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Q13435

- SF3B2_HUMAN

UniProt

Q13435 - SF3B2_HUMAN

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Protein

Splicing factor 3B subunit 2

Gene

SF3B2

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

Functioni

Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA processing Source: ProtInc
  3. mRNA splicing, via spliceosome Source: UniProtKB
  4. RNA splicing Source: Reactome
  5. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiREACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor 3B subunit 2
Alternative name(s):
Pre-mRNA-splicing factor SF3b 145 kDa subunit
Short name:
SF3b145
SF3b150
Spliceosome-associated protein 145
Short name:
SAP 145
Gene namesi
Name:SF3B2
Synonyms:SAP145
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:10769. SF3B2.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. spliceosomal complex Source: HGNC
  5. U12-type spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35687.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 895895Splicing factor 3B subunit 2PRO_0000174328Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei275 – 2751N6-acetyllysine1 Publication
Modified residuei289 – 2891Phosphoserine3 Publications
Modified residuei307 – 3071Phosphoserine3 Publications
Modified residuei309 – 3091Phosphoserine3 Publications
Modified residuei311 – 3111Phosphothreonine1 Publication
Modified residuei360 – 3601Phosphoserine1 Publication
Modified residuei362 – 3621Phosphoserine1 Publication
Modified residuei431 – 4311Phosphoserine4 Publications
Modified residuei435 – 4351Phosphoserine4 Publications
Modified residuei436 – 4361Phosphoserine4 Publications
Modified residuei780 – 7801Phosphothreonine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13435.
PaxDbiQ13435.
PRIDEiQ13435.

PTM databases

PhosphoSiteiQ13435.

Miscellaneous databases

PMAP-CutDBQ13435.

Expressioni

Gene expression databases

BgeeiQ13435.
CleanExiHS_SF3B2.
ExpressionAtlasiQ13435. baseline and differential.
GenevestigatoriQ13435.

Organism-specific databases

HPAiHPA045028.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Component of splicing factor SF3B which is composed of at least eight subunits; SF3B1/SAP155/SF3B155, SF3B2/SAP145/SF3B145, SF3B3/SAP130/SF3B130, SF3B4/SAP49/SF3B49, SF3B14A, PHF5A/SF3B14B, SF3B10 and SF3B125. SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). SF3B2 interacts directly with SF3B4. Interacts with HIV-1 Vpr.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX16O602312EBI-749111,EBI-311446
FRA10AC1Q70Z532EBI-749111,EBI-710176
KDM1AO603412EBI-749111,EBI-710124
PRPF3O433952EBI-749111,EBI-744322
PRPF8Q6P2Q93EBI-749111,EBI-538479
RNF113AO155412EBI-749111,EBI-2130294
SF3B4Q154273EBI-749111,EBI-348469
SLU7O953912EBI-749111,EBI-750559
U2AF1Q010812EBI-749111,EBI-632461
XAB2Q9HCS72EBI-749111,EBI-295232
ZNF830Q96NB32EBI-749111,EBI-3920997

Protein-protein interaction databases

BioGridi116188. 106 interactions.
IntActiQ13435. 49 interactions.
MINTiMINT-3027706.
STRINGi9606.ENSP00000318861.

Structurei

Secondary structure

1
895
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 3911
Helixi47 – 6115

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DO5NMR-A24-68[»]
ProteinModelPortaliQ13435.
SMRiQ13435. Positions 26-68.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13435.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 5835SAPPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili140 – 19960Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 216Poly-Pro
Compositional biasi91 – 966Poly-Pro
Compositional biasi104 – 11310Poly-Pro
Compositional biasi129 – 1324Poly-Pro
Compositional biasi249 – 2535Poly-Pro
Compositional biasi292 – 2976Poly-Glu
Compositional biasi331 – 3355Poly-Lys
Compositional biasi699 – 7024Poly-Glu
Compositional biasi720 – 7267Poly-Glu

Sequence similaritiesi

Contains 1 SAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5182.
GeneTreeiENSGT00390000006734.
HOVERGENiHBG054023.
InParanoidiQ13435.
KOiK12829.
OMAiDRLKGYM.
PhylomeDBiQ13435.
TreeFamiTF300635.

Family and domain databases

InterProiIPR007180. DUF382.
IPR006568. PSP.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF04037. DUF382. 1 hit.
PF04046. PSP. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00581. PSP. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13435-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATEHPEPPK AELQLPPPPP PGHYGAWAAQ ELQAKLAEIG APIQGNREEL
60 70 80 90 100
VERLQSYTRQ TGIVLNRPVL RGEDGDKAAP PPMSAQLPGI PMPPPPLGLP
110 120 130 140 150
PLQPPPPPPP PPPGLGLGFP MAHPPNLGPP PPLRVGEPVA LSEEERLKLA
160 170 180 190 200
QQQAALLMQQ EERAKQQGDH SLKEHELLEQ QKRAAVLLEQ ERQQEIAKMG
210 220 230 240 250
TPVPRPPQDM GQIGVRTPLG PRVAAPVGPV GPTPTVLPMG APVPRPRGPP
260 270 280 290 300
PPPGDENREM DDPSVGPKIP QALEKILQLK ESRQEEMNSQ QEEEEMETDA
310 320 330 340 350
RSSLGQSASE TEEDTVSVSK KEKNRKRRNR KKKKKPQRVR GVSSESSGDR
360 370 380 390 400
EKDSTRSRGS DSPAADVEIE YVTEEPEIYE PNFIFFKRIF EAFKLTDDVK
410 420 430 440 450
KEKEKEPEKL DKLENSAAPK KKGFEEEHKD SDDDSSDDEQ EKKPEAPKLS
460 470 480 490 500
KKKLRRMNRF TVAELKQLVA RPDVVEMHDV TAQDPKLLVH LKATRNSVPV
510 520 530 540 550
PRHWCFKRKY LQGKRGIEKP PFELPDFIKR TGIQEMREAL QEKEEQKTMK
560 570 580 590 600
SKMREKVRPK MGKIDIDYQK LHDAFFKWQT KPKLTIHGDL YYEGKEFETR
610 620 630 640 650
LKEKKPGDLS DELRISLGMP VGPNAHKVPP PWLIAMQRYG PPPSYPNLKI
660 670 680 690 700
PGLNSPIPES CSFGYHAGGW GKPPVDETGK PLYGDVFGTN AAEFQTKTEE
710 720 730 740 750
EEIDRTPWGE LEPSDEESSE EEEEEESDED KPDETGFITP ADSGLITPGG
760 770 780 790 800
FSSVPAGMET PELIELRKKK IEEAMDGSET PQLFTVLPEK RTATVGGAMM
810 820 830 840 850
GSTHIYDMST VMSRKGPAPE LQGVEVALAP EELELDPMAM TQKYEEHVRE
860 870 880 890
QQAQVEKEDF SDMVAEHAAK QKQKKRKAQP QDSRGGSKKY KEFKF
Length:895
Mass (Da):100,228
Last modified:May 18, 2010 - v2
Checksum:iD372AFA679443AD6
GO

Sequence cautioni

The sequence AAA97461.1 differs from that shown. Reason: Frameshift at position 28. Curated
The sequence AAA97461.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH53577.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAG61831.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti602 – 6021K → E in BAF83539. (PubMed:14702039)Curated
Sequence conflicti765 – 7651E → G in BAF83539. (PubMed:14702039)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK290850 mRNA. Translation: BAF83539.1.
AK300016 mRNA. Translation: BAG61831.1. Different initiation.
BC000401 mRNA. Translation: AAH00401.2.
BC007610 mRNA. Translation: AAH07610.1.
BC014125 mRNA. Translation: AAH14125.2.
BC053577 mRNA. Translation: AAH53577.1. Sequence problems.
U41371 mRNA. Translation: AAA97461.1. Frameshift.
CCDSiCCDS31612.1.
RefSeqiNP_006833.2. NM_006842.2.
UniGeneiHs.406423.

Genome annotation databases

EnsembliENST00000322535; ENSP00000318861; ENSG00000087365.
GeneIDi10992.
KEGGihsa:10992.
UCSCiuc001ogy.1. human.

Polymorphism databases

DMDMi296452908.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK290850 mRNA. Translation: BAF83539.1 .
AK300016 mRNA. Translation: BAG61831.1 . Different initiation.
BC000401 mRNA. Translation: AAH00401.2 .
BC007610 mRNA. Translation: AAH07610.1 .
BC014125 mRNA. Translation: AAH14125.2 .
BC053577 mRNA. Translation: AAH53577.1 . Sequence problems.
U41371 mRNA. Translation: AAA97461.1 . Frameshift.
CCDSi CCDS31612.1.
RefSeqi NP_006833.2. NM_006842.2.
UniGenei Hs.406423.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DO5 NMR - A 24-68 [» ]
ProteinModelPortali Q13435.
SMRi Q13435. Positions 26-68.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116188. 106 interactions.
IntActi Q13435. 49 interactions.
MINTi MINT-3027706.
STRINGi 9606.ENSP00000318861.

Chemistry

ChEMBLi CHEMBL1229011.

PTM databases

PhosphoSitei Q13435.

Polymorphism databases

DMDMi 296452908.

Proteomic databases

MaxQBi Q13435.
PaxDbi Q13435.
PRIDEi Q13435.

Protocols and materials databases

DNASUi 10992.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322535 ; ENSP00000318861 ; ENSG00000087365 .
GeneIDi 10992.
KEGGi hsa:10992.
UCSCi uc001ogy.1. human.

Organism-specific databases

CTDi 10992.
GeneCardsi GC11P065827.
H-InvDB HIX0009823.
HGNCi HGNC:10769. SF3B2.
HPAi HPA045028.
MIMi 605591. gene.
neXtProti NX_Q13435.
PharmGKBi PA35687.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5182.
GeneTreei ENSGT00390000006734.
HOVERGENi HBG054023.
InParanoidi Q13435.
KOi K12829.
OMAi DRLKGYM.
PhylomeDBi Q13435.
TreeFami TF300635.

Enzyme and pathway databases

Reactomei REACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi SF3B2. human.
EvolutionaryTracei Q13435.
GeneWikii SF3B2.
GenomeRNAii 10992.
NextBioi 41771.
PMAP-CutDB Q13435.
PROi Q13435.
SOURCEi Search...

Gene expression databases

Bgeei Q13435.
CleanExi HS_SF3B2.
ExpressionAtlasi Q13435. baseline and differential.
Genevestigatori Q13435.

Family and domain databases

InterProi IPR007180. DUF382.
IPR006568. PSP.
IPR003034. SAP_dom.
[Graphical view ]
Pfami PF04037. DUF382. 1 hit.
PF04046. PSP. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view ]
SMARTi SM00581. PSP. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view ]
PROSITEi PS50800. SAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Lymphoblast and Peripheral blood.
  2. "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].
    Tissue: Eye, Kidney, Lung and Testis.
  3. "Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A."
    Gozani O., Feld R., Reed R.
    Genes Dev. 10:233-243(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-895, PROTEIN SEQUENCE OF 174-182 AND 817-840.
    Tissue: Cervix carcinoma.
  4. "Functional association of U2 snRNP with the ATP-independent spliceosomal complex E."
    Das R., Zhou Z., Reed R.
    Mol. Cell 5:779-787(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE SPLICEOSOME.
  5. "Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein."
    Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R.
    EMBO J. 21:4978-4988(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SF3B COMPLEX.
  6. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  7. "Molecular architecture of the multiprotein splicing factor SF3b."
    Golas M.M., Sander B., Will C.L., Luhrmann R., Stark H.
    Science 300:980-984(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SF3B COMPLEX, ELECTRON MICROSCOPY OF THE SF3B COMPLEX.
  8. "The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
    Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
    RNA 10:929-941(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "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-431; SER-435 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Human immunodeficiency virus type 1 Vpr induces G2 checkpoint activation by interacting with the splicing factor SAP145."
    Terada Y., Yasuda Y.
    Mol. Cell. Biol. 26:8149-8158(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 VPR.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. "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.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-307; SER-309; THR-311 AND THR-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-435 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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].
  16. "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-307; SER-309; SER-360; SER-362 AND THR-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-307; SER-309; SER-431; SER-435; SER-436 AND THR-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-289; SER-431; SER-435 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Solution structure of the SAP domain of human splicing factor 3B subunit 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 24-68.

Entry informationi

Entry nameiSF3B2_HUMAN
AccessioniPrimary (citable) accession number: Q13435
Secondary accession number(s): A8K485
, B4DT19, Q7L4T5, Q7Z627, Q969K1, Q96CM6, Q9BWD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 136 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3