Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Atherin

Gene

SAMD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in atherogenesis by immobilizing LDL in the atherial wall.1 Publication

Names & Taxonomyi

Protein namesi
Recommended name:
Atherin
Alternative name(s):
Sterile alpha motif domain-containing protein 1
Short name:
SAM domain-containing protein 1
Gene namesi
Name:SAMD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:17958. SAMD1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34937.

Polymorphism and mutation databases

BioMutaiSAMD1.
DMDMi74749329.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538AtherinPRO_0000279494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611PhosphoserineCombined sources
Modified residuei261 – 2611PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6SPF0.
MaxQBiQ6SPF0.
PaxDbiQ6SPF0.
PRIDEiQ6SPF0.

PTM databases

iPTMnetiQ6SPF0.
PhosphoSiteiQ6SPF0.

Expressioni

Tissue specificityi

Expressed in atherosclerotic lesions, not in normal intima.1 Publication

Gene expression databases

CleanExiHS_SAMD1.

Organism-specific databases

HPAiHPA049059.

Interactioni

Protein-protein interaction databases

BioGridi124704. 52 interactions.
IntActiQ6SPF0. 27 interactions.
MINTiMINT-4991013.
STRINGi9606.ENSP00000431971.

Structurei

3D structure databases

ProteinModelPortaliQ6SPF0.
SMRiQ6SPF0. Positions 457-515.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini462 – 53069SAMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi101 – 235135Pro-richAdd
BLAST
Compositional biasi327 – 3326Poly-Glu

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IX26. Eukaryota.
ENOG4111QIZ. LUCA.
InParanoidiQ6SPF0.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6SPF0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGPPALPPP ETAAAATTAA AASSSAASPH YQEWILDTID SLRSRKARPD
60 70 80 90 100
LERICRMVRR RHGPEPERTR AELEKLIQQR AVLRVSYKGS ISYRNAARVQ
110 120 130 140 150
PPRRGATPPA PPRAPRGAPA AAAAAAPPPT PAPPPPPAPV AAAAPARAPR
160 170 180 190 200
AAAAAATAPP SPGPAQPGPR AQRAAPLAAP PPAPAAPPAV APPAGPRRAP
210 220 230 240 250
PPAVAAREPP LPPPPQPPAP PQQQQPPPPQ PQPPPEGGAV RAGGAARPVS
260 270 280 290 300
LREVVRYLGG SGGAGGRLTR GRVQGLLEEE AAARGRLERT RLGALALPRG
310 320 330 340 350
DRPGRAPPAA SARPSRSKRG GEERVLEKEE EEDDDEDEDE EDDVSEGSEV
360 370 380 390 400
PESDRPAGAQ HHQLNGERGP QSAKERVKEW TPCGPHQGQD EGRGPAPGSG
410 420 430 440 450
TRQVFSMAAM NKEGGTASVA TGPDSPSPVP LPPGKPALPG ADGTPFGCPP
460 470 480 490 500
GRKEKPSDPV EWTVMDVVEY FTEAGFPEQA TAFQEQEIDG KSLLLMQRTD
510 520 530
VLTGLSIRLG PALKIYEHHI KVLQQGHFED DDPDGFLG
Length:538
Mass (Da):56,052
Last modified:July 5, 2004 - v1
Checksum:i083A170790654F2F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 216106Missing in AC022098 (PubMed:15057824).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti340 – 3401E → D.
Corresponds to variant rs8062 [ dbSNP | Ensembl ].
VAR_061701

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_612361.1. NM_138352.1.
UniGeneiHs.140309.

Genome annotation databases

GeneIDi90378.
KEGGihsa:90378.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_612361.1. NM_138352.1.
UniGeneiHs.140309.

3D structure databases

ProteinModelPortaliQ6SPF0.
SMRiQ6SPF0. Positions 457-515.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124704. 52 interactions.
IntActiQ6SPF0. 27 interactions.
MINTiMINT-4991013.
STRINGi9606.ENSP00000431971.

PTM databases

iPTMnetiQ6SPF0.
PhosphoSiteiQ6SPF0.

Polymorphism and mutation databases

BioMutaiSAMD1.
DMDMi74749329.

Proteomic databases

EPDiQ6SPF0.
MaxQBiQ6SPF0.
PaxDbiQ6SPF0.
PRIDEiQ6SPF0.

Protocols and materials databases

DNASUi90378.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi90378.
KEGGihsa:90378.

Organism-specific databases

CTDi90378.
GeneCardsiSAMD1.
H-InvDBHIX0202906.
HGNCiHGNC:17958. SAMD1.
HPAiHPA049059.
neXtProtiNX_Q6SPF0.
PharmGKBiPA34937.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IX26. Eukaryota.
ENOG4111QIZ. LUCA.
InParanoidiQ6SPF0.

Miscellaneous databases

GenomeRNAii90378.
NextBioi76709.
PROiQ6SPF0.

Gene expression databases

CleanExiHS_SAMD1.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161 AND SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSAMD1_HUMAN
AccessioniPrimary (citable) accession number: Q6SPF0
Secondary accession number(s): Q6P0R3, Q6PIS7, Q96IM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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 PubMed:16159594. This sequence fits better with orthologous sequences but is not consistent with the human reference genome sequence.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. 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.