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Protein

SAM domain-containing protein SAMSN-1

Gene

Samsn1

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

Functioni

Negative regulator of B-cell activation. Down-regulates cell proliferation (in vitro). Promotes RAC1-dependent membrane ruffle formation and reorganization of the actin cytoskeleton. Regulates cell spreading and cell polarization. Stimulates HDAC1 activity. Regulates LYN activity by modulating its tyrosine phosphorylation.4 Publications

GO - Molecular functioni

GO - Biological processi

  • negative regulation of adaptive immune response Source: UniProtKB
  • negative regulation of B cell activation Source: UniProtKB
  • negative regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
SAM domain-containing protein SAMSN-1
Alternative name(s):
SAM domain, SH3 domain and nuclear localization signals protein 1
SH3 protein expressed in lymphocytes 2
SH3-lymphocyte protein 2
Short name:
SLy2
Gene namesi
Name:Samsn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1914992. Samsn1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB
  • ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice have normal bone marrow B-cell development and normal splenic T- and B-cell populations, but show an enhanced immune response upon immunization. Mice have constitutively activated Lyn, due to constitutive Lyn tyrosine phosphorylation.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231S → A: Loss of phosphorylation site. Strongly reduced interaction with YWHAG and YWHAB. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372SAM domain-containing protein SAMSN-1PRO_0000097575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei90 – 901PhosphoserineCombined sources
Modified residuei97 – 971PhosphoserineCombined sources
Modified residuei160 – 1601PhosphotyrosineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP57725.
MaxQBiP57725.
PaxDbiP57725.
PRIDEiP57725.

PTM databases

iPTMnetiP57725.
PhosphoSiteiP57725.

Expressioni

Tissue specificityi

Detected in spleen and lymph node (at protein level).1 Publication

Inductioni

Up-regulated in peripheral blood B-cells by IL4 and bacterial lipopolysaccharide (LPS).1 Publication

Gene expression databases

BgeeiP57725.
ExpressionAtlasiP57725. baseline and differential.
GenevisibleiP57725. MM.

Interactioni

Subunit structurei

Interacts with FASLG (By similarity). Interacts with phosphotyrosine containing proteins. Interacts (via SH3 domain) with CTTN. Interacts (phosphorylated at Ser-23) with YWHAB, YWHAE, YWHAG, YWHAH, YWHAZ and SFN. Interacts directly with SAP30 and HDAC1. Identified in a complex with SAP30 and HDAC1.By similarity3 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000109877.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi246 – 2516Combined sources
Turni252 – 2543Combined sources
Helixi256 – 2583Combined sources
Helixi259 – 2657Combined sources
Helixi270 – 2734Combined sources
Helixi278 – 2836Combined sources
Turni284 – 2863Combined sources
Helixi289 – 30315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V38NMR-A239-303[»]
ProteinModelPortaliP57725.
SMRiP57725. Positions 162-224, 237-303.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP57725.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini166 – 22257SH3Add
BLAST
Domaini241 – 30565SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi20 – 256Important for interaction with 14-3-3 proteins

Sequence similaritiesi

Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.Curated

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiKOG4384. Eukaryota.
ENOG410ZEDF. LUCA.
GeneTreeiENSGT00390000014672.
HOGENOMiHOG000049202.
HOVERGENiHBG000461.
InParanoidiP57725.
OrthoDBiEOG7KQ20X.
TreeFamiTF350709.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR021090. rSAM/SH3_domain-containing.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF07647. SAM_2. 1 hit.
PF07653. SH3_2. 1 hit.
PF12485. SLY. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P57725-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKRKPSNAS DKEKHQKPKR SSSFGNFDRF RNNSVSKSDD SIEVHDRELT
60 70 80 90 100
NGSEEQSKTS SSGGSLGKKV RAISWTMKKK VGKKYIKALS EEKEEESGEE
110 120 130 140 150
ALPYRNSDPM IGTHTEKISL KASDSMDSLY SGQSSSSGIT SCSDGTSNRD
160 170 180 190 200
SFRLDDDSPY SGPFCGRAKV HTDFTPSPYD TDSLKIKKGD IIDIICKTPM
210 220 230 240 250
GMWTGMLNNK VGNFKFIYVD VILEEEAAPK KIKVPRSRRR ENHQTIQEFL
260 270 280 290 300
ERIHLQEYTS TLLLNGYETL DDLKDIKESH LIELNIADPE DRARLLSAAE
310 320 330 340 350
SLLDEETTVE HEKESVPLSS NPDILSASQL EDCPRDSGCY ISSENSDNGK
360 370
EDLESENLSD MVQKIAITES SD
Length:372
Mass (Da):41,601
Last modified:August 29, 2003 - v2
Checksum:i2264EFEA11B15B30
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 2222MLKRK…PKRSS → MPQTRRNTKNRSAG in AAG23356 (Ref. 1) CuratedAdd
BLAST
Sequence conflicti93 – 931K → E in AAH52906 (PubMed:15489334).Curated
Sequence conflicti164 – 1641F → L in AAH52906 (PubMed:15489334).Curated
Sequence conflicti208 – 2081N → D in AAH64778 (PubMed:15489334).Curated
Sequence conflicti223 – 2231L → S in AAG23356 (Ref. 1) Curated
Sequence conflicti290 – 2901E → D in AAH52906 (PubMed:15489334).Curated
Sequence conflicti320 – 3201S → T in AAH64778 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222928 mRNA. Translation: AAG23356.1.
DQ333189 mRNA. Translation: ABC59720.1.
AK053946 mRNA. Translation: BAC35601.1.
BC052906 mRNA. Translation: AAH52906.1.
BC064778 mRNA. Translation: AAH64778.1.
CCDSiCCDS37378.1.
RefSeqiNP_075869.2. NM_023380.2.
UniGeneiMm.131406.

Genome annotation databases

EnsembliENSMUST00000114239; ENSMUSP00000109877; ENSMUSG00000022876.
GeneIDi67742.
KEGGimmu:67742.
UCSCiuc007zrs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222928 mRNA. Translation: AAG23356.1.
DQ333189 mRNA. Translation: ABC59720.1.
AK053946 mRNA. Translation: BAC35601.1.
BC052906 mRNA. Translation: AAH52906.1.
BC064778 mRNA. Translation: AAH64778.1.
CCDSiCCDS37378.1.
RefSeqiNP_075869.2. NM_023380.2.
UniGeneiMm.131406.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V38NMR-A239-303[»]
ProteinModelPortaliP57725.
SMRiP57725. Positions 162-224, 237-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000109877.

PTM databases

iPTMnetiP57725.
PhosphoSiteiP57725.

Proteomic databases

EPDiP57725.
MaxQBiP57725.
PaxDbiP57725.
PRIDEiP57725.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114239; ENSMUSP00000109877; ENSMUSG00000022876.
GeneIDi67742.
KEGGimmu:67742.
UCSCiuc007zrs.1. mouse.

Organism-specific databases

CTDi64092.
MGIiMGI:1914992. Samsn1.

Phylogenomic databases

eggNOGiKOG4384. Eukaryota.
ENOG410ZEDF. LUCA.
GeneTreeiENSGT00390000014672.
HOGENOMiHOG000049202.
HOVERGENiHBG000461.
InParanoidiP57725.
OrthoDBiEOG7KQ20X.
TreeFamiTF350709.

Miscellaneous databases

EvolutionaryTraceiP57725.
PROiP57725.
SOURCEiSearch...

Gene expression databases

BgeeiP57725.
ExpressionAtlasiP57725. baseline and differential.
GenevisibleiP57725. MM.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR021090. rSAM/SH3_domain-containing.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF07647. SAM_2. 1 hit.
PF07653. SH3_2. 1 hit.
PF12485. SLY. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A mouse homologue of SAMSN1."
    Groet J., Blechschmidt K., Yaspo M.-L., Rosenthal A., Nizetic D.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "SLy: a novel family of putative adaptor proteins in lymphocytes."
    von Holleben M., Kloeter S., Beer S.
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Oviduct.
  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].
    Strain: C57BL/6NCr.
    Tissue: Hematopoietic stem cell.
  5. "The SH3-SAM adaptor HACS1 is up-regulated in B cell activation signaling cascades."
    Zhu Y.X., Benn S., Li Z.H., Wei E., Masih-Khan E., Trieu Y., Bali M., McGlade C.J., Claudio J.O., Stewart A.K.
    J. Exp. Med. 200:737-747(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY IL4 AND LIPOPOLYSACCHARIDE, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TYROSINE PHOSPHORYLATED PROTEINS, TISSUE SPECIFICITY.
  6. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "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-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  10. "Enhanced adaptive immunity in mice lacking the immunoinhibitory adaptor Hacs1."
    Wang D., Stewart A.K., Zhuang L., Zhu Y., Wang Y., Shi C., Keating A., Slutsky A., Zhang H., Wen X.Y.
    FASEB J. 24:947-956(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  11. Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-23, INTERACTION WITH SAP30; HDAC1; YWHAB; YWHAE; YWHAG; YWHAH; YWHAZ AND SFN, SUBUNIT, MUTAGENESIS OF SER-23.
  12. "The immunoinhibitory adapter protein SRC homology domain 3 lymphocyte protein 2 (SLy2) regulates actin dynamics and B cell spreading."
    von Holleben M., Gohla A., Janssen K.P., Iritani B.M., Beer-Hammer S.
    J. Biol. Chem. 286:13489-13501(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTTN.
  13. "Solution structure of the sterile alpha motif (SAM) domain of mouse SAMSN1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 237-303.

Entry informationi

Entry nameiSAMN1_MOUSE
AccessioniPrimary (citable) accession number: P57725
Secondary accession number(s): Q2LE09
, Q5RKU0, Q6P210, Q8C6S2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 29, 2003
Last modified: June 8, 2016
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

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.