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Q96T23 (RSF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1441 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCENP-A containing nucleosome assembly at centromere

Traceable author statement. Source: Reactome

DNA-templated transcription, initiation

Inferred from direct assay PubMed 9836642. Source: UniProtKB

chromatin remodeling

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-templated

Inferred from direct assay Ref.1. Source: UniProtKB

nucleosome assembly

Inferred from direct assay Ref.7. Source: UniProtKB

nucleosome positioning

Inferred from direct assay PubMed 9836642. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of viral transcription

Inferred from direct assay Ref.2. Source: UniProtKB

   Cellular_componentRSF complex

Inferred from physical interaction PubMed 9836642. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.2Ref.7. Source: UniProtKB

   Molecular_functionhistone 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

SMARCA5O602645EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14411441Remodeling and spacing factor 1
PRO_0000059326

Regions

Domain17 – 8468DDT
Zinc finger891 – 94151PHD-type
Coiled coil942 – 101271 Potential
Compositional bias226 – 372147Glu-rich
Compositional bias875 – 88410Poly-Glu
Compositional bias1080 – 10834Poly-Ala
Compositional bias1146 – 124398Arg-rich
Compositional bias1286 – 12927Poly-Glu
Compositional bias1419 – 14246Poly-Glu

Amino acid modifications

Modified residue2271Phosphoserine Ref.15 Ref.16
Modified residue3971Phosphoserine Ref.8 Ref.15 Ref.16
Modified residue4731Phosphoserine Ref.15
Modified residue5241Phosphoserine Ref.10
Modified residue6041Phosphoserine Ref.8 Ref.15 Ref.16
Modified residue6221Phosphoserine Ref.8 Ref.11
Modified residue6291Phosphoserine Ref.11
Modified residue7481Phosphoserine Ref.15 Ref.16
Modified residue8821Phosphoserine Ref.15
Modified residue10501N6-acetyllysine Ref.14
Modified residue10961Phosphoserine Ref.8
Modified residue10981Phosphoserine Ref.8
Modified residue11051Phosphoserine Ref.8
Modified residue12211Phosphoserine Ref.11 Ref.16
Modified residue12231Phosphoserine Ref.11
Modified residue12261Phosphoserine Ref.11 Ref.16
Modified residue12581Phosphoserine Ref.16
Modified residue12771Phosphoserine Ref.11
Modified residue12781Phosphothreonine Ref.11
Modified residue13051Phosphothreonine Ref.11 Ref.13 Ref.16
Modified residue13101Phosphoserine Ref.13
Modified residue13251Phosphoserine Ref.10
Modified residue13391N6-acetyllysine Ref.14
Modified residue13451Phosphoserine Ref.8 Ref.9 Ref.13 Ref.15 Ref.16
Modified residue13591Phosphoserine Ref.8 Ref.11 Ref.13 Ref.15
Modified residue13751Phosphoserine Ref.8 Ref.13 Ref.15 Ref.16

Natural variations

Alternative sequence1 – 252252Missing in isoform 3.
VSP_012499
Alternative sequence93 – 12331Missing in isoform 2.
VSP_012500
Natural variant3041E → D.
Corresponds to variant rs58758035 [ dbSNP | Ensembl ].
VAR_061741
Natural variant4751S → P.
Corresponds to variant rs7950873 [ dbSNP | Ensembl ].
VAR_020885

Experimental info

Sequence conflict1321D → G in AAG43114. Ref.4
Sequence conflict2701V → G in AAG43114. Ref.4
Sequence conflict2761V → G in AAG43114. Ref.4
Sequence conflict2871V → A in AAG43114. Ref.4
Sequence conflict2911V → G in AAG43114. Ref.4
Sequence conflict3051K → N in AAG43114. Ref.4
Sequence conflict314 – 3152SF → PS in AAG43114. Ref.4
Sequence conflict3531F → L in AAG43114. Ref.4
Sequence conflict3811K → E in AAG43114. Ref.4
Sequence conflict10631I → V in BAA91591. Ref.6
Sequence conflict11371D → E in AAK57515. Ref.1
Sequence conflict11371D → E in AAF61709. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) (XAP8alpha) [UniParc].

Last modified July 7, 2009. Version 2.
Checksum: 0FCB9499B5097A2F

FASTA1,441163,821
        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 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 0C5AF21D8B1642C4
Show »

FASTA1,410160,129
Isoform 3 (Gamma) [UniParc].

Checksum: F5652F52FD1CFEF0
Show »

FASTA1,189134,946

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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-1096; SER-1098; SER-1105; SER-1345; SER-1359 AND SER-1375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, 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: 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 THR-1305; SER-1310; SER-1345; SER-1359 AND SER-1375, 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-1050 AND LYS-1339, 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-227; SER-397; SER-473; SER-604; SER-748; SER-882; SER-1345; SER-1359 AND SER-1375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

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.
RefSeqNP_057662.3. NM_016578.3.
UniGeneHs.420229.
Hs.593415.

3D structure databases

ProteinModelPortalQ96T23.
SMRQ96T23. Positions 906-938.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119724. 13 interactions.
IntActQ96T23. 6 interactions.
MINTMINT-3058575.
STRING9606.ENSP00000311513.

PTM databases

PhosphoSiteQ96T23.

Polymorphism databases

DMDM251757329.

Proteomic databases

PaxDbQ96T23.
PRIDEQ96T23.

Protocols and materials databases

DNASU51773.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308488; ENSP00000311513; ENSG00000048649. [Q96T23-1]
ENST00000360355; ENSP00000353511; ENSG00000048649. [Q96T23-2]
ENST00000480887; ENSP00000434509; ENSG00000048649. [Q96T23-3]
GeneID51773.
KEGGhsa:51773.
UCSCuc001oym.3. human. [Q96T23-1]

Organism-specific databases

CTD51773.
GeneCardsGC11M077371.
H-InvDBHIX0022742.
HGNCHGNC:18118. RSF1.
HPACAB022626.
HPA046129.
MIM608522. gene.
neXtProtNX_Q96T23.
PharmGKBPA29210.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG79337.
HOGENOMHOG000154205.
HOVERGENHBG105728.
InParanoidQ96T23.
KOK11657.
OMAMAPPGCP.
OrthoDBEOG7KDF93.
PhylomeDBQ96T23.
TreeFamTF106405.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ96T23.
BgeeQ96T23.
CleanExHS_RSF1.
GenevestigatorQ96T23.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR028938. Rsf-1.
IPR028942. WHIM1_dom.
IPR028941. WHIM2_dom.
IPR028935. WHIM3_domain.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR10615:SF49. PTHR10615:SF49. 1 hit.
PfamPF00628. PHD. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WHIM2. 1 hit.
PF15614. WHIM3. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRSF1. human.
GeneWikiRSF1.
GenomeRNAi51773.
NextBio55899.
PROQ96T23.
SOURCESearch...

Entry information

Entry nameRSF1_HUMAN
AccessionPrimary (citable) accession number: Q96T23
Secondary accession number(s): Q86X86 expand/collapse secondary AC list , Q9H3L8, Q9NVZ8, Q9NYU0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: July 7, 2009
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

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Human chromosome 11

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