O15061 (SYNEM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Synemin

Alternative name(s):
Desmuslin

Gene names

Name:	SYNM
Synonyms:	DMN, KIAA0353, SYN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1565 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.8 Ref.10
Subunit structure	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. Ref.1 Ref.2 Ref.8 Ref.10 Ref.11
Subcellular location	Cytoplasm › cytoskeleton. Cell junction › adherens 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. Ref.2 Ref.11
Tissue specificity	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. Ref.1 Ref.2
Developmental stage	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). Ref.7
Sequence similarities	Belongs to the intermediate filament family.
Sequence caution	The sequence AAI10067.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA20810.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell junction Cytoplasm Cytoskeleton Intermediate filament
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intermediate filament cytoskeleton organization Traceable author statement Ref.8. Source: UniProtKB
Cellular_component	adherens junction Inferred from direct assay Ref.8. Source: UniProtKB costamere Inferred from direct assay Ref.8Ref.11. Source: UniProtKB intermediate filament Inferred from direct assay Ref.1. Source: UniProtKB membrane Inferred from electronic annotation. Source: Compara neurofilament cytoskeleton Traceable author statement Ref.7. Source: UniProtKB
Molecular_function	intermediate filament binding Inferred from sequence or structural similarity. Source: UniProtKB structural constituent of cytoskeleton Inferred from direct assay Ref.1Ref.8. Source: UniProtKB structural constituent of muscle Inferred from direct assay Ref.1. Source: UniProtKB vinculin binding Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O15061-1)

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.

Isoform 2 (identifier: O15061-2)

Also known as: Beta;

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

Isoform 3 (identifier: O15061-3)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1565	1565	Synemin		PRO_0000063778
Regions
	Region	1 – 10	10	Head
	Region	11 – 320	310	Interaction with DMD and UTRN
	Region	11 – 300	290	Rod
	Region	11 – 49	39	Coil 1A
	Region	50 – 58	9	Linker 1
	Region	59 – 163	105	Coil 1B
	Region	164 – 186	23	Linker 12
	Region	187 – 300	114	Coil 2
	Region	301 – 1565	1265	Tail
	Region	1152 – 1463	312	Interaction with TLN1 and VCL
	Region	1244 – 1563	320	Interaction with DMD and UTRN
Amino acid modifications
	Modified residue	429	1	Phosphoserine Ref.13
	Modified residue	598	1	Phosphothreonine Ref.13
	Modified residue	1044	1	Phosphoserine Ref.12 Ref.14
	Modified residue	1049	1	Phosphoserine Ref.12 Ref.14
	Modified residue	1181	1	Phosphoserine Ref.13 Ref.14
	Modified residue	1184	1	Phosphoserine Ref.9
	Modified residue	1435	1	Phosphoserine Ref.12
Natural variations
	Alternative sequence	336 – 339	4	EFRN → DGCE in isoform 3.		VSP_036478
	Alternative sequence	340 – 1565	1226	Missing in isoform 3.		VSP_036479
	Alternative sequence	1152 – 1463	312	Missing in isoform 2.		VSP_002465
	Natural variant	272	1	A → V. Ref.1 Ref.15		VAR_012295
	Natural variant	330	1	V → I. Ref.15		VAR_012296
	Natural variant	338	1	R → W. Ref.15		VAR_012297
	Natural variant	355	1	R → W. Ref.1 Ref.4 Ref.5 Corresponds to variant rs3743242 [ dbSNP | Ensembl ].		VAR_059378
	Natural variant	462	1	G → S. Ref.4 Ref.5 Corresponds to variant rs3134595 [ dbSNP | Ensembl ].		VAR_059379
	Natural variant	567	1	P → L. Ref.1 Ref.15		VAR_012298
	Natural variant	612	1	E → A. Ref.15		VAR_012299
	Natural variant	761	1	P → L. Ref.15		VAR_012300
	Natural variant	946	1	R → W. Ref.15		VAR_012301
	Natural variant	976	1	Q → R. Ref.15		VAR_012302
	Natural variant	1059	1	P → L. Ref.15		VAR_012303
	Natural variant	1067	1	R → P. Ref.15		VAR_012304
	Natural variant	1077	1	S → L. Ref.15		VAR_012305
	Natural variant	1130	1	G → S. Corresponds to variant rs9920074 [ dbSNP | Ensembl ].		VAR_059380
	Natural variant	1345	1	G → A. Corresponds to variant rs7167599 [ dbSNP | Ensembl ].		VAR_059381
	Natural variant	1386	1	G → E. Ref.1 Corresponds to variant rs2292288 [ dbSNP | Ensembl ].		VAR_012306
	Natural variant	1462	1	F → C. Corresponds to variant rs2292287 [ dbSNP | Ensembl ].		VAR_012307
Experimental info
	Sequence conflict	4	1	W → L in CAC83858. Ref.1
	Sequence conflict	4	1	W → L in CAC83859. Ref.1
	Sequence conflict	4	1	W → L in CAG27071. Ref.3
	Sequence conflict	24	1	Missing in CAC83858. Ref.1
	Sequence conflict	24	1	Missing in CAC83859. Ref.1
	Sequence conflict	52	1	Missing in CAC83858. Ref.1
	Sequence conflict	52	1	Missing in CAC83859. Ref.1
	Sequence conflict	197	1	E → G in CAG27071. Ref.3
	Sequence conflict	241	1	A → T in CAG27071. Ref.3
	Sequence conflict	274	1	D → G in CAG27071. Ref.3
	Sequence conflict	318	1	E → G in CAG27071. Ref.3
	Sequence conflict	322	1	E → Q in CAC83858. Ref.1
	Sequence conflict	322	1	E → Q in CAC83859. Ref.1
	Sequence conflict	322	1	E → Q in CAG27071. Ref.3
	Sequence conflict	373	1	A → V in CAC83858. Ref.1
	Sequence conflict	373	1	A → V in CAC83859. Ref.1
	Sequence conflict	555	1	Q → H in CAC83858. Ref.1
	Sequence conflict	555	1	Q → H in CAC83859. Ref.1
	Sequence conflict	564	1	K → N in CAC83858. Ref.1
	Sequence conflict	564	1	K → N in CAC83859. Ref.1
	Sequence conflict	655	1	E → Q in CAC83858. Ref.1
	Sequence conflict	655	1	E → Q in CAC83859. Ref.1
	Sequence conflict	666	1	T → A in CAC83858. Ref.1
	Sequence conflict	666	1	T → A in CAC83859. Ref.1
	Sequence conflict	687	1	V → L in CAC83858. Ref.1
	Sequence conflict	687	1	V → L in CAC83859. Ref.1
	Sequence conflict	720	1	K → N in CAC83858. Ref.1
	Sequence conflict	720	1	K → N in CAC83859. Ref.1
	Sequence conflict	845	1	D → N in CAC83858. Ref.1
	Sequence conflict	845	1	D → N in CAC83859. Ref.1
	Sequence conflict	856	1	E → Q in CAC83858. Ref.1
	Sequence conflict	856	1	E → Q in CAC83859. Ref.1
	Sequence conflict	874	1	R → P in CAC83858. Ref.1
	Sequence conflict	874	1	R → P in CAC83859. Ref.1
	Sequence conflict	965	1	R → K in CAC83858. Ref.1
	Sequence conflict	965	1	R → K in CAC83859. Ref.1
	Sequence conflict	1004	1	N → D in CAC83858. Ref.1
	Sequence conflict	1004	1	N → D in CAC83859. Ref.1
	Sequence conflict	1019	1	L → V in CAC83858. Ref.1
	Sequence conflict	1019	1	L → V in CAC83859. Ref.1
	Sequence conflict	1039	1	L → M in CAC83858. Ref.1
	Sequence conflict	1039	1	L → M in CAC83859. Ref.1
	Sequence conflict	1076	1	P → L in CAC83858. Ref.1
	Sequence conflict	1076	1	P → L in CAC83859. Ref.1
	Sequence conflict	1151	1	E → G in CAC83859. Ref.1
	Sequence conflict	1292	1	I → T in CAC83859. Ref.1
	Sequence conflict	1493	1	A → R in AAI10067. Ref.5
	Sequence conflict	1509	1	A → V in CAC83858. Ref.1
	Sequence conflict	1509	1	A → V in CAC83859. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified January 23, 2002. Version 2. Checksum: 18D19000D3CEA537	FASTA	1,565	172,768
	10 20 30 40 50 60 MLSWRLQTGP EKAELQELNA RLYDYVCRVR ELERENLLLE EELRGRRGRE GLWAEGQARC 70 80 90 100 110 120 AEEARSLRQQ LDELSWATAL AEGERDALRR ELRELQRLDA EERAARGRLD AELGAQQREL 130 140 150 160 170 180 QEALGARAAL EALLGRLQAE RRGLDAAHER DVRELRARAA SLTMHFRARA TGPAAPPPRL 190 200 210 220 230 240 REVHDSYALL VAESWRETVQ LYEDEVRELE EALRRGQESR LQAEEETRLC AQEAEALRRE 250 260 270 280 290 300 ALGLEQLRAR LEDALLRMRE EYGIQAEERQ RAIDCLEDEK ATLTLAMADW LRDYQDLLQV 310 320 330 340 350 360 KTGLSLEVAT YRALLEGESN PEIVIWAEHV ENMPSEFRNK SYHYTDSLLQ RENERNLFSR 370 380 390 400 410 420 QKAPLASFNH SSALYSNLSG HRGSQTGTSI GGDARRGFLG SGYSSSATTQ QENSYGKAVS 430 440 450 460 470 480 SQTNVRTFSP TYGLLRNTEA QVKTFPDRPK AGDTREVPVY IGEDSTIARE SYRDRRDKVA 490 500 510 520 530 540 AGASESTRSN ERTVILGKKT EVKATREQER NRPETIRTKP EEKMFDSKEK ASEERNLRWE 550 560 570 580 590 600 ELTKLDKEAR QRESQQMKEK AKEKDSPKEK SVREREVPIS LEVSQDRRAE VSPKGLQTPV 610 620 630 640 650 660 KDAGGGTGRE AEARELRFRL GTSDATGSLQ GDSMTETVAE NIVTSILKQF TQSPETEASA 670 680 690 700 710 720 DSFPDTKVTY VDRKELPGER KTKTEIVVES KLTEDVDVSD EAGLDYLLSK DIKEVGLKGK 730 740 750 760 770 780 SAEQMIGDII NLGLKGREGR AKVVNVEIVE EPVSYVSGEK PEEFSVPFKV EEVEDVSPGP 790 800 810 820 830 840 WGLVKEEEGY GESDVTFSVN QHRRTKQPQE NTTHVEEVTE AGDSEGEQSY FVSTPDEHPG 850 860 870 880 890 900 GHDRDDGSVY GQIHIEEEST IRYSWQDEIV QGTRRRTQKD GAVGEKVVKP LDVPAPSLEG 910 920 930 940 950 960 DLGSTHWKEQ ARSGEFHAEP TVIEKEIKIP HEFHTSMKGI SSKEPRQQLV EVIGQLEETL 970 980 990 1000 1010 1020 PERMREELSA LTREGQGGPG SVSVDVKKVQ GAGGSSVTLV AEVNVSQTVD ADRLDLEELS 1030 1040 1050 1060 1070 1080 KDEASEMEKA VESVVRESLS RQRSPAPGSP DEEGGAEAPA AGIRFRRWAT RELYIPSGES 1090 1100 1110 1120 1130 1140 EVAGGASHSS GQRTPQGPVS ATVEVSSPTG FAQSQVLEDV SQAARHIKLG PSEVWRTERM 1150 1160 1170 1180 1190 1200 SYEGPTAEVV EVSAGGDLSQ AASPTGASRS VRHVTLGPGQ SPLSREVIFL GPAPACPEAW 1210 1220 1230 1240 1250 1260 GSPEPGPAES SADMDGSGRH STFGCRQFHA EKEIIFQGPI SAAGKVGDYF ATEESVGTQT 1270 1280 1290 1300 1310 1320 SVRQLQLGPK EGFSGQIQFT APLSDKVELG VIGDSVHMEG LPGSSTSIRH ISIGPQRHQT 1330 1340 1350 1360 1370 1380 TQQIVYHGLV PQLGESGDSE STVHGEGSAD VHQATHSHTS GRQTVMTEKS TFQSVVSESP 1390 1400 1410 1420 1430 1440 QEDSAGDTSG AEMTSGVSRS FRHIRLGPTE TETSEHIAIR GPVSRTFVLA GSADSPELGK 1450 1460 1470 1480 1490 1500 LADSSRTLRH IAPGPKETSF TFQMDVSNVE AIRSRTQEAG ALGVSDRGSW RDADSRNDQA 1510 1520 1530 1540 1550 1560 VGVSFKASAG EGDQAHREQG KEQAMFDKKV QLQRMVDQRS VISDEKKVAL LYLDNEEEEN DGHWF
	Isoform 2 (Beta) [UniParc]. Checksum: 88162E538D848F2A	FASTA	1,253	140,135
	10 20 30 40 50 60 MLSWRLQTGP EKAELQELNA RLYDYVCRVR ELERENLLLE EELRGRRGRE GLWAEGQARC 70 80 90 100 110 120 AEEARSLRQQ LDELSWATAL AEGERDALRR ELRELQRLDA EERAARGRLD AELGAQQREL 130 140 150 160 170 180 QEALGARAAL EALLGRLQAE RRGLDAAHER DVRELRARAA SLTMHFRARA TGPAAPPPRL 190 200 210 220 230 240 REVHDSYALL VAESWRETVQ LYEDEVRELE EALRRGQESR LQAEEETRLC AQEAEALRRE 250 260 270 280 290 300 ALGLEQLRAR LEDALLRMRE EYGIQAEERQ RAIDCLEDEK ATLTLAMADW LRDYQDLLQV 310 320 330 340 350 360 KTGLSLEVAT YRALLEGESN PEIVIWAEHV ENMPSEFRNK SYHYTDSLLQ RENERNLFSR 370 380 390 400 410 420 QKAPLASFNH SSALYSNLSG HRGSQTGTSI GGDARRGFLG SGYSSSATTQ QENSYGKAVS 430 440 450 460 470 480 SQTNVRTFSP TYGLLRNTEA QVKTFPDRPK AGDTREVPVY IGEDSTIARE SYRDRRDKVA 490 500 510 520 530 540 AGASESTRSN ERTVILGKKT EVKATREQER NRPETIRTKP EEKMFDSKEK ASEERNLRWE 550 560 570 580 590 600 ELTKLDKEAR QRESQQMKEK AKEKDSPKEK SVREREVPIS LEVSQDRRAE VSPKGLQTPV 610 620 630 640 650 660 KDAGGGTGRE AEARELRFRL GTSDATGSLQ GDSMTETVAE NIVTSILKQF TQSPETEASA 670 680 690 700 710 720 DSFPDTKVTY VDRKELPGER KTKTEIVVES KLTEDVDVSD EAGLDYLLSK DIKEVGLKGK 730 740 750 760 770 780 SAEQMIGDII NLGLKGREGR AKVVNVEIVE EPVSYVSGEK PEEFSVPFKV EEVEDVSPGP 790 800 810 820 830 840 WGLVKEEEGY GESDVTFSVN QHRRTKQPQE NTTHVEEVTE AGDSEGEQSY FVSTPDEHPG 850 860 870 880 890 900 GHDRDDGSVY GQIHIEEEST IRYSWQDEIV QGTRRRTQKD GAVGEKVVKP LDVPAPSLEG 910 920 930 940 950 960 DLGSTHWKEQ ARSGEFHAEP TVIEKEIKIP HEFHTSMKGI SSKEPRQQLV EVIGQLEETL 970 980 990 1000 1010 1020 PERMREELSA LTREGQGGPG SVSVDVKKVQ GAGGSSVTLV AEVNVSQTVD ADRLDLEELS 1030 1040 1050 1060 1070 1080 KDEASEMEKA VESVVRESLS RQRSPAPGSP DEEGGAEAPA AGIRFRRWAT RELYIPSGES 1090 1100 1110 1120 1130 1140 EVAGGASHSS GQRTPQGPVS ATVEVSSPTG FAQSQVLEDV SQAARHIKLG PSEVWRTERM 1150 1160 1170 1180 1190 1200 SYEGPTAEVV EMDVSNVEAI RSRTQEAGAL GVSDRGSWRD ADSRNDQAVG VSFKASAGEG 1210 1220 1230 1240 1250 DQAHREQGKE QAMFDKKVQL QRMVDQRSVI SDEKKVALLY LDNEEEENDG HWF
	Isoform 3 [UniParc]. Checksum: 090EEA199A0041C4	FASTA	339	39,042
	10 20 30 40 50 60 MLSWRLQTGP EKAELQELNA RLYDYVCRVR ELERENLLLE EELRGRRGRE GLWAEGQARC 70 80 90 100 110 120 AEEARSLRQQ LDELSWATAL AEGERDALRR ELRELQRLDA EERAARGRLD AELGAQQREL 130 140 150 160 170 180 QEALGARAAL EALLGRLQAE RRGLDAAHER DVRELRARAA SLTMHFRARA TGPAAPPPRL 190 200 210 220 230 240 REVHDSYALL VAESWRETVQ LYEDEVRELE EALRRGQESR LQAEEETRLC AQEAEALRRE 250 260 270 280 290 300 ALGLEQLRAR LEDALLRMRE EYGIQAEERQ RAIDCLEDEK ATLTLAMADW LRDYQDLLQV 310 320 330 KTGLSLEVAT YRALLEGESN PEIVIWAEHV ENMPSDGCE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; THR-598 AND SER-1181, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00299301. IPI00299302. IPI00921956.
RefSeq	NP_056101.5. NM_015286.5. NP_663780.2. NM_145728.2.
UniGene	Hs.207106.
3D structure databases
ProteinModelPortal	O15061.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-198289.
STRING	9606.ENSP00000336775.
PTM databases
PhosphoSite	O15061.
Proteomic databases
PaxDb	O15061.
PRIDE	O15061.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000336292; ENSP00000336775; ENSG00000182253.
GeneID	23336.
KEGG	hsa:23336.
UCSC	uc002buo.3. human. uc002bup.3. human.
Organism-specific databases
CTD	23336.
GeneCards	GC15P099645.
H-InvDB	HIX0172820.
HGNC	HGNC:24466. SYNM.
HPA	CAB017192.
MIM	606087. gene.
neXtProt	NX_O15061.
PharmGKB	PA164726408.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG139727.
HOGENOM	HOG000154476.
HOVERGEN	HBG008974.
InParanoid	O15061.
KO	K10376.
Gene expression databases
ArrayExpress	O15061.
Bgee	O15061.
CleanEx	HS_SYNM.
Genevestigator	O15061.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. [Graphical view]
PANTHER	PTHR23239. PTHR23239. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SYNM. human.
GenomeRNAi	23336.
NextBio	45283.
SOURCE	Search...

Entry information

Entry name

SYNEM_HUMAN

Accession

Primary (citable) accession number: O15061
Secondary accession number(s): A7E2Y2 , Q2TBJ4, Q5NJJ9, Q8TE61, Q8TE62

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	January 23, 2002
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 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.