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Q9NSI8 (SAMN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SAM domain-containing protein SAMSN-1
Alternative name(s):
Hematopoietic adaptor containing SH3 and SAM domains 1
Nash1
SAM domain, SH3 domain and nuclear localization signals protein 1
SH3-SAM adaptor protein
Gene names
Name:SAMSN1
Synonyms:HACS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. Ref.8

Subunit structure

Interacts with FASLG. 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 similarity. Ref.9

Subcellular location

Nucleus. Cytoplasm By similarity. Cell projectionruffle By similarity. Note: Shuttles between cytoplasm and nucleus. Colocalizes with the actin cytoskeleton and actin-rich membrane ruffles By similarity. Ref.7

Tissue specificity

Detected in peripheral blood B-cells (at protein level). Detected in spleen, liver and peripheral blood. Ref.7 Ref.8

Induction

Up-regulated in peripheral blood B-cells by IL4, IL13 and by CD40 stimulation. Ref.8

Sequence similarities

Contains 1 SAM (sterile alpha motif) domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAK07746.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NSI8-1)

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.
Isoform 2 (identifier: Q9NSI8-2)

Also known as: b;

The sequence of this isoform differs from the canonical sequence as follows:
     19-186: Missing.
Isoform 3 (identifier: Q9NSI8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MLKRKPSNVSEKEKHQKPK → MEIRLDTLSA...CSDMDLLHSW

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 373373SAM domain-containing protein SAMSN-1
PRO_0000097574

Regions

Domain166 – 22257SH3
Domain241 – 30565SAM
Motif20 – 256Important for interaction with 14-3-3 proteins By similarity

Amino acid modifications

Modified residue901Phosphoserine By similarity
Modified residue1601Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 1919MLKRK…HQKPK → MEIRLDTLSASLGRSSTLNN CNLEDKLAWYEGEAYMWHHW KPFPENPLWTCLDFQIAQVG PWDHCSSCIRHTRLKSSCSD MDLLHSW in isoform 3.
VSP_008120
Alternative sequence19 – 186168Missing in isoform 2.
VSP_008119
Natural variant631G → A.
Corresponds to variant rs34607574 [ dbSNP | Ensembl ].
VAR_051331

Experimental info

Sequence conflict1051R → G in BAG54155. Ref.4
Isoform 3:
Sequence conflict201N → D in AAK07746. Ref.2
Sequence conflict641H → Y in AAK07746. Ref.2

Secondary structure

.............. 373
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 964B852ADBA2D777

FASTA37341,708
        10         20         30         40         50         60 
MLKRKPSNVS EKEKHQKPKR SSSFGNFDRF RNNSLSKPDD STEAHEGDPT NGSGEQSKTS 

        70         80         90        100        110        120 
NNGGGLGKKM RAISWTMKKK VGKKYIKALS EEKDEEDGEN AHPYRNSDPV IGTHTEKVSL 

       130        140        150        160        170        180 
KASDSMDSLY SGQSSSSGIT SCSDGTSNRD SFRLDDDGPY SGPFCGRARV HTDFTPSPYD 

       190        200        210        220        230        240 
TDSLKIKKGD IIDIICKTPM GMWTGMLNNK VGNFKFIYVD VISEEEAAPK KIKANRRSNS 

       250        260        270        280        290        300 
KKSKTLQEFL ERIHLQEYTS TLLLNGYETL EDLKDIKESH LIELNIENPD DRRRLLSAAE 

       310        320        330        340        350        360 
NFLEEEIIQE QENEPEPLSL SSDISLNKSQ LDDCPRDSGC YISSGNSDNG KEDLESENLS 

       370 
DMVHKIIITE PSD 

« Hide

Isoform 2 (b) [UniParc].

Checksum: 362B2FB490B972BE
Show »

FASTA20523,466
Isoform 3 [UniParc].

Checksum: C2757916D880F563
Show »

FASTA44149,627

References

« Hide 'large scale' references
[1]"A novel gene, located on human chromosome 21q11."
Groet J., Blechschmidt K., Yaspo M., Rosenthal A., Nizetic D.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"HACS1 encodes a novel SH3-SAM adaptor protein differentially expressed in normal and malignant hematopoietic cells."
Claudio J.O., Zhu Y.X., Benn S.J., Shukla A.H., McGlade C.J., Falcioni N., Stewart A.K.
Oncogene 20:5373-5377(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]"Transcriptional map of the juxtacentromeric region of human chromosome 21."
Brun M.-E., Ruault M., Roizes G., De Sario A.
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Thymus.
[4]"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. expand/collapse author list , 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].
[5]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
Tissue: Lymph.
[7]"Identification of Nash1, a novel protein containing a nuclear localization signal, a sterile alpha motif, and an SH3 domain preferentially expressed in mast cells."
Uchida T., Nakao A., Nakano N., Kuramasu A., Saito H., Okumura K., Ra C., Ogawa H.
Biochem. Biophys. Res. Commun. 288:137-141(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"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, TISSUE SPECIFICITY.
[9]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"NMR solution structure of the HACS1 SH3 domain."
Donaldson L.
Submitted (FEB-2010) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 162-224.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF222927 mRNA. Translation: AAG23355.1.
AF218085 mRNA. Translation: AAK07746.1. Different initiation.
AF519621 mRNA. Translation: AAM75349.1.
AK125144 mRNA. Translation: BAG54155.1.
AL163206 Genomic DNA. Translation: CAB90391.1.
AF165138 Genomic DNA. No translation available.
BC029112 mRNA. Translation: AAH29112.1.
CCDSCCDS42906.1. [Q9NSI8-1]
RefSeqNP_001243299.1. NM_001256370.1. [Q9NSI8-3]
NP_001273452.1. NM_001286523.1.
NP_071419.3. NM_022136.4. [Q9NSI8-1]
UniGeneHs.473341.
Hs.719474.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KEANMR-A162-224[»]
ProteinModelPortalQ9NSI8.
SMRQ9NSI8. Positions 162-224, 234-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122054. 12 interactions.
IntActQ9NSI8. 2 interactions.
STRING9606.ENSP00000383411.

PTM databases

PhosphoSiteQ9NSI8.

Polymorphism databases

DMDM12230638.

Proteomic databases

MaxQBQ9NSI8.
PaxDbQ9NSI8.
PRIDEQ9NSI8.

Protocols and materials databases

DNASU64092.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285670; ENSP00000285670; ENSG00000155307.
ENST00000400564; ENSP00000383409; ENSG00000155307. [Q9NSI8-2]
ENST00000400566; ENSP00000383411; ENSG00000155307. [Q9NSI8-1]
GeneID64092.
KEGGhsa:64092.
UCSCuc002yju.2. human. [Q9NSI8-1]
uc010gky.2. human. [Q9NSI8-2]

Organism-specific databases

CTD64092.
GeneCardsGC21M015857.
H-InvDBHIX0016027.
HGNCHGNC:10528. SAMSN1.
HPAHPA010645.
HPA017055.
MIM607978. gene.
neXtProtNX_Q9NSI8.
PharmGKBPA34939.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG293245.
HOGENOMHOG000049202.
HOVERGENHBG000461.
OMAGPYSGPF.
OrthoDBEOG7KQ20X.
PhylomeDBQ9NSI8.
TreeFamTF350709.

Gene expression databases

ArrayExpressQ9NSI8.
BgeeQ9NSI8.
CleanExHS_SAMSN1.
GenevestigatorQ9NSI8.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
InterProIPR021090. rSAM/SH3_domain-containing.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF07647. SAM_2. 1 hit.
PF07653. SH3_2. 1 hit.
PF12485. SLY. 1 hit.
[Graphical view]
SMARTSM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NSI8.
GenomeRNAi64092.
NextBio65904.
PROQ9NSI8.
SOURCESearch...

Entry information

Entry nameSAMN1_HUMAN
AccessionPrimary (citable) accession number: Q9NSI8
Secondary accession number(s): B3KWJ3 expand/collapse secondary AC list , F8WAA1, Q8NFF7, Q9C041
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM