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Protein

Splicing factor, arginine/serine-rich 15

Gene

SCAF4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May act to physically and functionally link transcription and pre-mRNA processing.By similarity

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor, arginine/serine-rich 15
Alternative name(s):
CTD-binding SR-like protein RA4
SR-related and CTD-associated factor 4
Gene namesi
Name:SCAF4
Synonyms:KIAA1172, SFRS15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:19304. SCAF4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134903281.

Polymorphism and mutation databases

BioMutaiSCAF4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11471147Splicing factor, arginine/serine-rich 15PRO_0000081943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491N6-acetyllysineCombined sources
Modified residuei154 – 1541PhosphoserineCombined sources
Modified residuei656 – 6561PhosphoserineCombined sources
Modified residuei1004 – 10041PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO95104.
MaxQBiO95104.
PaxDbiO95104.
PeptideAtlasiO95104.
PRIDEiO95104.

PTM databases

iPTMnetiO95104.
PhosphoSiteiO95104.

Expressioni

Gene expression databases

BgeeiO95104.
CleanExiHS_SFRS15.
GenevisibleiO95104. HS.

Organism-specific databases

HPAiHPA018319.
HPA018668.
HPA021504.
HPA028807.

Interactioni

Subunit structurei

Interacts with the repetitive C-terminal domain (CTD) of RNA polymerase II.By similarity

Protein-protein interaction databases

BioGridi121536. 33 interactions.
IntActiO95104. 3 interactions.
MINTiMINT-1692995.
STRINGi9606.ENSP00000286835.

Structurei

3D structure databases

ProteinModelPortaliO95104.
SMRiO95104. Positions 1-137.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 139139CIDPROSITE-ProRule annotationAdd
BLAST
Domaini508 – 58275RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi155 – 1584Poly-Pro
Compositional biasi304 – 3118Poly-Ala
Compositional biasi313 – 3164Poly-Pro
Compositional biasi716 – 7238Poly-Pro
Compositional biasi740 – 7467Poly-Pro
Compositional biasi957 – 96610Poly-Gln

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 1 CID domain.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0132. Eukaryota.
ENOG410XT48. LUCA.
GeneTreeiENSGT00530000063946.
HOGENOMiHOG000143432.
HOVERGENiHBG055644.
InParanoidiO95104.
KOiK13167.
OMAiHISDNRK.
OrthoDBiEOG7QK0D9.
PhylomeDBiO95104.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95104-1) [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
MDAVNAFNQE LFSLMDMKPP ISRAKMILIT KAAIKAIKLY KHVVQIVEKF
60 70 80 90 100
IKKCKPEYKV PGLYVIDSIV RQSRHQFGTD KDVFGPRFSK NITATFQYLY
110 120 130 140 150
LCPSEDKSKI VRVLNLWQKN GVFKIEIIQP LLDMAAGTSN AAPVAENVTN
160 170 180 190 200
NEGSPPPPVK VSSEPPTQAT PNSVPAVPQL PSSDAFAAVA QLFQTTQGQQ
210 220 230 240 250
LQQILQTFQQ PPKPQSPALD NAVMAQVQAI TAQLKTTPTQ PSEQKAAFPP
260 270 280 290 300
PEQKTAFDKK LLDRFDYDDE PEAVEESKKE DTTAVTTTAP AAAVPPAPTA
310 320 330 340 350
TVPAAAAPAA ASPPPPQAPF GFPGDGMQQP AYTQHQNMDQ FQPRMMGIQQ
360 370 380 390 400
DPMHHQVPLP PNGQMPGFGL LPTPPFPPMA QPVIPPTPPV QQPFQASFQA
410 420 430 440 450
QNEPLTQKPH QQEMEVEQPC IQEVKRHMSD NRKSRSRSAS RSPKRRRSRS
460 470 480 490 500
GSRSRRSRHR RSRSRSRDRR RHSPRSRSQE RRDREKERER RQKGLPQVKP
510 520 530 540 550
ETASVCSTTL WVGQLDKRTT QQDVASLLEE FGPIESINMI PPRGCAYIVM
560 570 580 590 600
VHRQDAYRAL QKLSRGNYKV NQKSIKIAWA LNKGIKADYK QYWDVELGVT
610 620 630 640 650
YIPWDKVKPE ELESFCEGGM LDSDTLNPDW KGIPKKPENE VAQNGGAETS
660 670 680 690 700
HTEPVSPIPK PLPVPVPPIP VPAPITVPPP QVPPHQPGPP VVGALQPPAF
710 720 730 740 750
TPPLGIPPPG FGPGVPPPPP PPPFLRPGFN PMHLPPGFLP PGPPPPITPP
760 770 780 790 800
VSIPPPHTPP ISIPNSTIAG INEDTTKDLS IGNPIPTVVS GARGNAESGD
810 820 830 840 850
SVKMYGSAVP PAAPTNLPTP PVTQPVSLLG TQGVAPGPVI GLQAPSTGLL
860 870 880 890 900
GARPGLIPLQ RPPGMPPPHL QRFPLMPPRP MPPHMMHRGP PPGPGGFAMP
910 920 930 940 950
PPHGMKGPFP PHGPFVRPGG MPGLGGPGPG PGGPEDRDGR QQPPQQPQQQ
960 970 980 990 1000
PQPQAPQQPQ QQQQQQPPPS QQPPPTQQQP QQFRNDNRQQ FNSGRDQERF
1010 1020 1030 1040 1050
GRRSFGNRVE NDRERYGNRN DDRDNSNRDR REWGRRSPDR DRHRDLEERN
1060 1070 1080 1090 1100
RRSSGHRDRE RDSRDRESRR EKEEARGKEK PEVTDRAGGN KTVEPPISQV
1110 1120 1130 1140
GNVDTASELE KGVSEAAVLK PSEELPAEAT SSVEPEKDSG SAAEAPR
Length:1,147
Mass (Da):125,869
Last modified:February 15, 2005 - v3
Checksum:iDED5EEAB45DB4B83
GO
Isoform 2 (identifier: O95104-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     766-788: STIAGINEDTTKDLSIGNPIPTV → L

Note: No experimental confirmation available.
Show »
Length:1,125
Mass (Da):123,643
Checksum:iD771D62662D7B0C6
GO
Isoform 3 (identifier: O95104-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     38-52: Missing.

Note: No experimental confirmation available.
Show »
Length:1,132
Mass (Da):124,014
Checksum:iF19B820E11955748
GO

Sequence cautioni

The sequence AAD09327.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → W in AAD09327 (Ref. 1) Curated
Sequence conflicti260 – 2645Missing in CAB55911 (PubMed:17974005).Curated
Sequence conflicti283 – 2831T → I in AAD09327 (Ref. 1) Curated
Sequence conflicti286 – 2861T → A in AAD09327 (Ref. 1) Curated
Sequence conflicti299 – 2991T → A in AAD09327 (Ref. 1) Curated
Sequence conflicti302 – 3021V → L in BAA86486 (PubMed:10574461).Curated
Sequence conflicti552 – 5521H → Y in AAD09327 (Ref. 1) Curated
Sequence conflicti560 – 5601L → V in AAD09327 (Ref. 1) Curated
Sequence conflicti571 – 5711N → T (Ref. 1) Curated
Sequence conflicti598 – 6003GVT → CVI in AAD09327 (Ref. 1) Curated
Sequence conflicti604 – 6063WDK → CDN in AAD09327 (Ref. 1) Curated
Sequence conflicti612 – 6121L → M in AAD09327 (Ref. 1) Curated
Sequence conflicti616 – 6161C → Y in AAD09327 (Ref. 1) Curated
Sequence conflicti624 – 6241D → N in AK308406 (PubMed:17974005).Curated
Sequence conflicti808 – 82619AVPPA…VTQPV → TCCTHESAHPSCNPACLPC in AAD09327 (Ref. 1) CuratedAdd
BLAST
Sequence conflicti844 – 8441A → E in AAD09327 (Ref. 1) Curated
Sequence conflicti1139 – 11391S → G (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti846 – 8461S → Y.
Corresponds to variant rs12152067 [ dbSNP | Ensembl ].
VAR_052234

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei38 – 5215Missing in isoform 3. 1 PublicationVSP_047351Add
BLAST
Alternative sequencei766 – 78823STIAG…PIPTV → L in isoform 2. 2 PublicationsVSP_005879Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023142 mRNA. Translation: AAD09327.1. Different initiation.
AK308406 mRNA. No translation available.
AL834304 mRNA. Translation: CAD38974.2.
AL117417 mRNA. Translation: CAB55911.1. Sequence problems.
AP001711 Genomic DNA. No translation available.
BC014921 mRNA. Translation: AAH14921.1.
BC052286 mRNA. Translation: AAH52286.1.
BC064990 mRNA. Translation: AAH64990.1.
AB032998 mRNA. Translation: BAA86486.1.
CCDSiCCDS33537.1. [O95104-1]
CCDS46644.1. [O95104-2]
CCDS54482.1. [O95104-3]
RefSeqiNP_001138916.1. NM_001145444.1. [O95104-3]
NP_001138917.1. NM_001145445.1. [O95104-2]
NP_065757.1. NM_020706.2. [O95104-1]
UniGeneiHs.17255.

Genome annotation databases

EnsembliENST00000286835; ENSP00000286835; ENSG00000156304. [O95104-1]
ENST00000399804; ENSP00000382703; ENSG00000156304. [O95104-2]
ENST00000434667; ENSP00000402377; ENSG00000156304. [O95104-3]
GeneIDi57466.
KEGGihsa:57466.
UCSCiuc002ypd.3. human. [O95104-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023142 mRNA. Translation: AAD09327.1. Different initiation.
AK308406 mRNA. No translation available.
AL834304 mRNA. Translation: CAD38974.2.
AL117417 mRNA. Translation: CAB55911.1. Sequence problems.
AP001711 Genomic DNA. No translation available.
BC014921 mRNA. Translation: AAH14921.1.
BC052286 mRNA. Translation: AAH52286.1.
BC064990 mRNA. Translation: AAH64990.1.
AB032998 mRNA. Translation: BAA86486.1.
CCDSiCCDS33537.1. [O95104-1]
CCDS46644.1. [O95104-2]
CCDS54482.1. [O95104-3]
RefSeqiNP_001138916.1. NM_001145444.1. [O95104-3]
NP_001138917.1. NM_001145445.1. [O95104-2]
NP_065757.1. NM_020706.2. [O95104-1]
UniGeneiHs.17255.

3D structure databases

ProteinModelPortaliO95104.
SMRiO95104. Positions 1-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121536. 33 interactions.
IntActiO95104. 3 interactions.
MINTiMINT-1692995.
STRINGi9606.ENSP00000286835.

PTM databases

iPTMnetiO95104.
PhosphoSiteiO95104.

Polymorphism and mutation databases

BioMutaiSCAF4.

Proteomic databases

EPDiO95104.
MaxQBiO95104.
PaxDbiO95104.
PeptideAtlasiO95104.
PRIDEiO95104.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000286835; ENSP00000286835; ENSG00000156304. [O95104-1]
ENST00000399804; ENSP00000382703; ENSG00000156304. [O95104-2]
ENST00000434667; ENSP00000402377; ENSG00000156304. [O95104-3]
GeneIDi57466.
KEGGihsa:57466.
UCSCiuc002ypd.3. human. [O95104-1]

Organism-specific databases

CTDi57466.
GeneCardsiSCAF4.
HGNCiHGNC:19304. SCAF4.
HPAiHPA018319.
HPA018668.
HPA021504.
HPA028807.
MIMi616023. gene.
neXtProtiNX_O95104.
PharmGKBiPA134903281.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0132. Eukaryota.
ENOG410XT48. LUCA.
GeneTreeiENSGT00530000063946.
HOGENOMiHOG000143432.
HOVERGENiHBG055644.
InParanoidiO95104.
KOiK13167.
OMAiHISDNRK.
OrthoDBiEOG7QK0D9.
PhylomeDBiO95104.
TreeFamiTF324527.

Miscellaneous databases

ChiTaRSiSCAF4. human.
GenomeRNAii57466.
PROiO95104.
SOURCEiSearch...

Gene expression databases

BgeeiO95104.
CleanExiHS_SFRS15.
GenevisibleiO95104. 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. "Sequence, genomic organization and map localization of the human SR protein gene rA4."
    Tassone F., Villard L., Gardiner K.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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 3).
    Tissue: Trachea.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Melanoma and Testis.
  4. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Brain and Uterus.
  6. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
    Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
    DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1147 (ISOFORM 2).
    Tissue: Brain.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. "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 SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-154 AND SER-1004, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  16. "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-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSFR15_HUMAN
AccessioniPrimary (citable) accession number: O95104
Secondary accession number(s): C9JLZ0
, Q0P5W8, Q6P1M5, Q8N3I8, Q9UFM1, Q9ULP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 15, 2005
Last modified: July 6, 2016
This is version 144 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 21
    Human chromosome 21: 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.