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Protein

Protein SCAF11

Gene

SCAF11

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

Functioni

Plays a role in pre-mRNA alternative splicing by regulating spliceosome assembly.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri41 – 8242RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. mRNA processing Source: ProtInc
  2. RNA splicing Source: UniProtKB
  3. RNA splicing, via transesterification reactions Source: UniProtKB
  4. spliceosomal complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SCAF11
Alternative name(s):
CTD-associated SR protein 11
Renal carcinoma antigen NY-REN-40
SC35-interacting protein 1
SR-related and CTD-associated factor 11
SRSF2-interacting protein
Serine/arginine-rich splicing factor 2-interacting protein
Splicing factor, arginine/serine-rich 2-interacting protein
Splicing regulatory protein 129
Short name:
SRrp129
Gene namesi
Name:SCAF11
Synonyms:CASP11, SFRS2IP, SIP1, SRSF2IP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:10784. SCAF11.

Subcellular locationi

  1. Nucleus 1 Publication

GO - Cellular componenti

  1. nucleolus Source: HPA
  2. nucleoplasm Source: HPA
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35700.

Polymorphism and mutation databases

BioMutaiSCAF11.
DMDMi251757337.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14631463Protein SCAF11PRO_0000076314Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei338 – 3381Phosphoserine1 Publication
Modified residuei341 – 3411Phosphoserine1 Publication
Modified residuei344 – 3441Phosphoserine1 Publication
Modified residuei400 – 4001Phosphoserine1 Publication
Modified residuei401 – 4011Phosphoserine1 Publication
Modified residuei402 – 4021Phosphoserine1 Publication
Modified residuei405 – 4051Phosphoserine5 Publications
Modified residuei410 – 4101Phosphothreonine1 Publication
Modified residuei413 – 4131Phosphoserine1 Publication
Modified residuei533 – 5331Phosphoserine1 Publication
Modified residuei608 – 6081Phosphoserine5 Publications
Modified residuei614 – 6141Phosphoserine2 Publications
Modified residuei680 – 6801Phosphoserine2 Publications
Modified residuei687 – 6871Phosphoserine1 Publication
Modified residuei723 – 7231Phosphoserine1 Publication
Modified residuei726 – 7261Phosphoserine1 Publication
Modified residuei769 – 7691Phosphothreonine1 Publication
Modified residuei771 – 7711Phosphoserine1 Publication
Modified residuei776 – 7761Phosphoserine2 Publications
Modified residuei796 – 7961Phosphoserine5 Publications
Modified residuei798 – 7981Phosphoserine1 Publication
Modified residuei802 – 8021Phosphoserine4 Publications
Modified residuei807 – 8071Phosphothreonine1 Publication
Modified residuei816 – 8161Phosphoserine1 Publication
Modified residuei963 – 9631Phosphoserine1 Publication
Modified residuei1127 – 11271Phosphoserine2 Publications
Modified residuei1169 – 11691Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99590.
PaxDbiQ99590.
PRIDEiQ99590.

PTM databases

PhosphoSiteiQ99590.

Miscellaneous databases

PMAP-CutDBQ99590.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ99590.
CleanExiHS_SFRS2IP.
HS_SIP1.
ExpressionAtlasiQ99590. baseline and differential.
GenevestigatoriQ99590.

Organism-specific databases

HPAiHPA038862.
HPA045456.
HPA046345.

Interactioni

Subunit structurei

Interacts with SRSF2/SFRS2, U2AF2 and SNRNP70.1 Publication

Protein-protein interaction databases

BioGridi114610. 16 interactions.
IntActiQ99590. 2 interactions.
MINTiMINT-2866162.
STRINGi9606.ENSP00000358374.

Structurei

3D structure databases

ProteinModelPortaliQ99590.
SMRiQ99590. Positions 37-80.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi841 – 985145Arg-richAdd
BLAST
Compositional biasi1225 – 128561Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri41 – 8242RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG300312.
GeneTreeiENSGT00530000063661.
HOVERGENiHBG101126.
InParanoidiQ99590.
OMAiYCTEFIE.
OrthoDBiEOG7F24SX.
PhylomeDBiQ99590.
TreeFamiTF332183.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 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: Q99590-1) [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
MKKKTVCTLN MGDKKYEDME GEENGDNTIS TGLLYSEADR CPICLNCLLE
60 70 80 90 100
KEVGFPESCN HVFCMTCILK WAETLASCPI DRKPFQAVFK FSALEGYVKV
110 120 130 140 150
QVKKQLRETK DKKNENSFEK QVSCHENSKS CIRRKAIVRE DLLSAKVCDL
160 170 180 190 200
KWIHRNSLYS ETGGKKNAAI KINKPQRSNW STNQCFRNFF SNMFSSVSHS
210 220 230 240 250
GESSFTYRAY CTEFIEASEI SALIRQKRHE LELSWFPDTL PGIGRIGFIP
260 270 280 290 300
WNVETEVLPL ISSVLPRTIF PTSTISFEHF GTSCKGYALA HTQEGEEKKQ
310 320 330 340 350
TSGTSNTRGS RRKPAMTTPT RRSTRNTRAE TASQSQRSPI SDNSGCDAPG
360 370 380 390 400
NSNPSLSVPS SAESEKQTRQ APKRKSVRRG RKPPLLKKKL RSSVAAPEKS
410 420 430 440 450
SSNDSVDEET AESDTSPVLE KEHQPDVDSS NICTVQTHVE NQSANCLKSC
460 470 480 490 500
NEQIEESEKH TANYDTEERV GSSSSESCAQ DLPVLVGEEG EVKKLENTGI
510 520 530 540 550
EANVLCLESE ISENILEKGG DPLEKQDQIS GLSQSEVKTD VCTVHLPNDF
560 570 580 590 600
PTCLTSESKV YQPVSCPLSD LSENVESVVN EEKITESSLV EITEHKDFTL
610 620 630 640 650
KTEELIESPK LESSEGEIIQ TVDRQSVKSP EVQLLGHVET EDVEIIATCD
660 670 680 690 700
TFGNEDFNNI QDSENNLLKN NLLNTKLEKS LEEKNESLTE HPRSTELPKT
710 720 730 740 750
HIEQIQKHFS EDNNEMIPME CDSFCSDQNE SEVEPSVNAD LKQMNENSVT
760 770 780 790 800
HCSENNMPSS DLADEKVETV SQPSESPKDT IDKTKKPRTR RSRFHSPSTT
810 820 830 840 850
WSPNKDTPQE KKRPQSPSPR RETGKESRKS QSPSPKNESA RGRKKSRSQS
860 870 880 890 900
PKKDIARERR QSQSRSPKRD TTRESRRSES LSPRRETSRE NKRSQPRVKD
910 920 930 940 950
SSPGEKSRSQ SRERESDRDG QRRERERRTR KWSRSRSHSR SPSRCRTKSK
960 970 980 990 1000
SSSFGRIDRD SYSPRWKGRW ANDGWRCPRG NDRYRKNDPE KQNENTRKEK
1010 1020 1030 1040 1050
NDIHLDADDP NSADKHRNDC PNWITEKINS GPDPRTRNPE KLKESHWEEN
1060 1070 1080 1090 1100
RNENSGNSWN KNFGSGWVSN RGRGRGNRGR GTYRSSFAYK DQNENRWQNR
1110 1120 1130 1140 1150
KPLSGNSNSS GSESFKFVEQ QSYKRKSEQE FSFDTPADRS GWTSASSWAV
1160 1170 1180 1190 1200
RKTLPADVQN YYSRRGRNSS GPQSGWMKQE EETSGQDSSL KDQTNQQVDG
1210 1220 1230 1240 1250
SQLPINMMQP QMNVMQQQMN AQHQPMNIFP YPVGVHAPLM NIQRNPFNIH
1260 1270 1280 1290 1300
PQLPLHLHTG VPLMQVATPT SVSQGLPPPP PPPPPSQQVN YIASQPDGKQ
1310 1320 1330 1340 1350
LQGIPSSSHV SNNMSTPVLP APTAAPGNTG MVQGPSSGNT SSSSHSKASN
1360 1370 1380 1390 1400
AAVKLAESKV SVAVEASADS SKTDKKLQIQ EKAAQEVKLA IKPFYQNKDI
1410 1420 1430 1440 1450
TKEEYKEIVR KAVDKVCHSK SGEVNSTKVA NLVKAYVDKY KYSRKGSQKK
1460
TLEEPVSTEK NIG
Length:1,463
Mass (Da):164,652
Last modified:July 7, 2009 - v2
Checksum:i7170B88544BAF7D4
GO
Isoform 2 (identifier: Q99590-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-315: Missing.

Show »
Length:1,148
Mass (Da):128,875
Checksum:iB57FD40EE5E4C48C
GO

Sequence cautioni

The sequence AAC39565.1 differs from that shown. Reason: Frameshift at position 62. Curated
The sequence AAC39565.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH40951.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH40951.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti584 – 5841I → M in AAH40951 (PubMed:15489334).Curated
Sequence conflicti623 – 6231D → G in AAH40951 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti657 – 6571F → Y.
Corresponds to variant rs7315731 [ dbSNP | Ensembl ].
VAR_059722
Natural varianti1261 – 12611V → L.
Corresponds to variant rs11574973 [ dbSNP | Ensembl ].
VAR_059723

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 315315Missing in isoform 2. 1 PublicationVSP_037665Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11251 mRNA. Translation: CAA72121.1.
AF030234 mRNA. Translation: AAC39565.1. Sequence problems.
AC000015 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57892.1.
CH471111 Genomic DNA. Translation: EAW57894.1.
BC040951 mRNA. Translation: AAH40951.1. Sequence problems.
CCDSiCCDS8748.2. [Q99590-1]
PIRiT09073.
RefSeqiNP_004710.2. NM_004719.2. [Q99590-1]
XP_005269287.2. XM_005269230.2.
UniGeneiHs.210367.

Genome annotation databases

EnsembliENST00000369367; ENSP00000358374; ENSG00000139218. [Q99590-1]
ENST00000465950; ENSP00000449812; ENSG00000139218. [Q99590-2]
GeneIDi9169.
KEGGihsa:9169.
UCSCiuc001row.3. human. [Q99590-1]

Polymorphism and mutation databases

BioMutaiSCAF11.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11251 mRNA. Translation: CAA72121.1.
AF030234 mRNA. Translation: AAC39565.1. Sequence problems.
AC000015 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57892.1.
CH471111 Genomic DNA. Translation: EAW57894.1.
BC040951 mRNA. Translation: AAH40951.1. Sequence problems.
CCDSiCCDS8748.2. [Q99590-1]
PIRiT09073.
RefSeqiNP_004710.2. NM_004719.2. [Q99590-1]
XP_005269287.2. XM_005269230.2.
UniGeneiHs.210367.

3D structure databases

ProteinModelPortaliQ99590.
SMRiQ99590. Positions 37-80.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114610. 16 interactions.
IntActiQ99590. 2 interactions.
MINTiMINT-2866162.
STRINGi9606.ENSP00000358374.

PTM databases

PhosphoSiteiQ99590.

Polymorphism and mutation databases

BioMutaiSCAF11.
DMDMi251757337.

Proteomic databases

MaxQBiQ99590.
PaxDbiQ99590.
PRIDEiQ99590.

Protocols and materials databases

DNASUi9169.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369367; ENSP00000358374; ENSG00000139218. [Q99590-1]
ENST00000465950; ENSP00000449812; ENSG00000139218. [Q99590-2]
GeneIDi9169.
KEGGihsa:9169.
UCSCiuc001row.3. human. [Q99590-1]

Organism-specific databases

CTDi9169.
GeneCardsiGC12M046313.
H-InvDBHIX0010567.
HGNCiHGNC:10784. SCAF11.
HPAiHPA038862.
HPA045456.
HPA046345.
MIMi603668. gene.
neXtProtiNX_Q99590.
PharmGKBiPA35700.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300312.
GeneTreeiENSGT00530000063661.
HOVERGENiHBG101126.
InParanoidiQ99590.
OMAiYCTEFIE.
OrthoDBiEOG7F24SX.
PhylomeDBiQ99590.
TreeFamiTF332183.

Miscellaneous databases

ChiTaRSiSCAF11. human.
GeneWikiiSFRS2IP.
GenomeRNAii9169.
NextBioi34387.
PMAP-CutDBQ99590.
PROiQ99590.
SOURCEiSearch...

Gene expression databases

BgeeiQ99590.
CleanExiHS_SFRS2IP.
HS_SIP1.
ExpressionAtlasiQ99590. baseline and differential.
GenevestigatoriQ99590.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel SR-related protein specifically interacts with the carboxy-terminal domain (CTD) of RNA polymerase II through a conserved interaction domain."
    Tanner S., Stagljar I., Georgiev O., Schaffner W., Bourquin J.-P.
    Biol. Chem. 378:565-571(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Lymphocyte.
  2. "Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing."
    Zhang W.-J., Wu J.Y.
    Mol. Cell. Biol. 18:676-684(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SRSF2; U2AF2 AND SNRNP70, SUBCELLULAR LOCATION.
    Tissue: Cervix carcinoma.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] OF 212-669 (ISOFORM 1).
    Tissue: Prostate.
  6. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  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-405; SER-723 AND SER-726, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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].
  12. "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-405; SER-413; SER-608; SER-796; SER-798 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-608; SER-796; SER-802 AND SER-816, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSCAFB_HUMAN
AccessioniPrimary (citable) accession number: Q99590
Secondary accession number(s): A6NEU9, A6NLW5, Q8IW59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: July 7, 2009
Last modified: April 29, 2015
This is version 111 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 12
    Human chromosome 12: 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

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 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.