. Mol. Biol. 277:179-197(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Human Spt6 stimulates transcription elongation by RNA polymerase II in vitro." Endoh M., Zhu W., Hasegawa J., Watanabe H., Kim D.-K., Aida M., Inukai N., Narita T., Yamada T., Furuya A., Sato H., Yamaguchi Y., Mandal S.S., Reinberg D., Wada T., Handa H. Mol. Cell. Biol. 24:3324-3336(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH THE DSIF COMPLEX AND RNA POLYMERASE II.
[8]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1535; THR-1539 AND THR-1718, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; THR-1523; SER-1535; THR-1539; SER-1701; SER-1703 AND THR-1718, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-73; SER-75; SER-78; THR-1532; SER-1535; THR-1539; THR-1697; SER-1701; SER-1703 AND THR-1718, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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-743 AND LYS-1676, MASS SPECTROMETRY.
[13]	"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-125; THR-1523; THR-1532; THR-1697; SER-1701; SER-1703 AND THR-1718, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-12; SER-125 AND SER-1535, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[16]	"The cellular protein SPT6 is required for efficient replication of human cytomegalovirus." Cygnar D., Hagemeier S., Kronemann D., Bresnahan W.A. J. Virol. 86:2011-2020(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HHV-5 PROTEIN UL69.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U38623 mRNA. Translation: AAC99996.1. U38658 mRNA. Translation: AAB18949.1. Frameshift. U46691 mRNA. Translation: AAC50821.1. Different initiation. D79984 mRNA. Translation: BAA11479.2. Different initiation. CH471159 Genomic DNA. Translation: EAW51117.1. BC003692 mRNA. Translation: AAH03692.1. BC003696 mRNA. Translation: AAH03696.1. BC017105 mRNA. Translation: AAH17105.1. BC033074 mRNA. Translation: AAH33074.1. Different initiation. BC073963 mRNA. Translation: AAH73963.1. BC136522 mRNA. Translation: AAI36523.1. BC136524 mRNA. Translation: AAI36525.1. BC150268 mRNA. Translation: AAI50269.1. AF070532 mRNA. Translation: AAC28631.1.
IPI	IPI00430770. IPI00456683. IPI00784161.
RefSeq	NP_003161.2. NM_003170.3.
UniGene	Hs.250429.
3D structure databases
ProteinModelPortal	Q7KZ85.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42615N.
IntAct	Q7KZ85. 7 interactions.
MINT	MINT-1491202.
PTM databases
PhosphoSite	Q7KZ85.
Polymorphism databases
DMDM	51701986.
Proteomic databases
PaxDb	Q7KZ85.
PeptideAtlas	Q7KZ85.
PRIDE	Q7KZ85.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000314616; ENSP00000319104; ENSG00000109111. ENST00000347486; ENSP00000338143; ENSG00000109111.
GeneID	6830.
KEGG	hsa:6830.
UCSC	uc002hby.3. human.
Organism-specific databases
CTD	6830.
GeneCards	GC17P026989.
HGNC	HGNC:11470. SUPT6H.
HPA	CAB012416.
MIM	601333. gene.
neXtProt	NX_Q7KZ85.
PharmGKB	PA36256.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2183.
HOVERGEN	HBG093994.
InParanoid	Q7KZ85.
KO	K11292.
OMA	EADWIYR.
Gene expression databases
Bgee	Q7KZ85.
Genevestigator	Q7KZ85.
GermOnline	ENSG00000109111. Homo sapiens.
Family and domain databases
Gene3D	1.10.150.310. 1 hit. 1.10.3500.10. 2 hits. 2.40.50.140. 1 hit. 3.30.420.140. 1 hit. 3.30.505.10. 1 hit.
InterPro	IPR012340. NA-bd_OB-fold. IPR003029. Rbsml_prot_S1_RNA-bd_dom. IPR022967. RNA-binding_domain_S1. IPR000980. SH2. IPR023323. Tex-like_dom. IPR023097. Tex_RuvX-like_dom. IPR017072. TF_Spt6. IPR006641. YqgF/RNaseH-like_dom. [Graphical view]
PANTHER	PTHR10145. PTHR10145. 1 hit.
Pfam	PF00575. S1. 1 hit. PF00017. SH2. 1 hit. [Graphical view]
PIRSF	PIRSF036947. Spt6. 1 hit.
SMART	SM00316. S1. 1 hit. SM00252. SH2. 1 hit. SM00732. YqgFc. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
PROSITE	PS50126. S1. 1 hit. PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SUPT6H. human.
GenomeRNAi	6830.
NextBio	26667.
PMAP-CutDB	Q7KZ85.
SOURCE	Search...

Entry information

Entry name

SPT6H_HUMAN

Accession

Primary (citable) accession number: Q7KZ85
Secondary accession number(s): A7E2B4 , Q15737, Q6GMQ4, Q7KYW9, Q7LDK4, Q8N526, Q92775, Q96AH3, Q9BTH9, Q9BTI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	August 31, 2004
Last modified:	May 1, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.