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Protein

Scaffold attachment factor B2

Gene

SAFB2

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

Functioni

Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation.

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Scaffold attachment factor B2
Short name:
SAF-B2
Gene namesi
Name:SAFB2
Synonyms:KIAA0138
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:21605. SAFB2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134987683.

Polymorphism and mutation databases

BioMutaiSAFB2.
DMDMi38372432.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 953952Scaffold attachment factor B2PRO_0000081907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei109 – 1091Phosphoserine3 Publications
Modified residuei158 – 1581Phosphoserine1 Publication
Modified residuei201 – 2011Phosphothreonine1 Publication
Modified residuei207 – 2071Phosphoserine2 Publications
Cross-linki230 – 230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki293 – 293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei513 – 5131Phosphoserine2 Publications
Modified residuei616 – 6161N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14151.
PaxDbiQ14151.
PeptideAtlasiQ14151.
PRIDEiQ14151.

PTM databases

PhosphoSiteiQ14151.

Expressioni

Tissue specificityi

Expressed at high levels in the CNS and at low levels in the liver. Expressed in a wide number of breast cancer cell lines.

Gene expression databases

BgeeiQ14151.
CleanExiHS_SAFB2.
ExpressionAtlasiQ14151. baseline and differential.
GenevisibleiQ14151. HS.

Organism-specific databases

HPAiHPA050894.

Interactioni

Subunit structurei

Interacts with SAFB/SAFB1 and SCAM1. Interacts with isoform 2 SRPK1 and inhibits its activity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-352869,EBI-352869
ESR1P033722EBI-352869,EBI-78473
GABARAPL1Q9H0R82EBI-352869,EBI-746969
MAP1LC3BQ9GZQ83EBI-352869,EBI-373144
SAFBQ154243EBI-352869,EBI-348298
SORBS3O60504-23EBI-352869,EBI-1222956

Protein-protein interaction databases

BioGridi115022. 33 interactions.
IntActiQ14151. 24 interactions.
MINTiMINT-5006081.
STRINGi9606.ENSP00000252542.

Structurei

3D structure databases

ProteinModelPortaliQ14151.
SMRiQ14151. Positions 405-486.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 6435SAPPROSITE-ProRule annotationAdd
BLAST
Domaini407 – 48579RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni600 – 953354Interacts with SAFB1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi713 – 73018Nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi482 – 54564Lys-richAdd
BLAST
Compositional biasi619 – 724106Glu-richAdd
BLAST
Compositional biasi621 – 788168Arg-richAdd
BLAST
Compositional biasi792 – 926135Gly-richAdd
BLAST

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation
Contains 1 SAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG248048.
GeneTreeiENSGT00730000110777.
HOGENOMiHOG000092533.
HOVERGENiHBG078408.
InParanoidiQ14151.
OMAiDWGEHSQ.
OrthoDBiEOG722J7Z.
PhylomeDBiQ14151.
TreeFamiTF325240.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14151-1) [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
MAETLPGSGD SGPGTASLGP GVAETGTRRL SELRVIDLRA ELKKRNLDTG
60 70 80 90 100
GNKSVLMERL KKAVKEEGQD PDEIGIELEA TSKKSAKRCV KGLKMEEEGT
110 120 130 140 150
EDNGLEDDSR DGQEDMEASL ENLQNMGMMD MSVLDETEVA NSSAPDFGED
160 170 180 190 200
GTDGLLDSFC DSKEYVAAQL RQLPAQPPEH AVDGEGFKNT LETSSLNFKV
210 220 230 240 250
TPDIEESLLE PENEKILDIL GETCKSEPVK EESSELEQPF AQDTSSVGPD
260 270 280 290 300
RKLAEEEDLF DSAHPEEGDL DLASESTAHA QSSKADSLLA VVKREPAEQP
310 320 330 340 350
GDGERTDCEP VGLEPAVEQS SAASELAEAS SEELAEAPTE APSPEARDSK
360 370 380 390 400
EDGRKFDFDA CNEVPPAPKE SSTSEGADQK MSSFKEEKDI KPIIKDEKGR
410 420 430 440 450
VGSGSGRNLW VSGLSSTTRA TDLKNLFSKY GKVVGAKVVT NARSPGARCY
460 470 480 490 500
GFVTMSTSDE ATKCISHLHR TELHGRMISV EKAKNEPAGK KLSDRKECEV
510 520 530 540 550
KKEKLSSVDR HHSVEIKIEK TVIKKEEKIE KKEEKKPEDI KKEEKDQDEL
560 570 580 590 600
KPGPTNRSRV TKSGSRGMER TVVMDKSKGE PVISVKTTSR SKERSSKSQD
610 620 630 640 650
RKSESKEKRD ILSFDKIKEQ RERERQRQRE REIRETERRR EREQREREQR
660 670 680 690 700
LEAFHERKEK ARLQRERLQL ECQRQRLERE RMERERLERE RMRVERERRK
710 720 730 740 750
EQERIHRERE ELRRQQEQLR YEQERRPGRR PYDLDRRDDA YWPEGKRVAM
760 770 780 790 800
EDRYRADFPR PDHRFHDFDH RDRGQYQDHA IDRREGSRPM MGDHRDGQHY
810 820 830 840 850
GDDRHGHGGP PERHGRDSRD GWGGYGSDKR LSEGRGLPPP PRGGRDWGEH
860 870 880 890 900
NQRLEEHQAR AWQGAMDAGA ASREHARWQG GERGLSGPSG PGHMASRGGV
910 920 930 940 950
AGRGGFAQGG HSQGHVVPGG GLEGGGVASQ DRGSRVPHPH PHPPPYPHFT

RRY
Length:953
Mass (Da):107,473
Last modified:November 1, 1996 - v1
Checksum:i084343934F8B3196
GO
Isoform 2 (identifier: Q14151-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-115: LKMEEEGTEDNGLEDDSRDGQED → GHGSKSGEPAEYGHDGHECARRN
     116-953: Missing.

Note: No experimental confirmation available.
Show »
Length:115
Mass (Da):12,169
Checksum:i534B2863F1DC5B72
GO

Sequence cautioni

The sequence BAA09487.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti528 – 5281K → M in AAH25279 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei93 – 11523LKMEE…DGQED → GHGSKSGEPAEYGHDGHECA RRN in isoform 2. 1 PublicationVSP_056404Add
BLAST
Alternative sequencei116 – 953838Missing in isoform 2. 1 PublicationVSP_056405Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50928 mRNA. Translation: BAA09487.2. Different initiation.
AK296552 mRNA. Translation: BAG59175.1.
AC004611 Genomic DNA. Translation: AAC14666.1.
BC025279 mRNA. Translation: AAH25279.1.
CCDSiCCDS32879.1. [Q14151-1]
RefSeqiNP_055464.1. NM_014649.2. [Q14151-1]
UniGeneiHs.655392.

Genome annotation databases

EnsembliENST00000252542; ENSP00000252542; ENSG00000130254.
ENST00000591120; ENSP00000468505; ENSG00000130254. [Q14151-2]
GeneIDi9667.
KEGGihsa:9667.
UCSCiuc002mcd.3. human. [Q14151-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50928 mRNA. Translation: BAA09487.2. Different initiation.
AK296552 mRNA. Translation: BAG59175.1.
AC004611 Genomic DNA. Translation: AAC14666.1.
BC025279 mRNA. Translation: AAH25279.1.
CCDSiCCDS32879.1. [Q14151-1]
RefSeqiNP_055464.1. NM_014649.2. [Q14151-1]
UniGeneiHs.655392.

3D structure databases

ProteinModelPortaliQ14151.
SMRiQ14151. Positions 405-486.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115022. 33 interactions.
IntActiQ14151. 24 interactions.
MINTiMINT-5006081.
STRINGi9606.ENSP00000252542.

PTM databases

PhosphoSiteiQ14151.

Polymorphism and mutation databases

BioMutaiSAFB2.
DMDMi38372432.

Proteomic databases

MaxQBiQ14151.
PaxDbiQ14151.
PeptideAtlasiQ14151.
PRIDEiQ14151.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252542; ENSP00000252542; ENSG00000130254.
ENST00000591120; ENSP00000468505; ENSG00000130254. [Q14151-2]
GeneIDi9667.
KEGGihsa:9667.
UCSCiuc002mcd.3. human. [Q14151-1]

Organism-specific databases

CTDi9667.
GeneCardsiGC19M005587.
HGNCiHGNC:21605. SAFB2.
HPAiHPA050894.
MIMi608066. gene.
neXtProtiNX_Q14151.
PharmGKBiPA134987683.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG248048.
GeneTreeiENSGT00730000110777.
HOGENOMiHOG000092533.
HOVERGENiHBG078408.
InParanoidiQ14151.
OMAiDWGEHSQ.
OrthoDBiEOG722J7Z.
PhylomeDBiQ14151.
TreeFamiTF325240.

Miscellaneous databases

ChiTaRSiSAFB2. human.
GeneWikiiSAFB2.
GenomeRNAii9667.
NextBioi35472778.
PROiQ14151.
SOURCEiSearch...

Gene expression databases

BgeeiQ14151.
CleanExiHS_SAFB2.
ExpressionAtlasiQ14151. baseline and differential.
GenevisibleiQ14151. HS.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  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 2).
    Tissue: Thalamus.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] OF 1-528 (ISOFORM 1).
    Tissue: Pancreas.
  5. "SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor."
    Townson S.M., Dobrzycka K.M., Lee A.V., Air M., Deng W., Kang K., Jiang S., Kioka N., Michaelis K., Oesterreich S.
    J. Biol. Chem. 278:20059-20068(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "The enzymatic activity of SR protein kinases 1 and 1a is negatively affected by interaction with scaffold attachment factors B1 and 2."
    Tsianou D., Nikolakaki E., Tzitzira A., Bonanou S., Giannakouros T., Georgatsou E.
    FEBS J. 276:5212-5227(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRPK1.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-616, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-109; THR-201; SER-207 AND SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Co-repressor activity of scaffold attachment factor B1 requires sumoylation."
    Garee J.P., Meyer R., Oesterreich S.
    Biochem. Biophys. Res. Commun. 408:516-522(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-230 AND LYS-293.
  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-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  19. "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-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSAFB2_HUMAN
AccessioniPrimary (citable) accession number: Q14151
Secondary accession number(s): B4DKG3, Q8TB13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 145 of the entry and version 1 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 19
    Human chromosome 19: 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. 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.