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Protein

SAFB-like transcription modulator

Gene

Sltm

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

When overexpressed, acts as a general inhibitor of transcription that eventually leads to apoptosis.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
SAFB-like transcription modulator
Alternative name(s):
Modulator of estrogen-induced transcription
SAF-like transcription modulator
Gene namesi
Name:Sltm
Synonyms:Met
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1913910. Sltm.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Detected in punctate structures.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 10311030SAFB-like transcription modulatorPRO_0000307799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei93 – 931PhosphoserineBy similarity
Modified residuei97 – 971PhosphoserineBy similarity
Modified residuei139 – 1391PhosphoserineCombined sources
Modified residuei144 – 1441PhosphoserineBy similarity
Modified residuei289 – 2891PhosphoserineCombined sources
Modified residuei401 – 4011N6-acetyllysineBy similarity
Modified residuei421 – 4211PhosphoserineBy similarity
Cross-linki500 – 500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei549 – 5491PhosphoserineCombined sources
Modified residuei550 – 5501PhosphoserineCombined sources
Modified residuei552 – 5521PhosphoserineCombined sources
Modified residuei747 – 7471PhosphoserineBy similarity
Modified residuei797 – 7971PhosphoserineBy similarity
Cross-linki881 – 881Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei906 – 9061PhosphoserineBy similarity
Modified residuei999 – 9991PhosphoserineCombined sources
Modified residuei1011 – 10111PhosphoserineBy similarity
Modified residuei1016 – 10161PhosphoserineBy similarity
Modified residuei1018 – 10181PhosphoserineBy similarity
Modified residuei1021 – 10211N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8CH25.
MaxQBiQ8CH25.
PaxDbiQ8CH25.
PRIDEiQ8CH25.

PTM databases

iPTMnetiQ8CH25.
PhosphoSiteiQ8CH25.

Expressioni

Gene expression databases

BgeeiQ8CH25.
CleanExiMM_MET.
MM_SLTM.
ExpressionAtlasiQ8CH25. baseline and differential.
GenevisibleiQ8CH25. MM.

Interactioni

Protein-protein interaction databases

BioGridi211628. 2 interactions.
IntActiQ8CH25. 1 interaction.
MINTiMINT-4115860.
STRINGi10090.ENSMUSP00000049112.

Structurei

3D structure databases

ProteinModelPortaliQ8CH25.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 5635SAPPROSITE-ProRule annotationAdd
BLAST
Domaini384 – 46279RRMPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili107 – 18276Sequence analysisAdd
BLAST
Coiled coili608 – 727120Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi108 – 239132Glu-richAdd
BLAST
Compositional biasi568 – 903336Arg/Glu-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4661. Eukaryota.
ENOG4111F1G. LUCA.
GeneTreeiENSGT00730000110777.
HOGENOMiHOG000092533.
HOVERGENiHBG096731.
InParanoidiQ8CH25.
OMAiRERXIER.
OrthoDBiEOG79W94X.
PhylomeDBiQ8CH25.
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]
SUPFAMiSSF54928. SSF54928. 1 hit.
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: Q8CH25-1) [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
MAAAAGAVVA SAASGPAEGK KITELRVIDL RSELKRRNLD INGVKTVLVS
60 70 80 90 100
RLKQAIEEEG GDPDNIELTV STDTPNKKPT KGKGKKQEAD ELSGDASVED
110 120 130 140 150
DSFVKDCELE NQETHDQDGN EELKDLEEFG ENEEEIVHSQ ELLSTEENKT
160 170 180 190 200
TQEFVEAEAI EDREKEDIES QETEAQEGED DTFLTAQDGE EEENEKDIAG
210 220 230 240 250
SGDGTQEVSK PLPSEGSLAE ADHTAHEEME ANATGKEAED DNISVTIQAE
260 270 280 290 300
DAITLDFDGD DLLETGKNVK ITDSEASKPK DVQDAIAQSP EKEAKDYEMN
310 320 330 340 350
PNHKDGKKED SVKGEPVEKE ARESAKKAES GDKEKDTLKK GPSSTGASGQ
360 370 380 390 400
AKSSSKESKD SKTSSKDDKG STGSAGGSSG SSTKNIWVSG LSSNTKAADL
410 420 430 440 450
KNLFGKYGKV LSAKVVTNAR SPGAKCYGIV TMSSSTEVSR CVAHLHRTEL
460 470 480 490 500
HGQLISVEKV KGDPSKKEMK KENDEKSSSR SAGDKKNASD RSAKTQASIK
510 520 530 540 550
KEEKRSSEKS EKKESKDTKK IEKDEKNDDG PSGQTSESLK KSEEKKRISS
560 570 580 590 600
KSPGHMVILN QTKGDHCRPS RRGRYEKGHG RSKEKERASL DKKRDKDYRR
610 620 630 640 650
KEILPFEKMK EQRLREHLVR FERLKQAVEF RRRKEIAERE RRERERIRII
660 670 680 690 700
REREERERLQ RERERLEIER QKLERERMER ERLERERIRI EQERRREAER
710 720 730 740 750
IAREREELRR QQQQLRYEQE KRNSLKRPRD VDHRRDDPYW SENKKLSLDT
760 770 780 790 800
EARFGHGSDY RQQSRFLDFS HRERARFPDT ASVQSSFERR ERFVGQSEGK
810 820 830 840 850
KPRPAARREE PSFERYPKNF SDSRRNEPPP PRNELRETDR REVRGERDER
860 870 880 890 900
RTVILHDRPE VAHPRHPRET VPNPSRPTSW KSEANMSTEK RESRVERPER
910 920 930 940 950
SGREVSGHTV RGAPPGNRSS ASGYGTREGE RGVIADRGSG TQHYPEERHV
960 970 980 990 1000
VERHGRDTSG PRKEWHGPPS QGPSYHDTRR MGDGRAGAGM ITQHSSTASP
1010 1020 1030
VNRIVQMSGN SLPRGSSSGF KPFKSGPPRR F
Length:1,031
Mass (Da):116,919
Last modified:March 1, 2003 - v1
Checksum:iDBD3F617F816C79C
GO
Isoform 2 (identifier: Q8CH25-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     197-214: Missing.

Show »
Length:1,013
Mass (Da):115,179
Checksum:iF0D3C0E3C42E4FDE
GO

Sequence cautioni

The sequence AAH19992.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC32471.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE22267.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41A → R in BAB30967 (PubMed:16141072).Curated
Sequence conflicti985 – 9851R → Q in BAE22267 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei197 – 21418Missing in isoform 2. 1 PublicationVSP_028834Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF462146 mRNA. Translation: AAO15605.1.
AK017839 mRNA. Translation: BAB30967.1.
AK045723 mRNA. Translation: BAC32471.1. Different initiation.
AK077578 mRNA. Translation: BAC36873.1.
AK134756 mRNA. Translation: BAE22267.1. Different initiation.
BC019992 mRNA. Translation: AAH19992.1. Different initiation.
CCDSiCCDS23322.1. [Q8CH25-1]
RefSeqiNP_079966.2. NM_025690.3. [Q8CH25-1]
NP_080613.1. NM_026337.1. [Q8CH25-2]
UniGeneiMm.22379.

Genome annotation databases

EnsembliENSMUST00000049263; ENSMUSP00000049112; ENSMUSG00000032212. [Q8CH25-1]
GeneIDi66660.
KEGGimmu:66660.
UCSCiuc009qok.1. mouse. [Q8CH25-2]
uc009qol.1. mouse. [Q8CH25-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF462146 mRNA. Translation: AAO15605.1.
AK017839 mRNA. Translation: BAB30967.1.
AK045723 mRNA. Translation: BAC32471.1. Different initiation.
AK077578 mRNA. Translation: BAC36873.1.
AK134756 mRNA. Translation: BAE22267.1. Different initiation.
BC019992 mRNA. Translation: AAH19992.1. Different initiation.
CCDSiCCDS23322.1. [Q8CH25-1]
RefSeqiNP_079966.2. NM_025690.3. [Q8CH25-1]
NP_080613.1. NM_026337.1. [Q8CH25-2]
UniGeneiMm.22379.

3D structure databases

ProteinModelPortaliQ8CH25.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211628. 2 interactions.
IntActiQ8CH25. 1 interaction.
MINTiMINT-4115860.
STRINGi10090.ENSMUSP00000049112.

PTM databases

iPTMnetiQ8CH25.
PhosphoSiteiQ8CH25.

Proteomic databases

EPDiQ8CH25.
MaxQBiQ8CH25.
PaxDbiQ8CH25.
PRIDEiQ8CH25.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049263; ENSMUSP00000049112; ENSMUSG00000032212. [Q8CH25-1]
GeneIDi66660.
KEGGimmu:66660.
UCSCiuc009qok.1. mouse. [Q8CH25-2]
uc009qol.1. mouse. [Q8CH25-1]

Organism-specific databases

CTDi79811.
MGIiMGI:1913910. Sltm.

Phylogenomic databases

eggNOGiKOG4661. Eukaryota.
ENOG4111F1G. LUCA.
GeneTreeiENSGT00730000110777.
HOGENOMiHOG000092533.
HOVERGENiHBG096731.
InParanoidiQ8CH25.
OMAiRERXIER.
OrthoDBiEOG79W94X.
PhylomeDBiQ8CH25.
TreeFamiTF325240.

Miscellaneous databases

ChiTaRSiSltm. mouse.
NextBioi322303.
PROiQ8CH25.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CH25.
CleanExiMM_MET.
MM_SLTM.
ExpressionAtlasiQ8CH25. baseline and differential.
GenevisibleiQ8CH25. MM.

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]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel member of the SAF (scaffold attachment factor)-box protein family inhibits gene expression and induces apoptosis."
    Chan C.W., Lee Y.-B., Uney J., Flynn A., Tobias J.H., Norman M.
    Biochem. J. 407:355-362(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-582 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 425-1031 (ISOFORM 1/2).
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina, Embryo and Medulla oblongata.
  3. "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 528-1031 (ISOFORM 1/2).
    Strain: FVB/N.
    Tissue: Colon.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-999, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-549; SER-550; SER-552 AND SER-999, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSLTM_MOUSE
AccessioniPrimary (citable) accession number: Q8CH25
Secondary accession number(s): Q3UYE5
, Q8BP76, Q8BR40, Q8VCF4, Q9CS57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: March 1, 2003
Last modified: March 16, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.