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Protein

SAM domain-containing protein SAMSN-1

Gene

Samsn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1914992 Samsn1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Mutagenesisi23S → A: Loss of phosphorylation site. Strongly reduced interaction with YWHAG and YWHAB. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000975751 – 372SAM domain-containing protein SAMSN-1Add BLAST372

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23Phosphoserine1 Publication1
Modified residuei34PhosphoserineBy similarity1
Modified residuei74PhosphoserineBy similarity1
Modified residuei76PhosphothreonineBy similarity1
Modified residuei90PhosphoserineCombined sources1
Modified residuei97PhosphoserineCombined sources1
Modified residuei119PhosphoserineBy similarity1
Modified residuei160PhosphotyrosineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP57725
MaxQBiP57725
PaxDbiP57725
PRIDEiP57725

PTM databases

iPTMnetiP57725
PhosphoSitePlusiP57725

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

BgeeiENSMUSG00000022876
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

1372
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi246 – 251Combined sources6
Turni252 – 254Combined sources3
Helixi256 – 258Combined sources3
Helixi259 – 265Combined sources7
Helixi270 – 273Combined sources4
Helixi278 – 283Combined sources6
Turni284 – 286Combined sources3
Helixi289 – 303Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V38NMR-A239-303[»]
ProteinModelPortaliP57725
SMRiP57725
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP57725

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini163 – 224SH3PROSITE-ProRule annotationAdd BLAST62
Domaini241 – 305SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi20 – 25Important for interaction with 14-3-3 proteins6

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiKOG4384 Eukaryota
ENOG410ZEDF LUCA
GeneTreeiENSGT00390000014672
HOGENOMiHOG000049202
HOVERGENiHBG000461
InParanoidiP57725
TreeFamiTF350709

Family and domain databases

CDDicd09561 SAM_SAMSN1, 1 hit
InterProiView protein in InterPro
IPR021090 rSAM/SH3_domain-containing
IPR001660 SAM
IPR013761 SAM/pointed_sf
IPR037623 SAMSN1_SAM
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
PfamiView protein in Pfam
PF07647 SAM_2, 1 hit
PF07653 SH3_2, 1 hit
PF12485 SLY, 1 hit
SMARTiView protein in SMART
SM00454 SAM, 1 hit
SM00326 SH3, 1 hit
SUPFAMiSSF47769 SSF47769, 1 hit
SSF50044 SSF50044, 1 hit
PROSITEiView protein in PROSITE
PS50105 SAM_DOMAIN, 1 hit
PS50002 SH3, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 22MLKRK…PKRSS → MPQTRRNTKNRSAG in AAG23356 (Ref. 1) CuratedAdd BLAST22
Sequence conflicti93K → E in AAH52906 (PubMed:15489334).Curated1
Sequence conflicti164F → L in AAH52906 (PubMed:15489334).Curated1
Sequence conflicti208N → D in AAH64778 (PubMed:15489334).Curated1
Sequence conflicti223L → S in AAG23356 (Ref. 1) Curated1
Sequence conflicti290E → D in AAH52906 (PubMed:15489334).Curated1
Sequence conflicti320S → T in AAH64778 (PubMed:15489334).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiSAMN1_MOUSE
AccessioniPrimary (citable) accession number: P57725
Secondary accession number(s): Q2LE09
, Q5RKU0, Q6P210, Q8C6S2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 29, 2003
Last modified: May 23, 2018
This is version 123 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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