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Protein

Smoothelin

Gene

SMTN

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

Functioni

Structural protein of the cytoskeleton.

GO - Molecular functioni

  • actin binding Source: ProtInc
  • structural constituent of muscle Source: ProtInc

GO - Biological processi

  • muscle organ development Source: ProtInc
  • smooth muscle contraction Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Smoothelin
Gene namesi
Name:SMTN
Synonyms:SMSMO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:11126. SMTN.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: ProtInc
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35975.

Polymorphism and mutation databases

BioMutaiSMTN.
DMDMi338817991.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 917916SmoothelinPRO_0000071976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei299 – 2991PhosphoserineCombined sources
Modified residuei301 – 3011PhosphoserineCombined sources
Modified residuei304 – 3041PhosphoserineCombined sources
Modified residuei341 – 3411PhosphoserineCombined sources
Modified residuei351 – 3511PhosphothreonineCombined sources
Modified residuei357 – 3571PhosphoserineCombined sources
Modified residuei360 – 3601PhosphothreonineCombined sources
Modified residuei373 – 3731PhosphothreonineCombined sources
Modified residuei503 – 5031PhosphoserineCombined sources
Modified residuei514 – 5141PhosphoserineCombined sources
Modified residuei523 – 5231PhosphoserineCombined sources
Modified residuei576 – 5761PhosphoserineCombined sources
Modified residuei729 – 7291PhosphoserineCombined sources
Modified residuei792 – 7921PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP53814.
MaxQBiP53814.
PaxDbiP53814.
PeptideAtlasiP53814.
PRIDEiP53814.

PTM databases

iPTMnetiP53814.
PhosphoSiteiP53814.

Expressioni

Tissue specificityi

Smooth muscle; contractile or vascular (for the long form).

Gene expression databases

BgeeiP53814.
ExpressionAtlasiP53814. baseline and differential.
GenevisibleiP53814. HS.

Organism-specific databases

HPAiCAB001721.
HPA051778.
HPA058590.

Interactioni

GO - Molecular functioni

  • actin binding Source: ProtInc

Protein-protein interaction databases

BioGridi112416. 8 interactions.
IntActiP53814. 6 interactions.
STRINGi9606.ENSP00000351593.

Structurei

Secondary structure

1
917
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi801 – 81212Combined sources
Beta strandi813 – 8153Combined sources
Turni824 – 8296Combined sources
Helixi832 – 84110Combined sources
Turni843 – 8453Combined sources
Helixi856 – 86813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D87NMR-A801-868[»]
ProteinModelPortaliP53814.
SMRiP53814. Positions 794-905.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53814.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini799 – 903105CHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili24 – 8966Sequence analysisAdd
BLAST
Coiled coili603 – 63028Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi194 – 28289Pro-richAdd
BLAST
Compositional biasi710 – 7156Poly-Ser

Sequence similaritiesi

Belongs to the smoothelin family.Curated
Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4678. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOVERGENiHBG076678.
InParanoidiP53814.
OrthoDBiEOG7C2R13.
TreeFamiTF316716.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR022189. SMTN.
[Graphical view]
PfamiPF00307. CH. 1 hit.
PF12510. Smoothelin. 3 hits.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform B (identifier: P53814-1) [UniParc]FASTAAdd to basket

Also known as: Long, B1, L1

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.

« Hide

        10         20         30         40         50
MADEALAGLD EGALRKLLEV TADLAERRRI RSAIRELQRQ ELEREEEALA
60 70 80 90 100
SKRFRAERQD NKENWLHSQQ REAEQRAALA RLAGQLESMN DVEELTALLR
110 120 130 140 150
SAGEYEERKL IRAAIRRVRA QEIEAATLAG RLYSGRPNSG SREDSKGLAA
160 170 180 190 200
HRLEQCEVPE REEQEQQAEV SKPTPTPEGT SQDVTTVTLL LRAPPGSTSS
210 220 230 240 250
SPASPSSSPT PASPEPPLEP AEAQCLTAEV PGSPEPPPSP PKTTSPEPQE
260 270 280 290 300
SPTLPSTEGQ VVNKLLSGPK ETPAAQSPTR GPSDTKRADV AGPRPCQRSL
310 320 330 340 350
SVLSPRQPAQ NRESTPLASG PSSFQRAGSV RDRVHKFTSD SPMAARLQDG
360 370 380 390 400
TPQAALSPLT PARLLGPSLT STTPASSSSG SSSRGPSDTS SRFSKEQRGV
410 420 430 440 450
AQPLAQLRSC PQEEGPRGRG LAARPLENRA GGPVARSEEP GAPLPVAVGT
460 470 480 490 500
AEPGGSMKTT FTIEIKDGRG QASTGRVLLP TGNQRAELTL GLRAPPTLLS
510 520 530 540 550
TSSGGKSTIT RVNSPGTLAR LGSVTHVTSF SHAPPSSRGG CSIKMEAEPA
560 570 580 590 600
EPLAAAVEAA NGAEQTRVNK APEGRSPLSA EELMTIEDEG VLDKMLDQST
610 620 630 640 650
DFEERKLIRA ALRELRQRKR DQRDKERERR LQEARGRPGE GRGNTATETT
660 670 680 690 700
TRHSQRAADG SAVSTVTKTE RLVHSNDGTR TARTTTVESS FVRRSENGSG
710 720 730 740 750
STMMQTKTFS SSSSSKKMGS IFDREDQASP RAGSLAALEK RQAEKKKELM
760 770 780 790 800
KAQSLPKTSA SQARKAMIEK LEKEGAAGSP GGPRAAVQRS TSFGVPNANS
810 820 830 840 850
IKQMLLDWCR AKTRGYEHVD IQNFSSSWSD GMAFCALVHN FFPEAFDYGQ
860 870 880 890 900
LSPQNRRQNF EVAFSSAEML VDCVPLVEVD DMMIMGKKPD PKCVFTYVQS
910
LYNHLRRHEL RLRGKNV
Length:917
Mass (Da):99,059
Last modified:June 28, 2011 - v7
Checksum:iEC508A8239AA6B36
GO
Isoform A (identifier: P53814-2) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-456: Missing.

Note: Produced by alternative promoter usage.
Show »
Length:461
Mass (Da):50,572
Checksum:iFE6EDC0D644E1B5D
GO
Isoform B2 (identifier: P53814-5) [UniParc]FASTAAdd to basket

Also known as: L2

The sequence of this isoform differs from the canonical sequence as follows:
     869-917: MLVDCVPLVE...HELRLRGKNV → THADCPQLLD...QKGLVKTKKS

Show »
Length:915
Mass (Da):98,919
Checksum:iFF0ABC36BBEC9B30
GO
Isoform B3 (identifier: P53814-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     868-868: E → ETHADCPQLLDTEDMVRLREPDWK

Show »
Length:940
Mass (Da):101,810
Checksum:iE9C48F69CEEE2847
GO

Sequence cautioni

The sequence AAL36149.1 differs from that shown. Reason: Frameshift at positions 362 and 384. Curated
The sequence AAL36150.1 differs from that shown. Reason: Frameshift at positions 362 and 384. Curated
The sequence CAA73884.2 differs from that shown. Reason: Frameshift at positions 362 and 384. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti279 – 2791T → P in AAF03562 (PubMed:12176134).Curated
Sequence conflicti279 – 2791T → P in AAL36149 (PubMed:12176134).Curated
Sequence conflicti279 – 2791T → P in AAL36150 (PubMed:12176134).Curated
Sequence conflicti279 – 2791T → P in CAA73884 (PubMed:12176134).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti455 – 4551G → D.4 Publications
Corresponds to variant rs1064178 [ dbSNP | Ensembl ].
VAR_038785
Natural varianti547 – 5471A → P.4 Publications
Corresponds to variant rs3205187 [ dbSNP | Ensembl ].
VAR_038786
Natural varianti559 – 5591A → V.
Corresponds to variant rs5997872 [ dbSNP | Ensembl ].
VAR_038787
Natural varianti580 – 5801A → T.
Corresponds to variant rs12158015 [ dbSNP | Ensembl ].
VAR_038788
Natural varianti637 – 6371R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
Corresponds to variant rs777851029 [ dbSNP | Ensembl ].
VAR_035657
Natural varianti642 – 6421R → C.
Corresponds to variant rs34292278 [ dbSNP | Ensembl ].
VAR_062223
Natural varianti763 – 7631A → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035658

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 456456Missing in isoform A. 2 PublicationsVSP_004398Add
BLAST
Alternative sequencei868 – 8681E → ETHADCPQLLDTEDMVRLRE PDWK in isoform B3. 1 PublicationVSP_031242
Alternative sequencei869 – 91749MLVDC…RGKNV → THADCPQLLDTEDMVRLREP DWKCVYTYIQEFYRCLVQKG LVKTKKS in isoform B2. 4 PublicationsVSP_007020Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49989 mRNA. Translation: CAA90281.2.
AJ010306 mRNA. Translation: CAA09077.2.
Y13492 mRNA. Translation: CAA73884.2. Frameshift.
AY061971 mRNA. Translation: AAL36149.1. Frameshift.
AY061972 mRNA. Translation: AAL36150.1. Frameshift.
AF115570
, AF115552, AF115553, AF115554, AF115555, AF115556, AF115557, AF115558, AF115559, AF115560, AF115561, AF115562, AF115563, AF115564, AF115565, AF115566, AF115567, AF115568, AF115569 Genomic DNA. Translation: AAF03562.1.
AF115570
, AF115560, AF115561, AF115562, AF115563, AF115564, AF115565, AF115566, AF115567, AF115568, AF115569 Genomic DNA. Translation: AAF03563.1.
AF064238 mRNA. Translation: AAF01481.3.
AC005005 Genomic DNA. Translation: AAD15619.1.
CH471095 Genomic DNA. Translation: EAW59930.1.
BC034237 mRNA. Translation: AAH34237.1.
CCDSiCCDS13886.1. [P53814-1]
CCDS13887.1. [P53814-6]
CCDS13888.1. [P53814-5]
PIRiT09575.
RefSeqiNP_001193946.1. NM_001207017.1.
NP_001193947.1. NM_001207018.1.
NP_008863.3. NM_006932.4. [P53814-1]
NP_599031.1. NM_134269.2. [P53814-5]
NP_599032.2. NM_134270.2. [P53814-6]
UniGeneiHs.149098.

Genome annotation databases

EnsembliENST00000333137; ENSP00000329532; ENSG00000183963. [P53814-5]
ENST00000347557; ENSP00000328635; ENSG00000183963. [P53814-1]
ENST00000358743; ENSP00000351593; ENSG00000183963. [P53814-6]
GeneIDi6525.
KEGGihsa:6525.
UCSCiuc003ajk.3. human. [P53814-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49989 mRNA. Translation: CAA90281.2.
AJ010306 mRNA. Translation: CAA09077.2.
Y13492 mRNA. Translation: CAA73884.2. Frameshift.
AY061971 mRNA. Translation: AAL36149.1. Frameshift.
AY061972 mRNA. Translation: AAL36150.1. Frameshift.
AF115570
, AF115552, AF115553, AF115554, AF115555, AF115556, AF115557, AF115558, AF115559, AF115560, AF115561, AF115562, AF115563, AF115564, AF115565, AF115566, AF115567, AF115568, AF115569 Genomic DNA. Translation: AAF03562.1.
AF115570
, AF115560, AF115561, AF115562, AF115563, AF115564, AF115565, AF115566, AF115567, AF115568, AF115569 Genomic DNA. Translation: AAF03563.1.
AF064238 mRNA. Translation: AAF01481.3.
AC005005 Genomic DNA. Translation: AAD15619.1.
CH471095 Genomic DNA. Translation: EAW59930.1.
BC034237 mRNA. Translation: AAH34237.1.
CCDSiCCDS13886.1. [P53814-1]
CCDS13887.1. [P53814-6]
CCDS13888.1. [P53814-5]
PIRiT09575.
RefSeqiNP_001193946.1. NM_001207017.1.
NP_001193947.1. NM_001207018.1.
NP_008863.3. NM_006932.4. [P53814-1]
NP_599031.1. NM_134269.2. [P53814-5]
NP_599032.2. NM_134270.2. [P53814-6]
UniGeneiHs.149098.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D87NMR-A801-868[»]
ProteinModelPortaliP53814.
SMRiP53814. Positions 794-905.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112416. 8 interactions.
IntActiP53814. 6 interactions.
STRINGi9606.ENSP00000351593.

PTM databases

iPTMnetiP53814.
PhosphoSiteiP53814.

Polymorphism and mutation databases

BioMutaiSMTN.
DMDMi338817991.

Proteomic databases

EPDiP53814.
MaxQBiP53814.
PaxDbiP53814.
PeptideAtlasiP53814.
PRIDEiP53814.

Protocols and materials databases

DNASUi6525.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333137; ENSP00000329532; ENSG00000183963. [P53814-5]
ENST00000347557; ENSP00000328635; ENSG00000183963. [P53814-1]
ENST00000358743; ENSP00000351593; ENSG00000183963. [P53814-6]
GeneIDi6525.
KEGGihsa:6525.
UCSCiuc003ajk.3. human. [P53814-1]

Organism-specific databases

CTDi6525.
GeneCardsiSMTN.
H-InvDBHIX0016383.
HGNCiHGNC:11126. SMTN.
HPAiCAB001721.
HPA051778.
HPA058590.
MIMi602127. gene.
neXtProtiNX_P53814.
PharmGKBiPA35975.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4678. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOVERGENiHBG076678.
InParanoidiP53814.
OrthoDBiEOG7C2R13.
TreeFamiTF316716.

Miscellaneous databases

ChiTaRSiSMTN. human.
EvolutionaryTraceiP53814.
GeneWikiiSMTN.
GenomeRNAii6525.
PROiP53814.
SOURCEiSearch...

Gene expression databases

BgeeiP53814.
ExpressionAtlasiP53814. baseline and differential.
GenevisibleiP53814. HS.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR022189. SMTN.
[Graphical view]
PfamiPF00307. CH. 1 hit.
PF12510. Smoothelin. 3 hits.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Smoothelin, a novel cytoskeletal protein specific for smooth muscle cells."
    van der Loop F.T.L., Schaart G., Timmer E.D.J., Ramaekers F.C.S., van Eys G.J.J.M.
    J. Cell Biol. 134:401-411(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    Tissue: Colon smooth muscle.
  2. Rensen S.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO N-TERMINUS.
  3. "A novel isoform of the smooth muscle cell differentiation marker smoothelin."
    Kraemer J., Aguirre-Arteta A.M., Thiel C., Gross M.C., Dietz R., Cardoso M.C., Leonhardt H.
    J. Mol. Med. 77:294-298(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), VARIANTS ASP-455 AND PRO-547.
    Tissue: Fetus.
  4. "Identification and characterization of novel smoothelin isoforms in vascular smooth muscle."
    Kraemer J., Quensel C., Meding J., Cardoso M.C., Leonhardt H.
    J. Vasc. Res. 38:120-132(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND B2), VARIANT ASP-455.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A; B; B2 AND B3), ALTERNATIVE PROMOTER USAGE, VARIANT ASP-455.
    Tissue: Vascular smooth muscle.
  6. Kraemer J., Arteta-Aguirre A.M., Cardoso M.C., Leonhardt H.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B2), VARIANTS ASP-455 AND PRO-547.
  7. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-547.
  9. "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 B2), VARIANT PRO-547.
    Tissue: Uterus.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-304; SER-341; THR-373; SER-503; SER-514; SER-576 AND SER-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-357 AND THR-360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-299; SER-301; SER-304; THR-351; SER-357; THR-360; THR-373 AND SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-304; SER-341; SER-514; SER-523; SER-729 AND SER-792, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  15. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-637 AND VAL-763.

Entry informationi

Entry nameiSMTN_HUMAN
AccessioniPrimary (citable) accession number: P53814
Secondary accession number(s): O00569
, O95769, O95937, Q8N4H8, Q8WWW1, Q8WWW2, Q9P1S8, Q9UIT1, Q9UIT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 28, 2011
Last modified: July 6, 2016
This is version 151 of the entry and version 7 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.