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Protein

Protein SCAF8

Gene

SCAF8

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

Functioni

May play a role in mRNA processing.1 Publication

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • RNA binding Source: UniProtKB-KW
  • RNA polymerase core enzyme binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SCAF8
Alternative name(s):
CDC5L complex-associated protein 7
RNA-binding motif protein 16
SR-related and CTD-associated factor 8
Gene namesi
Name:SCAF8
Synonyms:CCAP7, KIAA1116, RBM16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:20959. SCAF8.

Subcellular locationi

  • Nucleus
  • Nucleus matrix

  • Note: Detected in granular nuclear foci which correspond to sites of active transcription.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394587.

Polymorphism and mutation databases

BioMutaiSCAF8.
DMDMi30580495.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12711271Protein SCAF8PRO_0000081780Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61Phosphothreonine1 Publication
Cross-linki18 – 18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Modified residuei615 – 6151PhosphothreonineCombined sources
Modified residuei617 – 6171PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UPN6.
MaxQBiQ9UPN6.
PaxDbiQ9UPN6.
PRIDEiQ9UPN6.

PTM databases

iPTMnetiQ9UPN6.
PhosphoSiteiQ9UPN6.

Expressioni

Gene expression databases

BgeeiQ9UPN6.
CleanExiHS_RBM16.
ExpressionAtlasiQ9UPN6. baseline and differential.
GenevisibleiQ9UPN6. HS.

Organism-specific databases

HPAiHPA035601.
HPA035602.

Interactioni

Subunit structurei

Interacts with POLR2A (via C-terminus). Has much higher affinity for phosphorylated POLR2A. Identified in a complex with CDC5L and other spliceosomal proteins. May associate with the spliceosome.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GOLGA2Q083793EBI-7954236,EBI-618309

GO - Molecular functioni

  • RNA polymerase core enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116503. 20 interactions.
IntActiQ9UPN6. 8 interactions.
MINTiMINT-6945747.
STRINGi9606.ENSP00000356146.

Structurei

Secondary structure

1
1271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Helixi13 – 164Combined sources
Helixi23 – 3513Combined sources
Helixi37 – 393Combined sources
Helixi40 – 5314Combined sources
Helixi56 – 583Combined sources
Helixi59 – 7719Combined sources
Turni79 – 813Combined sources
Helixi84 – 896Combined sources
Helixi92 – 998Combined sources
Helixi104 – 1063Combined sources
Helixi107 – 11913Combined sources
Helixi125 – 13612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIWNMR-A1-137[»]
3D9IX-ray1.91A/B1-136[»]
3D9JX-ray1.60A/B1-136[»]
3D9KX-ray2.20A/B1-136[»]
3D9LX-ray2.20A/B1-136[»]
3D9MX-ray1.75A/B1-136[»]
3D9NX-ray1.60A/B1-136[»]
3D9OX-ray2.00A/B1-136[»]
3D9PX-ray2.10A/B1-136[»]
ProteinModelPortaliQ9UPN6.
SMRiQ9UPN6. Positions 1-138.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UPN6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 139139CIDPROSITE-ProRule annotationAdd
BLAST
Domaini477 – 55175RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi193 – 371179Gln-richAdd
BLAST
Compositional biasi397 – 45963Arg-richAdd
BLAST
Compositional biasi635 – 1064430Pro-richAdd
BLAST
Compositional biasi1120 – 118263Arg-richAdd
BLAST

Sequence similaritiesi

Contains 1 CID domain.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0132. Eukaryota.
ENOG410XT48. LUCA.
GeneTreeiENSGT00530000063946.
HOGENOMiHOG000154078.
HOVERGENiHBG055796.
InParanoidiQ9UPN6.
KOiK13191.
OrthoDBiEOG7QK0D9.
PhylomeDBiQ9UPN6.
TreeFamiTF324527.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR006569. CID_dom.
IPR008942. ENTH_VHS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR006903. RNA_pol_II-bd.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF04818. CTD_bind. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00582. RPR. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS51391. CID. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UPN6-1) [UniParc]FASTAAdd to basket

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
MEAVKTFNSE LYSLNDYKPP ISKAKMTQIT KAAIKAIKFY KHVVQSVEKF
60 70 80 90 100
IQKCKPEYKV PGLYVIDSIV RQSRHQFGQE KDVFAPRFSN NIISTFQNLY
110 120 130 140 150
RCPGDDKSKI VRVLNLWQKN NVFKSEIIQP LLDMAAGIPP PVVTPVLAST
160 170 180 190 200
TTAMSNTPGT PVTPVTPANV VQGLPDPWVS QITNTDTLAA VAQILQSPQG
210 220 230 240 250
QQLQQLIQTL QIQQQKPQPS ILQALDAGLV VQLQALTAQL TAAAAAANTL
260 270 280 290 300
TPLEQGVSFN KKLMDRFDFG EDSEHSEEPK KEIPASQLSH VSESVNNSIF
310 320 330 340 350
HQIAEQLQQQ NLEHLRQQLL EQQQPQKATP QDSQEGTFGS EHSASPSQGS
360 370 380 390 400
SQQHFLEPEV NLDDSIDIQQ QDMDIDEGQD GVEEEVFEQE AKKVAVRSRS
410 420 430 440 450
RTHSRSRSRS PRKRRSRSRS GSRKRKHRKR SRSRSRERKR KSSRSYSSER
460 470 480 490 500
RAREREKERQ KKGLPPIRSK TLSVCSTTLW VGQVDKKATQ QDLTNLFEEF
510 520 530 540 550
GQIESINMIP PRGCAYVCMV HRQDAFRALQ KLSSGSYKIG SKVIKIAWAL
560 570 580 590 600
NKGVKTEYKQ FWDVDLGVTY IPWEKVKVDD LEGFAEGGMI DQETVNTEWE
610 620 630 640 650
TVKSSEPVKE TVQTTQSPTP VEKETVVTTQ AEVFPPPVAM LQIPVAPAVP
660 670 680 690 700
TVSLVPPAFP VSMPVPPPGF SPIPPPPFLR ASFNPSQPPP GFMPPPVPPP
710 720 730 740 750
VVPPPTIPPV VPTSLVQPSL SMTPETVKDV GFGSLVIPGG SVASNLATSA
760 770 780 790 800
LPAGNVFNAP TKQAEPEEKV PHLIDHQISS GENTRSVIPN DISSNAAILG
810 820 830 840 850
GQPPNVTSNS GILGVQRPNV SSNSEILGVR PSNVSSSSGI IAAQPPNILN
860 870 880 890 900
NSGILGIQPP SVSNSSGLLG VLPPNIPNNS GLVGVQPPNV PNTPGLLGTQ
910 920 930 940 950
PPAGPQNLPP LSIPNQRMPT MPMLDIRPGL IPQAPGPRFP LIQPGIPPQR
960 970 980 990 1000
GIPPPSVLDS ALHPPPRGPF PPGDIFSQPE RPFLAPGRQS VDNVTNPEKR
1010 1020 1030 1040 1050
IPLGNDNIQQ EGDRDYRFPP IETRESISRP PPVDVRDVVG RPIDPREGPG
1060 1070 1080 1090 1100
RPPLDGRDHF GRPPVDIREN LVRPGIDHLG RRDHFGFNPE KPWGHRGDFD
1110 1120 1130 1140 1150
EREHRVLPVY GGPKGLHEER GRFRSGNYRF DPRSGPWNRG FGQEVHRDFD
1160 1170 1180 1190 1200
DRRRPWERQR DRDDRDFDFC REMNGNRLGR DRIQNTWVPP PHARVFDYFE
1210 1220 1230 1240 1250
GATSQRKGDN VPQVNGENTE RHAQPPPIPV QNDPELYEKL TSSNEINKEK
1260 1270
SDTVADIESE PVVESTETEG T
Length:1,271
Mass (Da):140,519
Last modified:May 1, 2000 - v1
Checksum:i9856758DB7622319
GO
Isoform 2 (identifier: Q9UPN6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPQPLLPALPPLSSPSGAGSCGPSGGECSGRRLFRRRARGLRSDNM
     10-10: E → EDCASTPACTDCFSSSMDTRSI

Note: No experimental confirmation available.
Show »
Length:1,337
Mass (Da):147,345
Checksum:i9E5DC6D4A9329466
GO

Sequence cautioni

The sequence BAA83068.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti297 – 2971N → I in AAH70071 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti865 – 8651S → N.
Corresponds to variant rs34802160 [ dbSNP | Ensembl ].
VAR_052220

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPQPLLPALPPLSSPSGAGS CGPSGGECSGRRLFRRRARG LRSDNM in isoform 2. 1 PublicationVSP_056149
Alternative sequencei10 – 101E → EDCASTPACTDCFSSSMDTR SI in isoform 2. 1 PublicationVSP_056150

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029039 mRNA. Translation: BAA83068.2. Different initiation.
AK303001 mRNA. Translation: BAH13874.1.
AL121952, AL136976, AL591499 Genomic DNA. Translation: CAI21474.1.
AL136976, AL121952, AL591499 Genomic DNA. Translation: CAI21482.1.
AL591499, AL121952, AL136976 Genomic DNA. Translation: CAH70694.1.
BC070071 mRNA. Translation: AAH70071.1.
CCDSiCCDS5247.1. [Q9UPN6-1]
CCDS69226.1. [Q9UPN6-2]
RefSeqiNP_001273117.1. NM_001286188.1.
NP_001273118.1. NM_001286189.1. [Q9UPN6-2]
NP_001273123.1. NM_001286194.1.
NP_001273128.1. NM_001286199.1. [Q9UPN6-1]
NP_055707.3. NM_014892.4. [Q9UPN6-1]
UniGeneiHs.591329.

Genome annotation databases

EnsembliENST00000367178; ENSP00000356146; ENSG00000213079. [Q9UPN6-1]
ENST00000367186; ENSP00000356154; ENSG00000213079. [Q9UPN6-2]
GeneIDi22828.
KEGGihsa:22828.
UCSCiuc003qpz.5. human. [Q9UPN6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029039 mRNA. Translation: BAA83068.2. Different initiation.
AK303001 mRNA. Translation: BAH13874.1.
AL121952, AL136976, AL591499 Genomic DNA. Translation: CAI21474.1.
AL136976, AL121952, AL591499 Genomic DNA. Translation: CAI21482.1.
AL591499, AL121952, AL136976 Genomic DNA. Translation: CAH70694.1.
BC070071 mRNA. Translation: AAH70071.1.
CCDSiCCDS5247.1. [Q9UPN6-1]
CCDS69226.1. [Q9UPN6-2]
RefSeqiNP_001273117.1. NM_001286188.1.
NP_001273118.1. NM_001286189.1. [Q9UPN6-2]
NP_001273123.1. NM_001286194.1.
NP_001273128.1. NM_001286199.1. [Q9UPN6-1]
NP_055707.3. NM_014892.4. [Q9UPN6-1]
UniGeneiHs.591329.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIWNMR-A1-137[»]
3D9IX-ray1.91A/B1-136[»]
3D9JX-ray1.60A/B1-136[»]
3D9KX-ray2.20A/B1-136[»]
3D9LX-ray2.20A/B1-136[»]
3D9MX-ray1.75A/B1-136[»]
3D9NX-ray1.60A/B1-136[»]
3D9OX-ray2.00A/B1-136[»]
3D9PX-ray2.10A/B1-136[»]
ProteinModelPortaliQ9UPN6.
SMRiQ9UPN6. Positions 1-138.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116503. 20 interactions.
IntActiQ9UPN6. 8 interactions.
MINTiMINT-6945747.
STRINGi9606.ENSP00000356146.

PTM databases

iPTMnetiQ9UPN6.
PhosphoSiteiQ9UPN6.

Polymorphism and mutation databases

BioMutaiSCAF8.
DMDMi30580495.

Proteomic databases

EPDiQ9UPN6.
MaxQBiQ9UPN6.
PaxDbiQ9UPN6.
PRIDEiQ9UPN6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367178; ENSP00000356146; ENSG00000213079. [Q9UPN6-1]
ENST00000367186; ENSP00000356154; ENSG00000213079. [Q9UPN6-2]
GeneIDi22828.
KEGGihsa:22828.
UCSCiuc003qpz.5. human. [Q9UPN6-1]

Organism-specific databases

CTDi22828.
GeneCardsiSCAF8.
HGNCiHGNC:20959. SCAF8.
HPAiHPA035601.
HPA035602.
MIMi616024. gene.
neXtProtiNX_Q9UPN6.
PharmGKBiPA128394587.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0132. Eukaryota.
ENOG410XT48. LUCA.
GeneTreeiENSGT00530000063946.
HOGENOMiHOG000154078.
HOVERGENiHBG055796.
InParanoidiQ9UPN6.
KOiK13191.
OrthoDBiEOG7QK0D9.
PhylomeDBiQ9UPN6.
TreeFamiTF324527.

Miscellaneous databases

ChiTaRSiSCAF8. human.
EvolutionaryTraceiQ9UPN6.
GenomeRNAii22828.
NextBioi35480420.
PROiQ9UPN6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UPN6.
CleanExiHS_RBM16.
ExpressionAtlasiQ9UPN6. baseline and differential.
GenevisibleiQ9UPN6. HS.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR006569. CID_dom.
IPR008942. ENTH_VHS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR006903. RNA_pol_II-bd.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF04818. CTD_bind. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00582. RPR. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS51391. CID. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "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] (ISOFORM 2).
    Tissue: Testis.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Testis.
  5. "A nuclear matrix protein interacts with the phosphorylated C-terminal domain of RNA polymerase II."
    Patturajan M., Wei X., Berezney R., Corden J.L.
    Mol. Cell. Biol. 18:2406-2415(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLR2A, SUBCELLULAR LOCATION.
  6. "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry."
    Ajuh P., Kuster B., Panov K., Zomerdijk J.C.B.M., Mann M., Lamond A.I.
    EMBO J. 19:6569-6581(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CDC5L AND SPLICEOSOMAL PROTEINS, SUBUNIT, SUBCELLULAR LOCATION, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
    Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
    J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-18, PHOSPHORYLATION AT THR-6.
    Tissue: Cervix carcinoma.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Solution structure of the RPR domain of putative RNA-binding protein 16."
    RIKEN structural genomics initiative (RSGI)
    Submitted (SEP-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-140.
  17. "Snapshots of the RNA processing factor SCAF8 bound to different phosphorylated forms of the carboxyl-terminal domain of RNA polymerase II."
    Becker R., Loll B., Meinhart A.
    J. Biol. Chem. 283:22659-22669(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-136 IN COMPLEX WITH POLR2A PEPTIDE, INTERACTION WITH POLR2A, SUBUNIT.

Entry informationi

Entry nameiSCAF8_HUMAN
AccessioniPrimary (citable) accession number: Q9UPN6
Secondary accession number(s): B7Z888
, Q5TBU6, Q6NSK3, Q9BQN8, Q9BX43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: May 1, 2000
Last modified: April 13, 2016
This is version 135 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.