Q96T23 (RSF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Remodeling and spacing factor 1
Short name=Rsf-1

Alternative name(s):
HBV pX-associated protein 8
Hepatitis B virus X-associated protein
p325 subunit of RSF chromatin-remodeling complex

Gene names

Name:	RSF1
Synonyms:	HBXAP, XAP8

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	1441 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for assembly of regular nucleosome arrays by the RSF chromatin-remodeling complex. Facilitates transcription of hepatitis B virus (HBV) genes by the pX transcription activator. In case of infection by HBV, together with pX, it represses TNF-alpha induced NF-kappa-B transcription activation. Represses transcription when artificially recruited to chromatin by fusion to a heterogeneous DNA binding domain. Ref.2 Ref.7
Subunit structure	Interacts with SMARCA5/SNF2H to form the RSF complex. Also binds the HBV pX/HBx protein, which is required to activate transcription of the viral genome. Ref.1 Ref.2
Subcellular location	Nucleus Ref.1 Ref.2.
Tissue specificity	Ubiquitously expressed.
Sequence similarities	Contains 1 DDT domain. Contains 1 PHD-type zinc finger.
Sequence caution	The sequence AAG43114.1 differs from that shown. Reason: Frameshift at position 549. The sequence AAH46124.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAK57515.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA91591.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CENP-A containing nucleosome assembly at centromere Traceable author statement. Source: Reactome DNA-dependent transcription, initiation Inferred from direct assay PubMed 9836642. Source: UniProtKB negative regulation of DNA binding Inferred from direct assay Ref.7. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.1. Source: UniProtKB nucleosome positioning Inferred from direct assay PubMed 9836642. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.2. Source: UniProtKB positive regulation of viral transcription Inferred from direct assay Ref.2. Source: UniProtKB
Cellular_component	RSF complex Inferred from physical interaction PubMed 9836642. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	histone binding Inferred from direct assay Ref.7. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMARCA5	O60264	5	EBI-926768,EBI-352588

Alternative products

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

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q96T23-1)

Also known as: Alpha; XAP8alpha;

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: Q96T23-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     93-123: Missing.

Isoform 3 (identifier: Q96T23-3)

Also known as: Gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     1-252: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1441	1441	Remodeling and spacing factor 1		PRO_0000059326
Regions
	Domain	17 – 84	68	DDT
	Zinc finger	891 – 941	51	PHD-type
	Coiled coil	942 – 1012	71	Potential
	Compositional bias	226 – 372	147	Glu-rich
	Compositional bias	875 – 884	10	Poly-Glu
	Compositional bias	1080 – 1083	4	Poly-Ala
	Compositional bias	1146 – 1243	98	Arg-rich
	Compositional bias	1286 – 1292	7	Poly-Glu
	Compositional bias	1419 – 1424	6	Poly-Glu
Amino acid modifications
	Modified residue	227	1	Phosphoserine Ref.14 Ref.15
	Modified residue	397	1	Phosphoserine Ref.8 Ref.14 Ref.15
	Modified residue	473	1	Phosphoserine Ref.14
	Modified residue	524	1	Phosphoserine Ref.10
	Modified residue	604	1	Phosphoserine Ref.8 Ref.14 Ref.15
	Modified residue	622	1	Phosphoserine Ref.8 Ref.11
	Modified residue	629	1	Phosphoserine Ref.11
	Modified residue	748	1	Phosphoserine Ref.14 Ref.15
	Modified residue	778	1	Phosphoserine Ref.8
	Modified residue	882	1	Phosphoserine Ref.14
	Modified residue	1050	1	N6-acetyllysine Ref.13
	Modified residue	1096	1	Phosphoserine Ref.8
	Modified residue	1098	1	Phosphoserine Ref.8
	Modified residue	1105	1	Phosphoserine Ref.8
	Modified residue	1221	1	Phosphoserine Ref.11 Ref.15
	Modified residue	1223	1	Phosphoserine Ref.11
	Modified residue	1226	1	Phosphoserine Ref.11 Ref.15
	Modified residue	1258	1	Phosphoserine Ref.15
	Modified residue	1277	1	Phosphoserine Ref.11
	Modified residue	1278	1	Phosphothreonine Ref.11
	Modified residue	1305	1	Phosphothreonine Ref.11 Ref.12 Ref.15
	Modified residue	1310	1	Phosphoserine Ref.12
	Modified residue	1325	1	Phosphoserine Ref.10
	Modified residue	1339	1	N6-acetyllysine Ref.13
	Modified residue	1345	1	Phosphoserine Ref.8 Ref.9 Ref.12 Ref.14 Ref.15
	Modified residue	1359	1	Phosphoserine Ref.8 Ref.11 Ref.12 Ref.14
	Modified residue	1375	1	Phosphoserine Ref.8 Ref.12 Ref.14 Ref.15
Natural variations
	Alternative sequence	1 – 252	252	Missing in isoform 3.		VSP_012499
	Alternative sequence	93 – 123	31	Missing in isoform 2.		VSP_012500
	Natural variant	304	1	E → D. Corresponds to variant rs58758035 [ dbSNP | Ensembl ].		VAR_061741
	Natural variant	475	1	S → P. Corresponds to variant rs7950873 [ dbSNP | Ensembl ].		VAR_020885
Experimental info
	Sequence conflict	132	1	D → G in AAG43114. Ref.4
	Sequence conflict	270	1	V → G in AAG43114. Ref.4
	Sequence conflict	276	1	V → G in AAG43114. Ref.4
	Sequence conflict	287	1	V → A in AAG43114. Ref.4
	Sequence conflict	291	1	V → G in AAG43114. Ref.4
	Sequence conflict	305	1	K → N in AAG43114. Ref.4
	Sequence conflict	314 – 315	2	SF → PS in AAG43114. Ref.4
	Sequence conflict	353	1	F → L in AAG43114. Ref.4
	Sequence conflict	381	1	K → E in AAG43114. Ref.4
	Sequence conflict	1063	1	I → V in BAA91591. Ref.6
	Sequence conflict	1137	1	D → E in AAK57515. Ref.1
	Sequence conflict	1137	1	D → E in AAF61709. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) (XAP8alpha) [UniParc]. Last modified July 7, 2009. Version 2. Checksum: 0FCB9499B5097A2F	FASTA	1,441	163,821
	10 20 30 40 50 60 MATAAAAAAV MAPPGCPGSC PNFAVVCSFL ERYGPLLDLP ELPFPELERV LQAPPPDVGN 70 80 90 100 110 120 GEVPKELVEL HLKLMRKIGK SVTADRWEKY LIKICQEFNS TWAWEMEKKG YLEMSVECKL 130 140 150 160 170 180 ALLKYLCECQ FDDNLKFKNI INEEDADTMR LQPIGRDKDG LMYWYQLDQD HNVRMYIEEQ 190 200 210 220 230 240 DDQDGSSWKC IVRNRNELAE TLALLKAQID PVLLKNSSQQ DNSSRESPSL EDEETKKEEE 250 260 270 280 290 300 TPKQEEQKES EKMKSEEQPM DLENRSTANV LEETTVKKEK EDEKELVKLP VIVKLEKPLP 310 320 330 340 350 360 ENEEKKIIKE ESDSFKENVK PIKVEVKECR ADPKDTKSSM EKPVAQEPER IEFGGNIKSS 370 380 390 400 410 420 HEITEKSTEE TEKLKNDQQA KIPLKKREIK LSDDFDSPVK GPLCKSVTPT KEFLKDEIKQ 430 440 450 460 470 480 EEETCKRIST ITALGHEGKQ LVNGEVSDER VAPNFKTEPI ETKFYETKEE SYSPSKDRNI 490 500 510 520 530 540 ITEGNGTESL NSVITSMKTG ELEKETAPLR KDADSSISVL EIHSQKAQIE EPDPPEMETS 550 560 570 580 590 600 LDSSEMAKDL SSKTALSSTE SCTMKGEEKS PKTKKDKRPP ILECLEKLEK SKKTFLDKDA 610 620 630 640 650 660 QRLSPIPEEV PKSTLESEKP GSPEAAETSP PSNIIDHCEK LASEKEVVEC QSTSTVGGQS 670 680 690 700 710 720 VKKVDLETLK EDSEFTKVEM DNLDNAQTSG IEEPSETKGS MQKSKFKYKL VPEEETTASE 730 740 750 760 770 780 NTEITSERQK EGIKLTIRIS SRKKKPDSPP KVLEPENKQE KTEKEEEKTN VGRTLRRSPR 790 800 810 820 830 840 ISRPTAKVAE IRDQKADKKR GEGEDEVEEE STALQKTDKK EILKKSEKDT NSKVSKVKPK 850 860 870 880 890 900 GKVRWTGSRT RGRWKYSSND ESEGSGSEKS SAASEEEEEK ESEEAILADD DEPCKKCGLP 910 920 930 940 950 960 NHPELILLCD SCDSGYHTAC LRPPLMIIPD GEWFCPPCQH KLLCEKLEEQ LQDLDVALKK 970 980 990 1000 1010 1020 KERAERRKER LVYVGISIEN IIPPQEPDFS EDQEEKKKDS KKSKANLLER RSTRTRKCIS 1030 1040 1050 1060 1070 1080 YRFDEFDEAI DEAIEDDIKE ADGGGVGRGK DISTITGHRG KDISTILDEE RKENKRPQRA 1090 1100 1110 1120 1130 1140 AAARRKKRRR LNDLDSDSNL DEEESEDEFK ISDGSQDEFV VSDENPDESE EDPPSNDDSD 1150 1160 1170 1180 1190 1200 TDFCSRRLRR HPSRPMRQSR RLRRKTPKKK YSDDDEEEES EENSRDSESD FSDDFSDDFV 1210 1220 1230 1240 1250 1260 ETRRRRSRRN QKRQINYKED SESDGSQKSL RRGKEIRRVH KRRLSSSESE ESYLSKNSED 1270 1280 1290 1300 1310 1320 DELAKESKRS VRKRGRSTDE YSEADEEEEE EEGKPSRKRL HRIETDEEES CDNAHGDANQ 1330 1340 1350 1360 1370 1380 PARDSQPRVL PSEQESTKKP YRIESDEEED FENVGKVGSP LDYSLVDLPS TNGQSPGKAI 1390 1400 1410 1420 1430 1440 ENLIGKPTEK SQTPKDNSTA SASLASNGTS GGQEAGAPEE EEDELLRVTD LVDYVCNSEQ L
	Isoform 2 (Beta) [UniParc]. Checksum: 0C5AF21D8B1642C4	FASTA	1,410	160,129
	10 20 30 40 50 60 MATAAAAAAV MAPPGCPGSC PNFAVVCSFL ERYGPLLDLP ELPFPELERV LQAPPPDVGN 70 80 90 100 110 120 GEVPKELVEL HLKLMRKIGK SVTADRWEKY LIKYLCECQF DDNLKFKNII NEEDADTMRL 130 140 150 160 170 180 QPIGRDKDGL MYWYQLDQDH NVRMYIEEQD DQDGSSWKCI VRNRNELAET LALLKAQIDP 190 200 210 220 230 240 VLLKNSSQQD NSSRESPSLE DEETKKEEET PKQEEQKESE KMKSEEQPMD LENRSTANVL 250 260 270 280 290 300 EETTVKKEKE DEKELVKLPV IVKLEKPLPE NEEKKIIKEE SDSFKENVKP IKVEVKECRA 310 320 330 340 350 360 DPKDTKSSME KPVAQEPERI EFGGNIKSSH EITEKSTEET EKLKNDQQAK IPLKKREIKL 370 380 390 400 410 420 SDDFDSPVKG PLCKSVTPTK EFLKDEIKQE EETCKRISTI TALGHEGKQL VNGEVSDERV 430 440 450 460 470 480 APNFKTEPIE TKFYETKEES YSPSKDRNII TEGNGTESLN SVITSMKTGE LEKETAPLRK 490 500 510 520 530 540 DADSSISVLE IHSQKAQIEE PDPPEMETSL DSSEMAKDLS SKTALSSTES CTMKGEEKSP 550 560 570 580 590 600 KTKKDKRPPI LECLEKLEKS KKTFLDKDAQ RLSPIPEEVP KSTLESEKPG SPEAAETSPP 610 620 630 640 650 660 SNIIDHCEKL ASEKEVVECQ STSTVGGQSV KKVDLETLKE DSEFTKVEMD NLDNAQTSGI 670 680 690 700 710 720 EEPSETKGSM QKSKFKYKLV PEEETTASEN TEITSERQKE GIKLTIRISS RKKKPDSPPK 730 740 750 760 770 780 VLEPENKQEK TEKEEEKTNV GRTLRRSPRI SRPTAKVAEI RDQKADKKRG EGEDEVEEES 790 800 810 820 830 840 TALQKTDKKE ILKKSEKDTN SKVSKVKPKG KVRWTGSRTR GRWKYSSNDE SEGSGSEKSS 850 860 870 880 890 900 AASEEEEEKE SEEAILADDD EPCKKCGLPN HPELILLCDS CDSGYHTACL RPPLMIIPDG 910 920 930 940 950 960 EWFCPPCQHK LLCEKLEEQL QDLDVALKKK ERAERRKERL VYVGISIENI IPPQEPDFSE 970 980 990 1000 1010 1020 DQEEKKKDSK KSKANLLERR STRTRKCISY RFDEFDEAID EAIEDDIKEA DGGGVGRGKD 1030 1040 1050 1060 1070 1080 ISTITGHRGK DISTILDEER KENKRPQRAA AARRKKRRRL NDLDSDSNLD EEESEDEFKI 1090 1100 1110 1120 1130 1140 SDGSQDEFVV SDENPDESEE DPPSNDDSDT DFCSRRLRRH PSRPMRQSRR LRRKTPKKKY 1150 1160 1170 1180 1190 1200 SDDDEEEESE ENSRDSESDF SDDFSDDFVE TRRRRSRRNQ KRQINYKEDS ESDGSQKSLR 1210 1220 1230 1240 1250 1260 RGKEIRRVHK RRLSSSESEE SYLSKNSEDD ELAKESKRSV RKRGRSTDEY SEADEEEEEE 1270 1280 1290 1300 1310 1320 EGKPSRKRLH RIETDEEESC DNAHGDANQP ARDSQPRVLP SEQESTKKPY RIESDEEEDF 1330 1340 1350 1360 1370 1380 ENVGKVGSPL DYSLVDLPST NGQSPGKAIE NLIGKPTEKS QTPKDNSTAS ASLASNGTSG 1390 1400 1410 GQEAGAPEEE EDELLRVTDL VDYVCNSEQL
	Isoform 3 (Gamma) [UniParc]. Checksum: F5652F52FD1CFEF0	FASTA	1,189	134,946
	10 20 30 40 50 60 MKSEEQPMDL ENRSTANVLE ETTVKKEKED EKELVKLPVI VKLEKPLPEN EEKKIIKEES 70 80 90 100 110 120 DSFKENVKPI KVEVKECRAD PKDTKSSMEK PVAQEPERIE FGGNIKSSHE ITEKSTEETE 130 140 150 160 170 180 KLKNDQQAKI PLKKREIKLS DDFDSPVKGP LCKSVTPTKE FLKDEIKQEE ETCKRISTIT 190 200 210 220 230 240 ALGHEGKQLV NGEVSDERVA PNFKTEPIET KFYETKEESY SPSKDRNIIT EGNGTESLNS 250 260 270 280 290 300 VITSMKTGEL EKETAPLRKD ADSSISVLEI HSQKAQIEEP DPPEMETSLD SSEMAKDLSS 310 320 330 340 350 360 KTALSSTESC TMKGEEKSPK TKKDKRPPIL ECLEKLEKSK KTFLDKDAQR LSPIPEEVPK 370 380 390 400 410 420 STLESEKPGS PEAAETSPPS NIIDHCEKLA SEKEVVECQS TSTVGGQSVK KVDLETLKED 430 440 450 460 470 480 SEFTKVEMDN LDNAQTSGIE EPSETKGSMQ KSKFKYKLVP EEETTASENT EITSERQKEG 490 500 510 520 530 540 IKLTIRISSR KKKPDSPPKV LEPENKQEKT EKEEEKTNVG RTLRRSPRIS RPTAKVAEIR 550 560 570 580 590 600 DQKADKKRGE GEDEVEEEST ALQKTDKKEI LKKSEKDTNS KVSKVKPKGK VRWTGSRTRG 610 620 630 640 650 660 RWKYSSNDES EGSGSEKSSA ASEEEEEKES EEAILADDDE PCKKCGLPNH PELILLCDSC 670 680 690 700 710 720 DSGYHTACLR PPLMIIPDGE WFCPPCQHKL LCEKLEEQLQ DLDVALKKKE RAERRKERLV 730 740 750 760 770 780 YVGISIENII PPQEPDFSED QEEKKKDSKK SKANLLERRS TRTRKCISYR FDEFDEAIDE 790 800 810 820 830 840 AIEDDIKEAD GGGVGRGKDI STITGHRGKD ISTILDEERK ENKRPQRAAA ARRKKRRRLN 850 860 870 880 890 900 DLDSDSNLDE EESEDEFKIS DGSQDEFVVS DENPDESEED PPSNDDSDTD FCSRRLRRHP 910 920 930 940 950 960 SRPMRQSRRL RRKTPKKKYS DDDEEEESEE NSRDSESDFS DDFSDDFVET RRRRSRRNQK 970 980 990 1000 1010 1020 RQINYKEDSE SDGSQKSLRR GKEIRRVHKR RLSSSESEES YLSKNSEDDE LAKESKRSVR 1030 1040 1050 1060 1070 1080 KRGRSTDEYS EADEEEEEEE GKPSRKRLHR IETDEEESCD NAHGDANQPA RDSQPRVLPS 1090 1100 1110 1120 1130 1140 EQESTKKPYR IESDEEEDFE NVGKVGSPLD YSLVDLPSTN GQSPGKAIEN LIGKPTEKSQ 1150 1160 1170 1180 TPKDNSTASA SLASNGTSGG QEAGAPEEEE DELLRVTDLV DYVCNSEQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"HBXAP, a novel PHD-finger protein, possesses transcription repression activity." Shamay M., Barak O., Shaul Y. Genomics 79:523-529(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 4-1441 (ISOFORMS 1 AND 2), INTERACTION WITH PX OF HBV, SUBCELLULAR LOCATION.
[2]	"Hepatitis B virus pX interacts with HBXAP, a PHD finger protein to coactivate transcription." Shamay M., Barak O., Doitsh G., Ben-Dor I., Shaul Y. J. Biol. Chem. 277:9982-9988(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH PX OF HBV, SUBCELLULAR LOCATION, FUNCTION. Tissue: Spleen.
[3]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mao Y.M., Xie Y., Zheng Z.H. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 111-703. Tissue: Brain.
[5]	"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] OF 200-1002. Tissue: Lymph.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 494-1068.
[7]	"Functional analysis of the subunits of the chromatin assembly factor RSF." Loyola A., Huang J.-Y., LeRoy G., Hu S., Wang Y.-H., Donnelly R.J., Lane W.S., Lee S.-C., Reinberg D. Mol. Cell. Biol. 23:6759-6768(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[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-397; SER-604; SER-622; SER-778; SER-1096; SER-1098; SER-1105; SER-1345; SER-1359 AND SER-1375, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1345, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524 AND SER-1325, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"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-622; SER-629; SER-1221; SER-1223; SER-1226; SER-1277; THR-1278; THR-1305 AND SER-1359, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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 THR-1305; SER-1310; SER-1345; SER-1359 AND SER-1375, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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-1050 AND LYS-1339, MASS SPECTROMETRY.
[14]	"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-227; SER-397; SER-473; SER-604; SER-748; SER-882; SER-1345; SER-1359 AND SER-1375, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-397; SER-604; SER-748; SER-1221; SER-1226; SER-1258; THR-1305; SER-1345 AND SER-1375, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF380176 mRNA. Translation: AAK57515.1. Different initiation. AF227948 mRNA. Translation: AAF61709.2. AP000580 Genomic DNA. No translation available. AP000609 Genomic DNA. No translation available. AP002343 Genomic DNA. No translation available. AF059317 mRNA. Translation: AAG43114.1. Sequence problems. BC046124 mRNA. Translation: AAH46124.2. Sequence problems. AK001268 mRNA. Translation: BAA91591.1. Different initiation.
IPI	IPI00290652. IPI00514411. IPI00982445.
RefSeq	NP_057662.3. NM_016578.3.
UniGene	Hs.420229.
3D structure databases
ProteinModelPortal	Q96T23.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96T23. 6 interactions.
STRING	9606.ENSP00000311513.
PTM databases
PhosphoSite	Q96T23.
Polymorphism databases
DMDM	251757329.
Proteomic databases
PaxDb	Q96T23.
PRIDE	Q96T23.
Protocols and materials databases
DNASU	51773.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000308488; ENSP00000311513; ENSG00000048649. ENST00000360355; ENSP00000353511; ENSG00000048649. ENST00000480887; ENSP00000434509; ENSG00000048649.
GeneID	51773.
KEGG	hsa:51773.
UCSC	uc001oym.3. human.
Organism-specific databases
CTD	51773.
GeneCards	GC11M077371.
H-InvDB	HIX0022742.
HGNC	HGNC:18118. RSF1.
HPA	CAB022626.
MIM	608522. gene.
neXtProt	NX_Q96T23.
PharmGKB	PA29210.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG79337.
HOGENOM	HOG000154205.
HOVERGEN	HBG105728.
InParanoid	Q96T23.
KO	K11657.
OMA	QPRVLPS.
OrthoDB	EOG441QBQ.
PhylomeDB	Q96T23.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle.
Gene expression databases
ArrayExpress	Q96T23.
Bgee	Q96T23.
CleanEx	HS_RSF1.
Genevestigator	Q96T23.
GermOnline	ENSG00000048649. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF00628. PHD. 1 hit. [Graphical view]
SMART	SM00249. PHD. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS50827. DDT. False negative. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RSF1. human.
GenomeRNAi	51773.
NextBio	55899.
SOURCE	Search...

Entry information

Entry name

RSF1_HUMAN

Accession

Primary (citable) accession number: Q96T23
Secondary accession number(s): Q86X86 , Q9H3L8, Q9NVZ8, Q9NYU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	July 7, 2009
Last modified:	May 1, 2013
This is version 107 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.