Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Helicase SKI2W

Gene

SKIV2L

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

Functioni

Helicase; has ATPase activity. Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi332 – 3398ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: ProtInc
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Helicase SKI2W (EC:3.6.4.-)
Short name:
Ski2
Alternative name(s):
Helicase-like protein
Short name:
HLP
Gene namesi
Name:SKIV2L
Synonyms:DDX13, SKI2W, SKIV2, W
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:10898. SKIV2L.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • Ski complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Trichohepatoenteric syndrome 2 (THES2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by intrauterine growth retardation, severe diarrhea in infancy requiring total parenteral nutrition, facial dysmorphism, immunodeficiency, and hair abnormalities, mostly trichorrhexis nodosa. Hepatic involvement contributes to the poor prognosis of affected patients.
See also OMIM:614602
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti341 – 3411V → G in THES2. 1 Publication
Corresponds to variant rs281875237 [ dbSNP | Ensembl ].
VAR_067721

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiSKIV2L.
MIMi614602. phenotype.
Orphaneti84064. Syndromic diarrhea.
PharmGKBiPA35798.

Polymorphism and mutation databases

BioMutaiSKIV2L.
DMDMi313104288.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12461246Helicase SKI2WPRO_0000102091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei245 – 2451PhosphoserineCombined sources
Modified residuei256 – 2561PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ15477.
MaxQBiQ15477.
PaxDbiQ15477.
PeptideAtlasiQ15477.
PRIDEiQ15477.

PTM databases

iPTMnetiQ15477.
PhosphoSiteiQ15477.

Expressioni

Gene expression databases

BgeeiQ15477.
CleanExiHS_SKIV2L.
ExpressionAtlasiQ15477. baseline and differential.
GenevisibleiQ15477. HS.

Organism-specific databases

HPAiHPA051959.
HPA054419.

Interactioni

Subunit structurei

Component of the SKI complex which consists of WDR61, SKIV2L and TTC37.1 Publication

Protein-protein interaction databases

BioGridi112390. 32 interactions.
IntActiQ15477. 16 interactions.
STRINGi9606.ENSP00000364543.

Structurei

3D structure databases

ProteinModelPortaliQ15477.
SMRiQ15477. Positions 280-836, 1018-1244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini319 – 475157Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini585 – 755171Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi423 – 4264DEVH box

Sequence similaritiesi

Belongs to the helicase family. SKI2 subfamily.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0948. Eukaryota.
COG4581. LUCA.
GeneTreeiENSGT00820000127042.
HOGENOMiHOG000163048.
HOVERGENiHBG060025.
InParanoidiQ15477.
KOiK12599.
OMAiAIHMILE.
PhylomeDBiQ15477.
TreeFamiTF314438.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR025696. rRNA_proc-arch_dom.
IPR016438. Ski2.
IPR012961. Ski2_C.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF08148. DSHCT. 1 hit.
PF00271. Helicase_C. 1 hit.
PF13234. rRNA_proc-arch. 1 hit.
[Graphical view]
PIRSFiPIRSF005198. Antiviral_helicase_SKI2. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM01142. DSHCT. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15477-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMETERLVLP PPDPLDLPLR AVELGCTGHW ELLNLPGAPE SSLPHGLPPC
60 70 80 90 100
APDLQQEAEQ LFLSSPAWLP LHGVEHSARK WQRKTDPWSL LAVLGAPVPS
110 120 130 140 150
DLQAQRHPTT GQILGYKEVL LENTNLSATT SLSLRRPPGP ASQSLWGNPT
160 170 180 190 200
QYPFWPGGMD EPTITDLNTR EEAEEEIDFE KDLLTIPPGF KKGMDFAPKD
210 220 230 240 250
CPTPAPGLLS LSCMLEPLDL GGGDEDENEA VGQPGGPRGD TVSASPCSAP
260 270 280 290 300
LARASSLEDL VLKEASTAVS TPEAPEPPSQ EQWAIPVDAT SPVGDFYRLI
310 320 330 340 350
PQPAFQWAFE PDVFQKQAIL HLERHDSVFV AAHTSAGKTV VAEYAIALAQ
360 370 380 390 400
KHMTRTIYTS PIKALSNQKF RDFRNTFGDV GLLTGDVQLH PEASCLIMTT
410 420 430 440 450
EILRSMLYSG SDVIRDLEWV IFDEVHYIND VERGVVWEEV LIMLPDHVSI
460 470 480 490 500
ILLSATVPNA LEFADWIGRL KRRQIYVIST VTRPVPLEHY LFTGNSSKTQ
510 520 530 540 550
GELFLLLDSR GAFHTKGYYA AVEAKKERMS KHAQTFGAKQ PTHQGGPAQD
560 570 580 590 600
RGVYLSLLAS LRTRAQLPVV VFTFSRGRCD EQASGLTSLD LTTSSEKSEI
610 620 630 640 650
HLFLQRCLAR LRGSDRQLPQ VLHMSELLNR GLGVHHSGIL PILKEIVEML
660 670 680 690 700
FSRGLVKVLF ATETFAMGVN MPARTVVFDS MRKHDGSTFR DLLPGEYVQM
710 720 730 740 750
AGRAGRRGLD PTGTVILLCK GRVPEMADLH RMMMGKPSQL QSQFRLTYTM
760 770 780 790 800
ILNLLRVDAL RVEDMMKRSF SEFPSRKDSK AHEQALAELT KRLGALEEPD
810 820 830 840 850
MTGQLVDLPE YYSWGEELTE TQHMIQRRIM ESVNGLKSLS AGRVVVVKNQ
860 870 880 890 900
EHHNALGVIL QVSSNSTSRV FTTLVLCDKP LSQDPQDRGP ATAEVPYPDD
910 920 930 940 950
LVGFKLFLPE GPCDHTVVKL QPGDMAAITT KVLRVNGEKI LEDFSKRQQP
960 970 980 990 1000
KFKKDPPLAA VTTAVQELLR LAQAHPAGPP TLDPVNDLQL KDMSVVEGGL
1010 1020 1030 1040 1050
RARKLEELIQ GAQCVHSPRF PAQYLKLRER MQIQKEMERL RFLLSDQSLL
1060 1070 1080 1090 1100
LLPEYHQRVE VLRTLGYVDE AGTVKLAGRV ACAMSSHELL LTELMFDNAL
1110 1120 1130 1140 1150
STLRPEEIAA LLSGLVCQSP GDAGDQLPNT LKQGIERVRA VAKRIGEVQV
1160 1170 1180 1190 1200
ACGLNQTVEE FVGELNFGLV EVVYEWARGM PFSELAGLSG TPEGLVVRCI
1210 1220 1230 1240
QRLAEMCRSL RGAARLVGEP VLGAKMETAA TLLRRDIVFA ASLYTQ
Length:1,246
Mass (Da):137,755
Last modified:November 30, 2010 - v3
Checksum:i9F00097BA83A4AEC
GO

Sequence cautioni

The sequence AAB52523.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti366 – 3661S → T in AAB52523 (PubMed:7759100).Curated
Sequence conflicti623 – 6231H → Q in CAA88733 (PubMed:7610041).Curated
Sequence conflicti1052 – 10521L → F in CAA88733 (PubMed:7610041).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti151 – 1511Q → R.2 Publications
Corresponds to variant rs438999 [ dbSNP | Ensembl ].
VAR_060379
Natural varianti183 – 1831L → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035944
Natural varianti214 – 2141M → L.3 Publications
Corresponds to variant rs437179 [ dbSNP | Ensembl ].
VAR_060380
Natural varianti324 – 3241R → W.
Corresponds to variant rs36038685 [ dbSNP | Ensembl ].
VAR_055888
Natural varianti341 – 3411V → G in THES2. 1 Publication
Corresponds to variant rs281875237 [ dbSNP | Ensembl ].
VAR_067721
Natural varianti765 – 7651M → I in a colorectal cancer sample; somatic mutation. 1 Publication
Corresponds to variant rs557829269 [ dbSNP | Ensembl ].
VAR_035945
Natural varianti887 – 8871D → N.
Corresponds to variant rs3911893 [ dbSNP | Ensembl ].
VAR_055889
Natural varianti917 – 9171V → M.1 Publication
Corresponds to variant rs106287 [ dbSNP | Ensembl ].
VAR_055890
Natural varianti1071 – 10711A → V.1 Publication
Corresponds to variant rs449643 [ dbSNP | Ensembl ].
VAR_055891
Natural varianti1153 – 11531G → R.
Corresponds to variant rs2734329 [ dbSNP | Ensembl ].
VAR_060381
Natural varianti1238 – 12381V → G.
Corresponds to variant rs2746400 [ dbSNP | Ensembl ].
VAR_060382

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09877 mRNA. Translation: AAB52523.1. Different initiation.
X98378 Genomic DNA. Translation: CAA67024.1.
Z48796 mRNA. Translation: CAA88733.1.
AF019413 Genomic DNA. Translation: AAB67978.1.
AL662849 Genomic DNA. Translation: CAI17460.1.
AL645922 Genomic DNA. Translation: CAQ09280.1.
CCDSiCCDS4731.1.
PIRiS56752.
RefSeqiNP_008860.4. NM_006929.4.
UniGeneiHs.89864.

Genome annotation databases

EnsembliENST00000375394; ENSP00000364543; ENSG00000204351.
ENST00000383336; ENSP00000372827; ENSG00000206353.
ENST00000412823; ENSP00000400626; ENSG00000232616.
ENST00000421789; ENSP00000399530; ENSG00000228896.
ENST00000429465; ENSP00000412310; ENSG00000223493.
ENST00000448219; ENSP00000394400; ENSG00000225737.
GeneIDi6499.
KEGGihsa:6499.
UCSCiuc003nyn.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09877 mRNA. Translation: AAB52523.1. Different initiation.
X98378 Genomic DNA. Translation: CAA67024.1.
Z48796 mRNA. Translation: CAA88733.1.
AF019413 Genomic DNA. Translation: AAB67978.1.
AL662849 Genomic DNA. Translation: CAI17460.1.
AL645922 Genomic DNA. Translation: CAQ09280.1.
CCDSiCCDS4731.1.
PIRiS56752.
RefSeqiNP_008860.4. NM_006929.4.
UniGeneiHs.89864.

3D structure databases

ProteinModelPortaliQ15477.
SMRiQ15477. Positions 280-836, 1018-1244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112390. 32 interactions.
IntActiQ15477. 16 interactions.
STRINGi9606.ENSP00000364543.

PTM databases

iPTMnetiQ15477.
PhosphoSiteiQ15477.

Polymorphism and mutation databases

BioMutaiSKIV2L.
DMDMi313104288.

Proteomic databases

EPDiQ15477.
MaxQBiQ15477.
PaxDbiQ15477.
PeptideAtlasiQ15477.
PRIDEiQ15477.

Protocols and materials databases

DNASUi6499.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375394; ENSP00000364543; ENSG00000204351.
ENST00000383336; ENSP00000372827; ENSG00000206353.
ENST00000412823; ENSP00000400626; ENSG00000232616.
ENST00000421789; ENSP00000399530; ENSG00000228896.
ENST00000429465; ENSP00000412310; ENSG00000223493.
ENST00000448219; ENSP00000394400; ENSG00000225737.
GeneIDi6499.
KEGGihsa:6499.
UCSCiuc003nyn.2. human.

Organism-specific databases

CTDi6499.
GeneCardsiSKIV2L.
H-InvDBHIX0005742.
HIX0166115.
HIX0166390.
HIX0166908.
HIX0167165.
HIX0167404.
HGNCiHGNC:10898. SKIV2L.
HPAiHPA051959.
HPA054419.
MalaCardsiSKIV2L.
MIMi600478. gene.
614602. phenotype.
neXtProtiNX_Q15477.
Orphaneti84064. Syndromic diarrhea.
PharmGKBiPA35798.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0948. Eukaryota.
COG4581. LUCA.
GeneTreeiENSGT00820000127042.
HOGENOMiHOG000163048.
HOVERGENiHBG060025.
InParanoidiQ15477.
KOiK12599.
OMAiAIHMILE.
PhylomeDBiQ15477.
TreeFamiTF314438.

Enzyme and pathway databases

ReactomeiR-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

ChiTaRSiSKIV2L. human.
GeneWikiiSKIV2L.
GenomeRNAii6499.
PROiQ15477.
SOURCEiSearch...

Gene expression databases

BgeeiQ15477.
CleanExiHS_SKIV2L.
ExpressionAtlasiQ15477. baseline and differential.
GenevisibleiQ15477. HS.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR025696. rRNA_proc-arch_dom.
IPR016438. Ski2.
IPR012961. Ski2_C.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF08148. DSHCT. 1 hit.
PF00271. Helicase_C. 1 hit.
PF13234. rRNA_proc-arch. 1 hit.
[Graphical view]
PIRSFiPIRSF005198. Antiviral_helicase_SKI2. 1 hit.
SMARTiSM00487. DEXDc. 1 hit.
SM01142. DSHCT. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a human cDNA homologous to yeast SKI2."
    Lee S.-G., Lee I., Park S.H., Kang C., Song K.
    Genomics 25:660-666(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Human helicase gene SKI2W in the HLA class III region exhibits striking structural similarities to the yeast antiviral gene SKI2 and to the human gene KIAA0052: emergence of a new gene family."
    Dangel A.W., Shen L., Mendoza A.R., Wu L.-C., Yu C.Y.
    Nucleic Acids Res. 23:2120-2126(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS ARG-151 AND LEU-214.
  3. "Localization of eight additional genes in the human major histocompatibility complex, including the gene encoding the casein kinase II beta subunit (CSNK2B)."
    Albertella M.R., Jones H., Thomson W., Olavesen M.G., Campbell R.D.
    Genomics 36:240-251(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-214.
  4. "Sequence determination of 300 kilobases of the human class III MHC locus."
    Rowen L., Dankers C., Baskin D., Faust J., Loretz C., Ahearn M.E., Banta A., Swartzell S., Smith T.M., Spies T., Hood L.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-151; LEU-214; MET-917 AND VAL-1071.
  5. "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].
  6. "The human PAF complex coordinates transcription with events downstream of RNA synthesis."
    Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K., Tempst P., Reinberg D.
    Genes Dev. 19:1668-1673(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SKI COMPLEX.
  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. "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-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  18. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-183 AND ILE-765.
  20. Cited for: VARIANT THES2 GLY-341.

Entry informationi

Entry nameiSKIV2_HUMAN
AccessioniPrimary (citable) accession number: Q15477
Secondary accession number(s): O15005
, Q12902, Q15476, Q5ST66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 30, 2010
Last modified: July 6, 2016
This is version 159 of the entry and version 3 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 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. 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.