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O15061

- SYNEM_HUMAN

UniProt

O15061 - SYNEM_HUMAN

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Protein

Synemin

Gene

SYNM

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

Functioni

Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteropolymeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteropolymeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells.3 Publications

GO - Molecular functioni

  1. intermediate filament binding Source: UniProtKB
  2. structural constituent of cytoskeleton Source: UniProtKB
  3. structural constituent of muscle Source: UniProtKB
  4. vinculin binding Source: UniProtKB

GO - Biological processi

  1. intermediate filament cytoskeleton organization Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Synemin
Alternative name(s):
Desmuslin
Gene namesi
Name:SYNM
Synonyms:DMN, KIAA0353, SYN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:24466. SYNM.

Subcellular locationi

Cytoplasmcytoskeleton. Cell junctionadherens junction
Note: There are at least two distinct SYNM subpopulations, one in which SYMN interacts with DES within the Z-lines, and another in which it interacts with both DTNA and DES at the costamere.

GO - Cellular componenti

  1. adherens junction Source: UniProtKB
  2. costamere Source: UniProtKB
  3. intermediate filament Source: UniProtKB
  4. membrane Source: Ensembl
  5. neurofilament cytoskeleton Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Intermediate filament

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164726408.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15651565SyneminPRO_0000063778Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei429 – 4291Phosphoserine1 Publication
Modified residuei598 – 5981Phosphothreonine1 Publication
Modified residuei1044 – 10441Phosphoserine2 Publications
Modified residuei1049 – 10491Phosphoserine2 Publications
Modified residuei1181 – 11811Phosphoserine2 Publications
Modified residuei1184 – 11841Phosphoserine1 Publication
Modified residuei1435 – 14351Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO15061.
PaxDbiO15061.
PRIDEiO15061.

PTM databases

PhosphoSiteiO15061.

Expressioni

Tissue specificityi

Isoform 2 is strongly detected in adult heart, fetal skeletal muscles and fetal heart. Isoform 1 is weakly detected in fetal heart and also in fetal skeletal muscle. Isoform 1 and isoform 2 are detected in adult bladder (at protein level). The mRNA is predominantly expressed in heart and muscle with some expression in brain which may be due to tissue-specific isoforms.2 Publications

Developmental stagei

In lens, first detected at 16 weeks when expression is weakly and uniformly distributed. Subsequently, expression becomes much stronger in the epithelium of the anterior part at 25 weeks and later. In retina, weakly expressed at 15 weeks in the nerve fiber and ganglion cell layers (NFL and GCL). From 25 weeks onwards, much stronger expression is observed in the endfeet of Mueller cells, the NFL, and GCL, and much lower expression is observed in a minor subpopulation of cells in the inner cell layer (INL). At 30 and 36 weeks, expression remains in the neural retina, and subsequently becomes stronger in the NFL, GCL, and INL and is decreased in Mueller cells. At 36 weeks, also expressed at the external border of the outer nuclear layer (ONL) (at protein level).1 Publication

Gene expression databases

BgeeiO15061.
CleanExiHS_SYNM.
ExpressionAtlasiO15061. baseline and differential.
GenevestigatoriO15061.

Organism-specific databases

HPAiCAB017192.

Interactioni

Subunit structurei

Interacts with GFAP and VIM (By similarity). Isoform 1 interacts with TLN1 and VCL. Isoform 2 interacts with DES and DTNA. Isoform 1 and isoform 2 interact with DMD and UTRN.By similarity5 Publications

Protein-protein interaction databases

BioGridi116923. 14 interactions.
IntActiO15061. 1 interaction.
MINTiMINT-198289.
STRINGi9606.ENSP00000336775.

Structurei

3D structure databases

ProteinModelPortaliO15061.
SMRiO15061. Positions 251-318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 1010Head
Regioni11 – 320310Interaction with DMD and UTRNAdd
BLAST
Regioni11 – 300290RodAdd
BLAST
Regioni11 – 4939Coil 1AAdd
BLAST
Regioni50 – 589Linker 1
Regioni59 – 163105Coil 1BAdd
BLAST
Regioni164 – 18623Linker 12Add
BLAST
Regioni187 – 300114Coil 2Add
BLAST
Regioni301 – 15651265TailAdd
BLAST
Regioni1152 – 1463312Interaction with TLN1 and VCLAdd
BLAST
Regioni1244 – 1563320Interaction with DMD and UTRNAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG139727.
HOGENOMiHOG000154476.
HOVERGENiHBG008974.
InParanoidiO15061.
KOiK10376.
PhylomeDBiO15061.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15061-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha

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
MLSWRLQTGP EKAELQELNA RLYDYVCRVR ELERENLLLE EELRGRRGRE
60 70 80 90 100
GLWAEGQARC AEEARSLRQQ LDELSWATAL AEGERDALRR ELRELQRLDA
110 120 130 140 150
EERAARGRLD AELGAQQREL QEALGARAAL EALLGRLQAE RRGLDAAHER
160 170 180 190 200
DVRELRARAA SLTMHFRARA TGPAAPPPRL REVHDSYALL VAESWRETVQ
210 220 230 240 250
LYEDEVRELE EALRRGQESR LQAEEETRLC AQEAEALRRE ALGLEQLRAR
260 270 280 290 300
LEDALLRMRE EYGIQAEERQ RAIDCLEDEK ATLTLAMADW LRDYQDLLQV
310 320 330 340 350
KTGLSLEVAT YRALLEGESN PEIVIWAEHV ENMPSEFRNK SYHYTDSLLQ
360 370 380 390 400
RENERNLFSR QKAPLASFNH SSALYSNLSG HRGSQTGTSI GGDARRGFLG
410 420 430 440 450
SGYSSSATTQ QENSYGKAVS SQTNVRTFSP TYGLLRNTEA QVKTFPDRPK
460 470 480 490 500
AGDTREVPVY IGEDSTIARE SYRDRRDKVA AGASESTRSN ERTVILGKKT
510 520 530 540 550
EVKATREQER NRPETIRTKP EEKMFDSKEK ASEERNLRWE ELTKLDKEAR
560 570 580 590 600
QRESQQMKEK AKEKDSPKEK SVREREVPIS LEVSQDRRAE VSPKGLQTPV
610 620 630 640 650
KDAGGGTGRE AEARELRFRL GTSDATGSLQ GDSMTETVAE NIVTSILKQF
660 670 680 690 700
TQSPETEASA DSFPDTKVTY VDRKELPGER KTKTEIVVES KLTEDVDVSD
710 720 730 740 750
EAGLDYLLSK DIKEVGLKGK SAEQMIGDII NLGLKGREGR AKVVNVEIVE
760 770 780 790 800
EPVSYVSGEK PEEFSVPFKV EEVEDVSPGP WGLVKEEEGY GESDVTFSVN
810 820 830 840 850
QHRRTKQPQE NTTHVEEVTE AGDSEGEQSY FVSTPDEHPG GHDRDDGSVY
860 870 880 890 900
GQIHIEEEST IRYSWQDEIV QGTRRRTQKD GAVGEKVVKP LDVPAPSLEG
910 920 930 940 950
DLGSTHWKEQ ARSGEFHAEP TVIEKEIKIP HEFHTSMKGI SSKEPRQQLV
960 970 980 990 1000
EVIGQLEETL PERMREELSA LTREGQGGPG SVSVDVKKVQ GAGGSSVTLV
1010 1020 1030 1040 1050
AEVNVSQTVD ADRLDLEELS KDEASEMEKA VESVVRESLS RQRSPAPGSP
1060 1070 1080 1090 1100
DEEGGAEAPA AGIRFRRWAT RELYIPSGES EVAGGASHSS GQRTPQGPVS
1110 1120 1130 1140 1150
ATVEVSSPTG FAQSQVLEDV SQAARHIKLG PSEVWRTERM SYEGPTAEVV
1160 1170 1180 1190 1200
EVSAGGDLSQ AASPTGASRS VRHVTLGPGQ SPLSREVIFL GPAPACPEAW
1210 1220 1230 1240 1250
GSPEPGPAES SADMDGSGRH STFGCRQFHA EKEIIFQGPI SAAGKVGDYF
1260 1270 1280 1290 1300
ATEESVGTQT SVRQLQLGPK EGFSGQIQFT APLSDKVELG VIGDSVHMEG
1310 1320 1330 1340 1350
LPGSSTSIRH ISIGPQRHQT TQQIVYHGLV PQLGESGDSE STVHGEGSAD
1360 1370 1380 1390 1400
VHQATHSHTS GRQTVMTEKS TFQSVVSESP QEDSAGDTSG AEMTSGVSRS
1410 1420 1430 1440 1450
FRHIRLGPTE TETSEHIAIR GPVSRTFVLA GSADSPELGK LADSSRTLRH
1460 1470 1480 1490 1500
IAPGPKETSF TFQMDVSNVE AIRSRTQEAG ALGVSDRGSW RDADSRNDQA
1510 1520 1530 1540 1550
VGVSFKASAG EGDQAHREQG KEQAMFDKKV QLQRMVDQRS VISDEKKVAL
1560
LYLDNEEEEN DGHWF
Length:1,565
Mass (Da):172,768
Last modified:January 23, 2002 - v2
Checksum:i18D19000D3CEA537
GO
Isoform 2 (identifier: O15061-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     1152-1463: Missing.

Show »
Length:1,253
Mass (Da):140,135
Checksum:i88162E538D848F2A
GO
Isoform 3 (identifier: O15061-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     336-339: EFRN → DGCE
     340-1565: Missing.

Show »
Length:339
Mass (Da):39,042
Checksum:i090EEA199A0041C4
GO

Sequence cautioni

The sequence AAI10067.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAA20810.2 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41W → L in CAC83858. (PubMed:11737198)Curated
Sequence conflicti4 – 41W → L in CAC83859. (PubMed:11737198)Curated
Sequence conflicti4 – 41W → L in CAG27071. 1 PublicationCurated
Sequence conflicti24 – 241Missing in CAC83858. (PubMed:11737198)Curated
Sequence conflicti24 – 241Missing in CAC83859. (PubMed:11737198)Curated
Sequence conflicti52 – 521Missing in CAC83858. (PubMed:11737198)Curated
Sequence conflicti52 – 521Missing in CAC83859. (PubMed:11737198)Curated
Sequence conflicti197 – 1971E → G in CAG27071. 1 PublicationCurated
Sequence conflicti241 – 2411A → T in CAG27071. 1 PublicationCurated
Sequence conflicti274 – 2741D → G in CAG27071. 1 PublicationCurated
Sequence conflicti318 – 3181E → G in CAG27071. 1 PublicationCurated
Sequence conflicti322 – 3221E → Q in CAC83858. (PubMed:11737198)Curated
Sequence conflicti322 – 3221E → Q in CAC83859. (PubMed:11737198)Curated
Sequence conflicti322 – 3221E → Q in CAG27071. 1 PublicationCurated
Sequence conflicti373 – 3731A → V in CAC83858. (PubMed:11737198)Curated
Sequence conflicti373 – 3731A → V in CAC83859. (PubMed:11737198)Curated
Sequence conflicti555 – 5551Q → H in CAC83858. (PubMed:11737198)Curated
Sequence conflicti555 – 5551Q → H in CAC83859. (PubMed:11737198)Curated
Sequence conflicti564 – 5641K → N in CAC83858. (PubMed:11737198)Curated
Sequence conflicti564 – 5641K → N in CAC83859. (PubMed:11737198)Curated
Sequence conflicti655 – 6551E → Q in CAC83858. (PubMed:11737198)Curated
Sequence conflicti655 – 6551E → Q in CAC83859. (PubMed:11737198)Curated
Sequence conflicti666 – 6661T → A in CAC83858. (PubMed:11737198)Curated
Sequence conflicti666 – 6661T → A in CAC83859. (PubMed:11737198)Curated
Sequence conflicti687 – 6871V → L in CAC83858. (PubMed:11737198)Curated
Sequence conflicti687 – 6871V → L in CAC83859. (PubMed:11737198)Curated
Sequence conflicti720 – 7201K → N in CAC83858. (PubMed:11737198)Curated
Sequence conflicti720 – 7201K → N in CAC83859. (PubMed:11737198)Curated
Sequence conflicti845 – 8451D → N in CAC83858. (PubMed:11737198)Curated
Sequence conflicti845 – 8451D → N in CAC83859. (PubMed:11737198)Curated
Sequence conflicti856 – 8561E → Q in CAC83858. (PubMed:11737198)Curated
Sequence conflicti856 – 8561E → Q in CAC83859. (PubMed:11737198)Curated
Sequence conflicti874 – 8741R → P in CAC83858. (PubMed:11737198)Curated
Sequence conflicti874 – 8741R → P in CAC83859. (PubMed:11737198)Curated
Sequence conflicti965 – 9651R → K in CAC83858. (PubMed:11737198)Curated
Sequence conflicti965 – 9651R → K in CAC83859. (PubMed:11737198)Curated
Sequence conflicti1004 – 10041N → D in CAC83858. (PubMed:11737198)Curated
Sequence conflicti1004 – 10041N → D in CAC83859. (PubMed:11737198)Curated
Sequence conflicti1019 – 10191L → V in CAC83858. (PubMed:11737198)Curated
Sequence conflicti1019 – 10191L → V in CAC83859. (PubMed:11737198)Curated
Sequence conflicti1039 – 10391L → M in CAC83858. (PubMed:11737198)Curated
Sequence conflicti1039 – 10391L → M in CAC83859. (PubMed:11737198)Curated
Sequence conflicti1076 – 10761P → L in CAC83858. (PubMed:11737198)Curated
Sequence conflicti1076 – 10761P → L in CAC83859. (PubMed:11737198)Curated
Sequence conflicti1151 – 11511E → G in CAC83859. (PubMed:11737198)Curated
Sequence conflicti1292 – 12921I → T in CAC83859. (PubMed:11737198)Curated
Sequence conflicti1493 – 14931A → R in AAI10067. (PubMed:15489334)Curated
Sequence conflicti1509 – 15091A → V in CAC83858. (PubMed:11737198)Curated
Sequence conflicti1509 – 15091A → V in CAC83859. (PubMed:11737198)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti272 – 2721A → V.2 Publications
VAR_012295
Natural varianti330 – 3301V → I.1 Publication
VAR_012296
Natural varianti338 – 3381R → W.1 Publication
VAR_012297
Natural varianti355 – 3551R → W.3 Publications
Corresponds to variant rs3743242 [ dbSNP | Ensembl ].
VAR_059378
Natural varianti462 – 4621G → S.2 Publications
Corresponds to variant rs3134595 [ dbSNP | Ensembl ].
VAR_059379
Natural varianti567 – 5671P → L.2 Publications
VAR_012298
Natural varianti612 – 6121E → A.1 Publication
VAR_012299
Natural varianti761 – 7611P → L.1 Publication
VAR_012300
Natural varianti946 – 9461R → W.1 Publication
VAR_012301
Natural varianti976 – 9761Q → R.1 Publication
VAR_012302
Natural varianti1059 – 10591P → L.1 Publication
VAR_012303
Natural varianti1067 – 10671R → P.1 Publication
VAR_012304
Natural varianti1077 – 10771S → L.1 Publication
VAR_012305
Natural varianti1130 – 11301G → S.
Corresponds to variant rs9920074 [ dbSNP | Ensembl ].
VAR_059380
Natural varianti1345 – 13451G → A.
Corresponds to variant rs7167599 [ dbSNP | Ensembl ].
VAR_059381
Natural varianti1386 – 13861G → E.1 Publication
Corresponds to variant rs2292288 [ dbSNP | Ensembl ].
VAR_012306
Natural varianti1462 – 14621F → C.
Corresponds to variant rs2292287 [ dbSNP | Ensembl ].
VAR_012307

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei336 – 3394EFRN → DGCE in isoform 3. 1 PublicationVSP_036478
Alternative sequencei340 – 15651226Missing in isoform 3. 1 PublicationVSP_036479Add
BLAST
Alternative sequencei1152 – 1463312Missing in isoform 2. 2 PublicationsVSP_002465Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ310521 mRNA. Translation: CAC83858.1.
AJ310522 mRNA. Translation: CAC83859.1.
AF359284 mRNA. Translation: AAK57487.1.
AJ697971 mRNA. Translation: CAG27071.1.
AB002351 mRNA. Translation: BAA20810.2. Different initiation.
BC110066 mRNA. Translation: AAI10067.1. Different initiation.
BC151243 mRNA. Translation: AAI51244.1.
CCDSiCCDS73786.1. [O15061-2]
CCDS73787.1. [O15061-1]
RefSeqiNP_056101.5. NM_015286.5.
NP_663780.2. NM_145728.2.
UniGeneiHs.207106.

Genome annotation databases

EnsembliENST00000336292; ENSP00000336775; ENSG00000182253.
GeneIDi23336.
KEGGihsa:23336.
UCSCiuc002buo.3. human. [O15061-2]
uc002bup.3. human. [O15061-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ310521 mRNA. Translation: CAC83858.1 .
AJ310522 mRNA. Translation: CAC83859.1 .
AF359284 mRNA. Translation: AAK57487.1 .
AJ697971 mRNA. Translation: CAG27071.1 .
AB002351 mRNA. Translation: BAA20810.2 . Different initiation.
BC110066 mRNA. Translation: AAI10067.1 . Different initiation.
BC151243 mRNA. Translation: AAI51244.1 .
CCDSi CCDS73786.1. [O15061-2 ]
CCDS73787.1. [O15061-1 ]
RefSeqi NP_056101.5. NM_015286.5.
NP_663780.2. NM_145728.2.
UniGenei Hs.207106.

3D structure databases

ProteinModelPortali O15061.
SMRi O15061. Positions 251-318.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116923. 14 interactions.
IntActi O15061. 1 interaction.
MINTi MINT-198289.
STRINGi 9606.ENSP00000336775.

PTM databases

PhosphoSitei O15061.

Proteomic databases

MaxQBi O15061.
PaxDbi O15061.
PRIDEi O15061.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336292 ; ENSP00000336775 ; ENSG00000182253 .
GeneIDi 23336.
KEGGi hsa:23336.
UCSCi uc002buo.3. human. [O15061-2 ]
uc002bup.3. human. [O15061-1 ]

Organism-specific databases

CTDi 23336.
GeneCardsi GC15P099645.
H-InvDB HIX0172820.
HGNCi HGNC:24466. SYNM.
HPAi CAB017192.
MIMi 606087. gene.
neXtProti NX_O15061.
PharmGKBi PA164726408.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG139727.
HOGENOMi HOG000154476.
HOVERGENi HBG008974.
InParanoidi O15061.
KOi K10376.
PhylomeDBi O15061.

Miscellaneous databases

ChiTaRSi SYNM. human.
GenomeRNAii 23336.
NextBioi 45283.
PROi O15061.
SOURCEi Search...

Gene expression databases

Bgeei O15061.
CleanExi HS_SYNM.
ExpressionAtlasi O15061. baseline and differential.
Genevestigatori O15061.

Family and domain databases

InterProi IPR001664. IF.
IPR018039. Intermediate_filament_CS.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
Pfami PF00038. Filament. 1 hit.
[Graphical view ]
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human synemin gene generates splice variants encoding two distinct intermediate filament proteins."
    Titeux M., Brocheriou V., Xue Z., Gao J., Pellissier J.-F., Guicheney P., Paulin D., Li Z.
    Eur. J. Biochem. 268:6435-6449(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBUNIT, TISSUE SPECIFICITY, VARIANTS VAL-272; TRP-355; LEU-567 AND GLU-1386.
    Tissue: Placenta and Skeletal muscle.
  2. "Desmuslin, an intermediate filament protein that interacts with alpha-dystrobrevin and desmin."
    Mizuno Y., Thompson T.G., Guyon J.R., Lidov H.G.W., Brosius M., Imamura M., Ozawa E., Watkins S.C., Kunkel L.M.
    Proc. Natl. Acad. Sci. U.S.A. 98:6156-6161(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH DES AND DTNA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Skeletal muscle.
  3. "Synemin gene generates different spliced isoforms expressed selectively in either astrocytes or neurons."
    Xue Z., Izmiryan A., Paulin D., Li Z.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  4. Nagase T., Kikuno R., Yamakawa H., Ohara O.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS TRP-355 AND SER-462.
    Tissue: Brain.
  5. "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), VARIANTS TRP-355 AND SER-462.
  6. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-1565 (ISOFORM 1).
    Tissue: Brain.
  7. "Synemin expression in developing normal and pathological human retina and lens."
    Tawk M., Titeux M., Fallet C., Li Z., Daumas-Duport C., Cavalcante L.A., Paulin D., Moura-Neto V.
    Exp. Neurol. 183:499-507(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  8. "Interactions of intermediate filament protein synemin with dystrophin and utrophin."
    Bhosle R.C., Michele D.E., Campbell K.P., Li Z., Robson R.M.
    Biochem. Biophys. Res. Commun. 346:768-777(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DMD AND UTRN.
  9. "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-1184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Human alpha-synemin interacts directly with vinculin and metavinculin."
    Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.
    Biochem. J. 409:657-667(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VCL.
  11. "Identification of a repeated domain within mammalian alpha-synemin that interacts directly with talin."
    Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.
    Exp. Cell Res. 314:1839-1849(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TLN1, SUBCELLULAR LOCATION.
  12. "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-1044; SER-1049 AND SER-1435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; THR-598 AND SER-1181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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-1044; SER-1049 AND SER-1181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Genomic organization and single-nucleotide polymorphism map of desmuslin, a novel intermediate filament protein on chromosome 15q26.3."
    Mizuno Y., Puca A.A., O'Brien K.F., Beggs A.H., Kunkel L.M.
    BMC Genet. 2:8-8(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VAL-272; ILE-330; TRP-338; LEU-567; ALA-612; LEU-761; TRP-946; ARG-976; LEU-1059; PRO-1067 AND LEU-1077.

Entry informationi

Entry nameiSYNEM_HUMAN
AccessioniPrimary (citable) accession number: O15061
Secondary accession number(s): A7E2Y2
, Q2TBJ4, Q5NJJ9, Q8TE61, Q8TE62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: October 29, 2014
This is version 120 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3