Q6SPF0 (SAMD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Atherin

Alternative name(s):
Sterile alpha motif domain-containing protein 1
Short name=SAM domain-containing protein 1

Gene names

Name:

SAMD1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	538 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in atherogenesis by immobilizing LDL in the atherial wall. Ref.1
Subcellular location	Cytoplasm. Secreted Ref.1.
Tissue specificity	Expressed in atherosclerotic lesions, not in normal intima. Ref.1
Sequence similarities	Contains 1 SAM (sterile alpha motif) domain.
Caution	Due to its high GC content it turned out to be difficult to sequence the 5' end of the gene encoding the N-terminal proline-rich region of the protein and to unambiguously determine which sequence is correct. We display the sequence described in Ref.1. This sequence fits better with orthologous sequences but is not consistent with the human reference genome sequence.

Ontologies

Keywords
Cellular component	Cytoplasm Secreted
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 538	538	Atherin		PRO_0000279494
Regions
	Domain	462 – 530	69	SAM
	Compositional bias	101 – 235	135	Pro-rich
	Compositional bias	327 – 332	6	Poly-Glu
Amino acid modifications
	Modified residue	107	1	Phosphothreonine Ref.5 Ref.8 Ref.10
	Modified residue	161	1	Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
	Modified residue	261	1	Phosphoserine Ref.8
	Modified residue	315	1	Phosphoserine Ref.5
	Modified residue	345	1	Phosphoserine Ref.5
Natural variations
	Natural variant	340	1	E → D. Corresponds to variant rs8062 [ dbSNP | Ensembl ].		VAR_061701
Experimental info
	Sequence conflict	111 – 216	106	Missing in AC022098. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q6SPF0 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 083A170790654F2F	FASTA	538	56,052
	10 20 30 40 50 60 MAGPPALPPP ETAAAATTAA AASSSAASPH YQEWILDTID SLRSRKARPD LERICRMVRR 70 80 90 100 110 120 RHGPEPERTR AELEKLIQQR AVLRVSYKGS ISYRNAARVQ PPRRGATPPA PPRAPRGAPA 130 140 150 160 170 180 AAAAAAPPPT PAPPPPPAPV AAAAPARAPR AAAAAATAPP SPGPAQPGPR AQRAAPLAAP 190 200 210 220 230 240 PPAPAAPPAV APPAGPRRAP PPAVAAREPP LPPPPQPPAP PQQQQPPPPQ PQPPPEGGAV 250 260 270 280 290 300 RAGGAARPVS LREVVRYLGG SGGAGGRLTR GRVQGLLEEE AAARGRLERT RLGALALPRG 310 320 330 340 350 360 DRPGRAPPAA SARPSRSKRG GEERVLEKEE EEDDDEDEDE EDDVSEGSEV PESDRPAGAQ 370 380 390 400 410 420 HHQLNGERGP QSAKERVKEW TPCGPHQGQD EGRGPAPGSG TRQVFSMAAM NKEGGTASVA 430 440 450 460 470 480 TGPDSPSPVP LPPGKPALPG ADGTPFGCPP GRKEKPSDPV EWTVMDVVEY FTEAGFPEQA 490 500 510 520 530 TAFQEQEIDG KSLLLMQRTD VLTGLSIRLG PALKIYEHHI KVLQQGHFED DDPDGFLG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Atherin: a newly identified, lesion-specific, LDL-binding protein in human atherosclerosis." Lees A.M., Deconinck A.E., Campbell B.D., Lees R.S. Atherosclerosis 182:219-230(2005) [PubMed: 16159594] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION. Tissue: Aorta.
[2]	"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: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 244-538. Tissue: Lung, Lymph and Ovary.
[4]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107; SER-161; SER-315 AND SER-345, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107; SER-161 AND SER-261, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107 AND SER-161, MASS SPECTROMETRY. Tissue: Leukemic T-cell.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY453840 mRNA. Translation: AAR24087.1. AC022098 Genomic DNA. No translation available. BC007384 mRNA. Translation: AAH07384.2. BC030129 mRNA. Translation: AAH30129.1. BC065477 mRNA. Translation: AAH65477.1. BC080588 mRNA. Translation: AAH80588.1.
IPI	IPI00395474.
RefSeq	NP_612361.1. NM_138352.1.
UniGene	Hs.140309.
3D structure databases
HSSP	HSSP built from PDB template 1PK1 based on UniProtKB P39769.
ProteinModelPortal	Q6SPF0.
SMR	Q6SPF0. Positions 457-522.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6SPF0.
PTM databases
PhosphoSite	Q6SPF0.
Polymorphism databases
DMDM	74749329.
Proteomic databases
PRIDE	Q6SPF0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	90378.
KEGG	hsa:90378.
UCSC	uc002mya.1. human.
Organism-specific databases
CTD	90378.
GeneCards	GC19M014199.
H-InvDB	HIX0202906.
HGNC	HGNC:17958. SAMD1.
neXtProt	NX_Q6SPF0.
PharmGKB	PA34937.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14785.
InParanoid	Q6SPF0.
Gene expression databases
CleanEx	HS_SAMD1.
Genevestigator	Q6SPF0.
Family and domain databases
InterPro	IPR001660. SAM. IPR013761. SAM/pointed. IPR021129. SAM_type1. [Graphical view]
Gene3D	G3DSA:1.10.150.50. SAM_type. 1 hit.
Pfam	PF00536. SAM_1. 1 hit. [Graphical view]
SMART	SM00454. SAM. 1 hit. [Graphical view]
SUPFAM	SSF47769. SAM_homology. 1 hit.
PROSITE	PS50105. SAM_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	76709.

Entry information

Entry name

SAMD1_HUMAN

Accession

Primary (citable) accession number: Q6SPF0
Secondary accession number(s): Q6P0R3, Q6PIS7, Q96IM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	July 5, 2004
Last modified:	December 14, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.