Skip Header

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

Q12872

- SFSWA_HUMAN

UniProt

Q12872 - SFSWA_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Splicing factor, suppressor of white-apricot homolog

Gene

SFSWAP

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

Functioni

Plays a role as an alternative splicing regulator. Regulate its own expression at the level of RNA processing. Also regulates the splicing of fibronectin and CD45 genes. May act, at least in part, by interaction with other R/S-containing splicing factors. Represses the splicing of MAPT/Tau exon 10.1 Publication

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. mRNA processing Source: ProtInc
  2. mRNA splice site selection Source: ProtInc
  3. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor, suppressor of white-apricot homolog
Alternative name(s):
Splicing factor, arginine/serine-rich 8
Suppressor of white apricot protein homolog
Gene namesi
Name:SFSWAP
Synonyms:SFRS8, SWAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:10790. SFSWAP.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35706.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 951951Splicing factor, suppressor of white-apricot homologPRO_0000081934Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei283 – 2831Phosphoserine2 Publications
Modified residuei315 – 3151N6-acetyllysine1 Publication
Modified residuei604 – 6041Phosphoserine3 Publications
Modified residuei642 – 6421Phosphothreonine1 Publication
Modified residuei909 – 9091Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ12872.
PaxDbiQ12872.
PRIDEiQ12872.

PTM databases

PhosphoSiteiQ12872.

Expressioni

Gene expression databases

BgeeiQ12872.
CleanExiHS_SFRS8.
ExpressionAtlasiQ12872. baseline and differential.
GenevestigatoriQ12872.

Organism-specific databases

HPAiHPA039362.
HPA040063.

Interactioni

Protein-protein interaction databases

BioGridi112331. 4 interactions.
IntActiQ12872. 2 interactions.
STRINGi9606.ENSP00000261674.

Structurei

Secondary structure

1
951
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi192 – 1943Combined sources
Beta strandi198 – 2003Combined sources
Helixi206 – 22116Combined sources
Helixi224 – 23310Combined sources
Helixi241 – 2433Combined sources
Helixi249 – 26214Combined sources
Turni454 – 4563Combined sources
Helixi457 – 46913Combined sources
Helixi472 – 48110Combined sources
Helixi484 – 4863Combined sources
Beta strandi490 – 4923Combined sources
Helixi496 – 50914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5ZNMR-A440-522[»]
2E60NMR-A189-282[»]
ProteinModelPortaliQ12872.
SMRiQ12872. Positions 189-282, 455-522.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12872.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati211 – 25343SURP motif 1Add
BLAST
Repeati459 – 49941SURP motif 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi165 – 1684Poly-Glu
Compositional biasi287 – 2904Poly-Asp
Compositional biasi382 – 3854Poly-Pro
Compositional biasi413 – 4164Poly-Pro
Compositional biasi420 – 4245Poly-Pro
Compositional biasi434 – 4407Poly-Thr
Compositional biasi451 – 4544Poly-Pro
Compositional biasi616 – 6194Poly-Ser
Compositional biasi660 – 6634Poly-Ala
Compositional biasi754 – 76310Poly-Lys
Compositional biasi789 – 951163Arg/Ser-rich (RS domain)Add
BLAST
Compositional biasi850 – 8534Poly-Lys

Sequence similaritiesi

Contains 2 SURP motif repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG289028.
GeneTreeiENSGT00730000111096.
HOVERGENiHBG079184.
InParanoidiQ12872.
OMAiPPCVVVE.
OrthoDBiEOG786H2Z.
PhylomeDBiQ12872.
TreeFamiTF106264.

Family and domain databases

InterProiIPR000061. Surp.
IPR019147. SWAP_N_domain.
[Graphical view]
PfamiPF09750. DRY_EERY. 1 hit.
PF01805. Surp. 2 hits.
[Graphical view]
SMARTiSM00648. SWAP. 2 hits.
[Graphical view]
SUPFAMiSSF109905. SSF109905. 2 hits.
PROSITEiPS50128. SURP. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q12872-1) [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
MYGASGGRAK PERKSGAKEE AGPGGAGGGG SRVELLVFGY ACKLFRDDER
60 70 80 90 100
ALAQEQGQHL IPWMGDHKIL IDRYDGRGHL HDLSEYDAEY STWNRDYQLS
110 120 130 140 150
EEEARIEALC DEERYLALHT DLLEEEARQE EEYKRLSEAL AEDGSYNAVG
160 170 180 190 200
FTYGSDYYDP SEPTEEEEPS KQREKNEAEN LEENEEPFVA PLGLSVPSDV
210 220 230 240 250
ELPPTAKMHA IIERTASFVC RQGAQFEIML KAKQARNSQF DFLRFDHYLN
260 270 280 290 300
PYYKFIQKAM KEGRYTVLAE NKSDEKKKSG VSSDNEDDDD EEDGNYLHPS
310 320 330 340 350
LFASKKCNRL EELMKPLKVV DPDHPLAALV RKAQADSSTP TPHNADGAPV
360 370 380 390 400
QPSQVEYTAD STVAAMYYSY YMLPDGTYCL APPPPGIDVT TYYSTLPAGV
410 420 430 440 450
TVSNSPGVTT TAPPPPGTTP LPPPTTAETS SGATSTTTTT SALAPVAAII
460 470 480 490 500
PPPPDVQPVI DKLAEYVARN GLKFETSVRA KNDQRFEFLQ PWHQYNAYYE
510 520 530 540 550
FKKQFFLQKE GGDSMQAVSA PEEAPTDSAP EKPSDAGEDG APEDAAEVGA
560 570 580 590 600
RAGSGGKKEA SSSKTVPDGK LVKASFAPIS FAIKAKENDL LPLEKNRVKL
610 620 630 640 650
DDDSDDDEES KEGQESSSSA ANTNPAVAPP CVVVEEKKPQ LTQEELEAKQ
660 670 680 690 700
AKQKLEDRLA AAAREKLAQA SKESKEKQLQ AERKRKAALF LQTLKNPLPE
710 720 730 740 750
AEAGKIEESP FSVEESSTTP CPLLTGGRPL PTLEVKPPDR PSSKSKDPPR
760 770 780 790 800
EEEKEKKKKK HKKRSRTRSR SPKYHSSSKS RSRSHSKAKH SLPSAYRTVR
810 820 830 840 850
RSRSRSRSPR RRAHSPERRR EERSVPTAYR VSRSPGASRK RTRSRSPHEK
860 870 880 890 900
KKKRRSRSRT KSKARSQSVS PSKQAAPRPA APAAHSAHSA SVSPVESRGS
910 920 930 940 950
SQERSRGVSQ EKEAQISSAI VSSVQSKITQ DLMAKVRAML AASKNLQTSA

S
Length:951
Mass (Da):104,822
Last modified:March 23, 2010 - v3
Checksum:iA942D589F4B6BF47
GO
Isoform 2 (identifier: Q12872-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     801-801: R → RSRVTASPGTLRAEPCQSSASVTAAAEPGSYQAASTTTRFDSASSFEGKPGKT

Note: No experimental confirmation available.

Show »
Length:1,003
Mass (Da):110,012
Checksum:iC67AFFE577FF7CA4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361R → P in AAA19604. (PubMed:8206918)Curated
Sequence conflicti493 – 4931H → Y in AAA19604. (PubMed:8206918)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521L → Q.1 Publication
Corresponds to variant rs1051207 [ dbSNP | Ensembl ].
VAR_046442
Natural varianti122 – 1221L → F.
Corresponds to variant rs1051314 [ dbSNP | Ensembl ].
VAR_046443
Natural varianti136 – 1361L → F.1 Publication
Corresponds to variant rs1131564 [ dbSNP | Ensembl ].
VAR_046444
Natural varianti421 – 4211L → P.3 Publications
Corresponds to variant rs1982528 [ dbSNP | Ensembl ].
VAR_021789
Natural varianti512 – 5121G → S.
Corresponds to variant rs34541796 [ dbSNP | Ensembl ].
VAR_057248
Natural varianti538 – 5381E → G.
Corresponds to variant rs34744641 [ dbSNP | Ensembl ].
VAR_057249
Natural varianti887 – 8871A → E.
Corresponds to variant rs34729193 [ dbSNP | Ensembl ].
VAR_057250

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei801 – 8011R → RSRVTASPGTLRAEPCQSSA SVTAAAEPGSYQAASTTTRF DSASSFEGKPGKT in isoform 2. 1 PublicationVSP_044786

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08377 mRNA. Translation: AAA19604.1.
AC117500 Genomic DNA. No translation available.
AC131009 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98526.1.
BC008707 mRNA. Translation: AAH08707.1.
BC015953 mRNA. Translation: AAH15953.1.
BC136678 mRNA. Translation: AAI36679.1.
BC144364 mRNA. Translation: AAI44365.1.
CCDSiCCDS58290.1. [Q12872-2]
CCDS9273.1. [Q12872-1]
PIRiA54037.
B54037.
C54037.
RefSeqiNP_001248340.1. NM_001261411.1. [Q12872-2]
NP_004583.2. NM_004592.3. [Q12872-1]
UniGeneiHs.308171.

Genome annotation databases

EnsembliENST00000261674; ENSP00000261674; ENSG00000061936. [Q12872-1]
ENST00000541286; ENSP00000437738; ENSG00000061936. [Q12872-2]
GeneIDi6433.
KEGGihsa:6433.
UCSCiuc001uja.2. human. [Q12872-1]

Polymorphism databases

DMDMi292495067.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08377 mRNA. Translation: AAA19604.1 .
AC117500 Genomic DNA. No translation available.
AC131009 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98526.1 .
BC008707 mRNA. Translation: AAH08707.1 .
BC015953 mRNA. Translation: AAH15953.1 .
BC136678 mRNA. Translation: AAI36679.1 .
BC144364 mRNA. Translation: AAI44365.1 .
CCDSi CCDS58290.1. [Q12872-2 ]
CCDS9273.1. [Q12872-1 ]
PIRi A54037.
B54037.
C54037.
RefSeqi NP_001248340.1. NM_001261411.1. [Q12872-2 ]
NP_004583.2. NM_004592.3. [Q12872-1 ]
UniGenei Hs.308171.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E5Z NMR - A 440-522 [» ]
2E60 NMR - A 189-282 [» ]
ProteinModelPortali Q12872.
SMRi Q12872. Positions 189-282, 455-522.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112331. 4 interactions.
IntActi Q12872. 2 interactions.
STRINGi 9606.ENSP00000261674.

PTM databases

PhosphoSitei Q12872.

Polymorphism databases

DMDMi 292495067.

Proteomic databases

MaxQBi Q12872.
PaxDbi Q12872.
PRIDEi Q12872.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261674 ; ENSP00000261674 ; ENSG00000061936 . [Q12872-1 ]
ENST00000541286 ; ENSP00000437738 ; ENSG00000061936 . [Q12872-2 ]
GeneIDi 6433.
KEGGi hsa:6433.
UCSCi uc001uja.2. human. [Q12872-1 ]

Organism-specific databases

CTDi 6433.
GeneCardsi GC12P132196.
H-InvDB HIX0036782.
HGNCi HGNC:10790. SFSWAP.
HPAi HPA039362.
HPA040063.
MIMi 601945. gene.
neXtProti NX_Q12872.
PharmGKBi PA35706.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG289028.
GeneTreei ENSGT00730000111096.
HOVERGENi HBG079184.
InParanoidi Q12872.
OMAi PPCVVVE.
OrthoDBi EOG786H2Z.
PhylomeDBi Q12872.
TreeFami TF106264.

Miscellaneous databases

ChiTaRSi SFSWAP. human.
EvolutionaryTracei Q12872.
GenomeRNAii 6433.
NextBioi 24987.
PROi Q12872.
SOURCEi Search...

Gene expression databases

Bgeei Q12872.
CleanExi HS_SFRS8.
ExpressionAtlasi Q12872. baseline and differential.
Genevestigatori Q12872.

Family and domain databases

InterProi IPR000061. Surp.
IPR019147. SWAP_N_domain.
[Graphical view ]
Pfami PF09750. DRY_EERY. 1 hit.
PF01805. Surp. 2 hits.
[Graphical view ]
SMARTi SM00648. SWAP. 2 hits.
[Graphical view ]
SUPFAMi SSF109905. SSF109905. 2 hits.
PROSITEi PS50128. SURP. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Conservation of regulated alternative splicing and identification of functional domains in vertebrate homologs to the Drosophila splicing regulator, suppressor-of-white-apricot."
    Denhez F., Lafyatis R.
    J. Biol. Chem. 269:16170-16179(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-52; PHE-136 AND PRO-421.
    Tissue: Placenta.
  2. "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].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-421.
  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] (ISOFORMS 1 AND 2), VARIANT PRO-421.
    Tissue: Brain and Skin.
  5. "The mammalian homolog of suppressor-of-white-apricot regulates alternative mRNA splicing of CD45 exon 4 and fibronectin IIICS."
    Sarkissian M., Winne A., Lafyatis R.
    J. Biol. Chem. 271:31106-31114(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-642, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-604 AND SER-909, 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-283 AND SER-909, 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-315, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Solution structure of the SURP1 and SURP2 domain in splicing factor, arginine/serine-rich 8."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 189-282 AND 434-522.

Entry informationi

Entry nameiSFSWA_HUMAN
AccessioniPrimary (citable) accession number: Q12872
Secondary accession number(s): B2RN45
, B7ZM97, F5H6B8, Q6PJF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: March 23, 2010
Last modified: November 26, 2014
This is version 128 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3