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Q96T23

- RSF1_HUMAN

UniProt

Q96T23 - RSF1_HUMAN

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Protein

Remodeling and spacing factor 1

Gene

RSF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri891 – 94151PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. histone binding Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. CENP-A containing nucleosome assembly Source: Reactome
  2. chromatin remodeling Source: UniProtKB
  3. DNA-templated transcription, initiation Source: UniProtKB
  4. negative regulation of DNA binding Source: UniProtKB
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. nucleosome assembly Source: UniProtKB
  7. nucleosome positioning Source: UniProtKB
  8. positive regulation of transcription, DNA-templated Source: UniProtKB
  9. positive regulation of viral transcription Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.

Names & Taxonomyi

Protein namesi
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 namesi
Name:RSF1
Synonyms:HBXAP, XAP8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:18118. RSF1.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
  3. RSF complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29210.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14411441Remodeling and spacing factor 1PRO_0000059326Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei227 – 2271Phosphoserine2 Publications
Modified residuei397 – 3971Phosphoserine3 Publications
Modified residuei473 – 4731Phosphoserine1 Publication
Modified residuei524 – 5241Phosphoserine1 Publication
Modified residuei604 – 6041Phosphoserine3 Publications
Modified residuei622 – 6221Phosphoserine2 Publications
Modified residuei629 – 6291Phosphoserine1 Publication
Modified residuei748 – 7481Phosphoserine2 Publications
Modified residuei882 – 8821Phosphoserine1 Publication
Modified residuei1050 – 10501N6-acetyllysine1 Publication
Modified residuei1096 – 10961Phosphoserine1 Publication
Modified residuei1098 – 10981Phosphoserine1 Publication
Modified residuei1105 – 11051Phosphoserine1 Publication
Modified residuei1221 – 12211Phosphoserine2 Publications
Modified residuei1223 – 12231Phosphoserine1 Publication
Modified residuei1226 – 12261Phosphoserine2 Publications
Modified residuei1258 – 12581Phosphoserine1 Publication
Modified residuei1277 – 12771Phosphoserine1 Publication
Modified residuei1278 – 12781Phosphothreonine1 Publication
Modified residuei1305 – 13051Phosphothreonine3 Publications
Modified residuei1310 – 13101Phosphoserine1 Publication
Modified residuei1325 – 13251Phosphoserine1 Publication
Modified residuei1339 – 13391N6-acetyllysine1 Publication
Modified residuei1345 – 13451Phosphoserine5 Publications
Modified residuei1359 – 13591Phosphoserine4 Publications
Modified residuei1375 – 13751Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96T23.
PaxDbiQ96T23.
PRIDEiQ96T23.

PTM databases

PhosphoSiteiQ96T23.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiQ96T23.
CleanExiHS_RSF1.
ExpressionAtlasiQ96T23. baseline and differential.
GenevestigatoriQ96T23.

Organism-specific databases

HPAiCAB022626.
HPA046129.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SMARCA5O602645EBI-926768,EBI-352588

Protein-protein interaction databases

BioGridi119724. 14 interactions.
IntActiQ96T23. 6 interactions.
MINTiMINT-3058575.
STRINGi9606.ENSP00000311513.

Structurei

3D structure databases

ProteinModelPortaliQ96T23.
SMRiQ96T23. Positions 906-938.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 8468DDTAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili942 – 101271Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi226 – 372147Glu-richAdd
BLAST
Compositional biasi875 – 88410Poly-Glu
Compositional biasi1080 – 10834Poly-Ala
Compositional biasi1146 – 124398Arg-richAdd
BLAST
Compositional biasi1286 – 12927Poly-Glu
Compositional biasi1419 – 14246Poly-Glu

Sequence similaritiesi

Contains 1 DDT domain.Curated
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri891 – 94151PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG79337.
GeneTreeiENSGT00530000064411.
HOGENOMiHOG000154205.
HOVERGENiHBG105728.
InParanoidiQ96T23.
KOiK11657.
OMAiMAPPGCP.
OrthoDBiEOG7KDF93.
PhylomeDBiQ96T23.
TreeFamiTF106405.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR028938. 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]
PANTHERiPTHR10615:SF2. PTHR10615:SF2. 1 hit.
PfamiPF00628. PHD. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WHIM2. 1 hit.
PF15614. WHIM3. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q96T23-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MATAAAAAAV MAPPGCPGSC PNFAVVCSFL ERYGPLLDLP ELPFPELERV
60 70 80 90 100
LQAPPPDVGN GEVPKELVEL HLKLMRKIGK SVTADRWEKY LIKICQEFNS
110 120 130 140 150
TWAWEMEKKG YLEMSVECKL ALLKYLCECQ FDDNLKFKNI INEEDADTMR
160 170 180 190 200
LQPIGRDKDG LMYWYQLDQD HNVRMYIEEQ DDQDGSSWKC IVRNRNELAE
210 220 230 240 250
TLALLKAQID PVLLKNSSQQ DNSSRESPSL EDEETKKEEE TPKQEEQKES
260 270 280 290 300
EKMKSEEQPM DLENRSTANV LEETTVKKEK EDEKELVKLP VIVKLEKPLP
310 320 330 340 350
ENEEKKIIKE ESDSFKENVK PIKVEVKECR ADPKDTKSSM EKPVAQEPER
360 370 380 390 400
IEFGGNIKSS HEITEKSTEE TEKLKNDQQA KIPLKKREIK LSDDFDSPVK
410 420 430 440 450
GPLCKSVTPT KEFLKDEIKQ EEETCKRIST ITALGHEGKQ LVNGEVSDER
460 470 480 490 500
VAPNFKTEPI ETKFYETKEE SYSPSKDRNI ITEGNGTESL NSVITSMKTG
510 520 530 540 550
ELEKETAPLR KDADSSISVL EIHSQKAQIE EPDPPEMETS LDSSEMAKDL
560 570 580 590 600
SSKTALSSTE SCTMKGEEKS PKTKKDKRPP ILECLEKLEK SKKTFLDKDA
610 620 630 640 650
QRLSPIPEEV PKSTLESEKP GSPEAAETSP PSNIIDHCEK LASEKEVVEC
660 670 680 690 700
QSTSTVGGQS VKKVDLETLK EDSEFTKVEM DNLDNAQTSG IEEPSETKGS
710 720 730 740 750
MQKSKFKYKL VPEEETTASE NTEITSERQK EGIKLTIRIS SRKKKPDSPP
760 770 780 790 800
KVLEPENKQE KTEKEEEKTN VGRTLRRSPR ISRPTAKVAE IRDQKADKKR
810 820 830 840 850
GEGEDEVEEE STALQKTDKK EILKKSEKDT NSKVSKVKPK GKVRWTGSRT
860 870 880 890 900
RGRWKYSSND ESEGSGSEKS SAASEEEEEK ESEEAILADD DEPCKKCGLP
910 920 930 940 950
NHPELILLCD SCDSGYHTAC LRPPLMIIPD GEWFCPPCQH KLLCEKLEEQ
960 970 980 990 1000
LQDLDVALKK KERAERRKER LVYVGISIEN IIPPQEPDFS EDQEEKKKDS
1010 1020 1030 1040 1050
KKSKANLLER RSTRTRKCIS YRFDEFDEAI DEAIEDDIKE ADGGGVGRGK
1060 1070 1080 1090 1100
DISTITGHRG KDISTILDEE RKENKRPQRA AAARRKKRRR LNDLDSDSNL
1110 1120 1130 1140 1150
DEEESEDEFK ISDGSQDEFV VSDENPDESE EDPPSNDDSD TDFCSRRLRR
1160 1170 1180 1190 1200
HPSRPMRQSR RLRRKTPKKK YSDDDEEEES EENSRDSESD FSDDFSDDFV
1210 1220 1230 1240 1250
ETRRRRSRRN QKRQINYKED SESDGSQKSL RRGKEIRRVH KRRLSSSESE
1260 1270 1280 1290 1300
ESYLSKNSED DELAKESKRS VRKRGRSTDE YSEADEEEEE EEGKPSRKRL
1310 1320 1330 1340 1350
HRIETDEEES CDNAHGDANQ PARDSQPRVL PSEQESTKKP YRIESDEEED
1360 1370 1380 1390 1400
FENVGKVGSP LDYSLVDLPS TNGQSPGKAI ENLIGKPTEK SQTPKDNSTA
1410 1420 1430 1440
SASLASNGTS GGQEAGAPEE EEDELLRVTD LVDYVCNSEQ L
Length:1,441
Mass (Da):163,821
Last modified:July 7, 2009 - v2
Checksum:i0FCB9499B5097A2F
GO
Isoform 2 (identifier: Q96T23-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

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

Show »
Length:1,410
Mass (Da):160,129
Checksum:i0C5AF21D8B1642C4
GO
Isoform 3 (identifier: Q96T23-3) [UniParc]FASTAAdd to Basket

Also known as: Gamma

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

Show »
Length:1,189
Mass (Da):134,946
Checksum:iF5652F52FD1CFEF0
GO

Sequence cautioni

The sequence AAH46124.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAG43114.1 differs from that shown. Reason: Frameshift at position 549.
The sequence AAK57515.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAA91591.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321D → G in AAG43114. 1 PublicationCurated
Sequence conflicti270 – 2701V → G in AAG43114. 1 PublicationCurated
Sequence conflicti276 – 2761V → G in AAG43114. 1 PublicationCurated
Sequence conflicti287 – 2871V → A in AAG43114. 1 PublicationCurated
Sequence conflicti291 – 2911V → G in AAG43114. 1 PublicationCurated
Sequence conflicti305 – 3051K → N in AAG43114. 1 PublicationCurated
Sequence conflicti314 – 3152SF → PS in AAG43114. 1 PublicationCurated
Sequence conflicti353 – 3531F → L in AAG43114. 1 PublicationCurated
Sequence conflicti381 – 3811K → E in AAG43114. 1 PublicationCurated
Sequence conflicti1063 – 10631I → V in BAA91591. (PubMed:14702039)Curated
Sequence conflicti1137 – 11371D → E in AAK57515. (PubMed:11944984)Curated
Sequence conflicti1137 – 11371D → E in AAF61709. (PubMed:11788598)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti304 – 3041E → D.
Corresponds to variant rs58758035 [ dbSNP | Ensembl ].
VAR_061741
Natural varianti475 – 4751S → P.
Corresponds to variant rs7950873 [ dbSNP | Ensembl ].
VAR_020885

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 252252Missing in isoform 3. 2 PublicationsVSP_012499Add
BLAST
Alternative sequencei93 – 12331Missing in isoform 2. 1 PublicationVSP_012500Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS8253.1. [Q96T23-1]
RefSeqiNP_057662.3. NM_016578.3. [Q96T23-1]
UniGeneiHs.420229.
Hs.593415.

Genome annotation databases

EnsembliENST00000308488; ENSP00000311513; ENSG00000048649. [Q96T23-1]
ENST00000480887; ENSP00000434509; ENSG00000048649. [Q96T23-3]
GeneIDi51773.
KEGGihsa:51773.
UCSCiuc001oym.3. human. [Q96T23-1]

Polymorphism databases

DMDMi251757329.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS8253.1. [Q96T23-1 ]
RefSeqi NP_057662.3. NM_016578.3. [Q96T23-1 ]
UniGenei Hs.420229.
Hs.593415.

3D structure databases

ProteinModelPortali Q96T23.
SMRi Q96T23. Positions 906-938.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119724. 14 interactions.
IntActi Q96T23. 6 interactions.
MINTi MINT-3058575.
STRINGi 9606.ENSP00000311513.

PTM databases

PhosphoSitei Q96T23.

Polymorphism databases

DMDMi 251757329.

Proteomic databases

MaxQBi Q96T23.
PaxDbi Q96T23.
PRIDEi Q96T23.

Protocols and materials databases

DNASUi 51773.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308488 ; ENSP00000311513 ; ENSG00000048649 . [Q96T23-1 ]
ENST00000480887 ; ENSP00000434509 ; ENSG00000048649 . [Q96T23-3 ]
GeneIDi 51773.
KEGGi hsa:51773.
UCSCi uc001oym.3. human. [Q96T23-1 ]

Organism-specific databases

CTDi 51773.
GeneCardsi GC11M077371.
H-InvDB HIX0022742.
HGNCi HGNC:18118. RSF1.
HPAi CAB022626.
HPA046129.
MIMi 608522. gene.
neXtProti NX_Q96T23.
PharmGKBi PA29210.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG79337.
GeneTreei ENSGT00530000064411.
HOGENOMi HOG000154205.
HOVERGENi HBG105728.
InParanoidi Q96T23.
KOi K11657.
OMAi MAPPGCP.
OrthoDBi EOG7KDF93.
PhylomeDBi Q96T23.
TreeFami TF106405.

Enzyme and pathway databases

Reactomei REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.

Miscellaneous databases

ChiTaRSi RSF1. human.
GeneWikii RSF1.
GenomeRNAii 51773.
NextBioi 55899.
PROi Q96T23.
SOURCEi Search...

Gene expression databases

Bgeei Q96T23.
CleanExi HS_RSF1.
ExpressionAtlasi Q96T23. baseline and differential.
Genevestigatori Q96T23.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR028938. 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 ]
PANTHERi PTHR10615:SF2. PTHR10615:SF2. 1 hit.
Pfami PF00628. PHD. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WHIM2. 1 hit.
PF15614. WHIM3. 1 hit.
[Graphical view ]
SMARTi SM00249. PHD. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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-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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524 AND SER-1325, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. 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].

Entry informationi

Entry nameiRSF1_HUMAN
AccessioniPrimary (citable) accession number: Q96T23
Secondary accession number(s): Q86X86
, Q9H3L8, Q9NVZ8, Q9NYU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: July 7, 2009
Last modified: October 29, 2014
This is version 122 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3