Q05682 (CALD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Caldesmon
Short name=CDM

Gene names

Name:	CALD1
Synonyms:	CAD, CDM

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	793 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration By similarity. Ref.6
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cytoplasm › myofibril By similarity. Note: On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle) By similarity.
Tissue specificity	High-molecular-weight caldesmon (isoform 1) is predominantly expressed in smooth muscles, whereas low-molecular-weight caldesmon (isoforms 2, 3, 4 and 5) are widely distributed in non-muscle tissues and cells. Not expressed in skeletal muscle or heart.
Domain	The N-terminal part seems to be a myosin/calmodulin-binding domain, and the C-terminal a tropomyosin/actin/calmodulin-binding domain. These two domains are separated by a central helical region in the smooth-muscle form.
Post-translational modification	In non-muscle cells, phosphorylation by CDK1 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividing smooth muscle cells with similar effects on the interaction with actin and calmodulin and on microfilaments reorganization. CDK1-mediated phosphorylation promotes Schwann cell migration during peripheral nerve regeneration By similarity.
Sequence similarities	Belongs to the caldesmon family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Actin-binding Calmodulin-binding
Molecular function	Muscle protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular component movement Traceable author statement. Source: UniProtKB muscle contraction Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome myofibril Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: HPA
Molecular function	actin binding Traceable author statement. Source: ProtInc calmodulin binding Traceable author statement. Source: ProtInc myosin binding Inferred from electronic annotation. Source: InterPro tropomyosin binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q05682-1)

Also known as: H-CAD;

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: Q05682-2)

Also known as: WI-38 L-CAD I;

The sequence of this isoform differs from the canonical sequence as follows:
     208-436: Missing.

Isoform 3 (identifier: Q05682-3)

Also known as: HELA L-CAD I;

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MDDFERRRELRRQKREEMRLEAER → MLGGSGSHGRRSLAALSQ
     208-436: Missing.

Isoform 4 (identifier: Q05682-4)

Also known as: WI-38 L-CAD II; 1-CAD;

The sequence of this isoform differs from the canonical sequence as follows:
     208-462: Missing.

Isoform 5 (identifier: Q05682-5)

Also known as: HELA L-CAD II;

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MDDFERRRELRRQKREEMRLEAER → MLGGSGSHGRRSLAALSQ
     208-462: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 793	793	Caldesmon		PRO_0000089288
Regions
	Repeat	319 – 332	14	1
	Repeat	333 – 346	14	2
	Repeat	347 – 360	14	3
	Region	26 – 207	182	Myosin and calmodulin-binding By similarity
	Region	319 – 375	57	3 X 14 AA tandem repeats of E-E-E-K-R-A-A-E-E-R-Q-R-I-K
	Region	564 – 621	58	Tropomyosin-binding Potential
	Region	653 – 686	34	Strong actin-binding By similarity
	Region	664 – 674	11	Tropomyosin-binding Potential
	Region	716 – 722	7	Calmodulin-binding By similarity
	Region	768 – 793	26	Weak actin-binding By similarity
	Compositional bias	39 – 46	8	Poly-Arg
	Compositional bias	81 – 86	6	Poly-Thr
	Compositional bias	189 – 196	8	Poly-Glu
	Compositional bias	376 – 379	4	Poly-Glu
	Compositional bias	540 – 543	4	Poly-Arg
	Compositional bias	580 – 583	4	Poly-Glu
	Compositional bias	597 – 600	4	Poly-Glu
Amino acid modifications
	Modified residue	27	1	Phosphotyrosine Ref.7
	Modified residue	202	1	Phosphoserine Ref.7
	Modified residue	518	1	Phosphoserine Ref.9
	Modified residue	656	1	Phosphoserine Ref.8 Ref.10
	Modified residue	682	1	Phosphotyrosine Ref.12
	Modified residue	723	1	Phosphoserine Ref.8
	Modified residue	724	1	Phosphoserine Ref.7 Ref.8 Ref.10 Ref.11
	Modified residue	726	1	Phosphothreonine Ref.11
	Modified residue	730	1	Phosphothreonine; by CDK1 By similarity
	Modified residue	735	1	Phosphothreonine Ref.10
	Modified residue	753	1	Phosphothreonine; by CDK1 By similarity
	Modified residue	759	1	Phosphoserine Ref.7 Ref.9 Ref.10
	Modified residue	765	1	Phosphoserine Ref.9
	Modified residue	789	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	1 – 24	24	MDDFE…LEAER → MLGGSGSHGRRSLAALSQ in isoform 3 and isoform 5.		VSP_004154
	Alternative sequence	208 – 462	255	Missing in isoform 4 and isoform 5.		VSP_004156
	Alternative sequence	208 – 436	229	Missing in isoform 2 and isoform 3.		VSP_004155
	Natural variant	397	1	H → R. Ref.2 Corresponds to variant rs6973420 [ dbSNP | Ensembl ].		VAR_065254
Experimental info
	Sequence conflict	530	1	V → M in AAA35636. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (H-CAD) [UniParc]. Last modified June 28, 2011. Version 3. Checksum: 7468E2C3E40BF697	FASTA	793	93,231
	10 20 30 40 50 60 MDDFERRREL RRQKREEMRL EAERIAYQRN DDDEEEAARE RRRRARQERL RQKQEEESLG 70 80 90 100 110 120 QVTDQVEVNA QNSVPDEEAK TTTTNTQVEG DDEAAFLERL ARREERRQKR LQEALERQKE 130 140 150 160 170 180 FDPTITDASL SLPSRRMQND TAENETTEKE EKSESRQERY EIEETETVTK SYQKNDWRDA 190 200 210 220 230 240 EENKKEDKEK EEEEEEKPKR GSIGENQVEV MVEEKTTESQ EETVVMSLKN GQISSEEPKQ 250 260 270 280 290 300 EEEREQGSDE ISHHEKMEEE DKERAEAERA RLEAEERERI KAEQDKKIAD ERARIEAEEK 310 320 330 340 350 360 AAAQERERRE AEERERMREE EKRAAEERQR IKEEEKRAAE ERQRIKEEEK RAAEERQRIK 370 380 390 400 410 420 EEEKRAAEER QRARAEEEEK AKVEEQKRNK QLEEKKHAMQ ETKIKGEKVE QKIEGKWVNE 430 440 450 460 470 480 KKAQEDKLQT AVLKKQGEEK GTKVQAKREK LQEDKPTFKK EEIKDEKIKK DKEPKEEVKS 490 500 510 520 530 540 FMDRKKGFTE VKSQNGEFMT HKLKHTENTF SRPGGRASVD TKEAEGAPQV EAGKRLEELR 550 560 570 580 590 600 RRRGETESEE FEKLKQKQQE AALELEELKK KREERRKVLE EEEQRRKQEE ADRKLREEEE 610 620 630 640 650 660 KRRLKEEIER RRAEAAEKRQ KMPEDGLSDD KKPFKCFTPK GSSLKIEERA EFLNKSVQKS 670 680 690 700 710 720 SGVKSTHQAA IVSKIDSRLE QYTSAIEGTK SAKPTKPAAS DLPVPAEGVR NIKSMWEKGN 730 740 750 760 770 780 VFSSPTAAGT PNKETAGLKV GVSSRINEWL TKTPDGNKSP APKPSDLRPG DVSSKRNLWE 790 KQSVDKVTSP TKV
	Isoform 2 (WI-38 L-CAD I) [UniParc]. Checksum: 57791B75720D2902	FASTA	564	65,707
	10 20 30 40 50 60 MDDFERRREL RRQKREEMRL EAERIAYQRN DDDEEEAARE RRRRARQERL RQKQEEESLG 70 80 90 100 110 120 QVTDQVEVNA QNSVPDEEAK TTTTNTQVEG DDEAAFLERL ARREERRQKR LQEALERQKE 130 140 150 160 170 180 FDPTITDASL SLPSRRMQND TAENETTEKE EKSESRQERY EIEETETVTK SYQKNDWRDA 190 200 210 220 230 240 EENKKEDKEK EEEEEEKPKR GSIGENQGEE KGTKVQAKRE KLQEDKPTFK KEEIKDEKIK 250 260 270 280 290 300 KDKEPKEEVK SFMDRKKGFT EVKSQNGEFM THKLKHTENT FSRPGGRASV DTKEAEGAPQ 310 320 330 340 350 360 VEAGKRLEEL RRRRGETESE EFEKLKQKQQ EAALELEELK KKREERRKVL EEEEQRRKQE 370 380 390 400 410 420 EADRKLREEE EKRRLKEEIE RRRAEAAEKR QKMPEDGLSD DKKPFKCFTP KGSSLKIEER 430 440 450 460 470 480 AEFLNKSVQK SSGVKSTHQA AIVSKIDSRL EQYTSAIEGT KSAKPTKPAA SDLPVPAEGV 490 500 510 520 530 540 RNIKSMWEKG NVFSSPTAAG TPNKETAGLK VGVSSRINEW LTKTPDGNKS PAPKPSDLRP 550 560 GDVSSKRNLW EKQSVDKVTS PTKV
	Isoform 3 (HELA L-CAD I) [UniParc]. Checksum: AA511974B9C483DC	FASTA	558	64,256
	10 20 30 40 50 60 MLGGSGSHGR RSLAALSQIA YQRNDDDEEE AARERRRRAR QERLRQKQEE ESLGQVTDQV 70 80 90 100 110 120 EVNAQNSVPD EEAKTTTTNT QVEGDDEAAF LERLARREER RQKRLQEALE RQKEFDPTIT 130 140 150 160 170 180 DASLSLPSRR MQNDTAENET TEKEEKSESR QERYEIEETE TVTKSYQKND WRDAEENKKE 190 200 210 220 230 240 DKEKEEEEEE KPKRGSIGEN QGEEKGTKVQ AKREKLQEDK PTFKKEEIKD EKIKKDKEPK 250 260 270 280 290 300 EEVKSFMDRK KGFTEVKSQN GEFMTHKLKH TENTFSRPGG RASVDTKEAE GAPQVEAGKR 310 320 330 340 350 360 LEELRRRRGE TESEEFEKLK QKQQEAALEL EELKKKREER RKVLEEEEQR RKQEEADRKL 370 380 390 400 410 420 REEEEKRRLK EEIERRRAEA AEKRQKMPED GLSDDKKPFK CFTPKGSSLK IEERAEFLNK 430 440 450 460 470 480 SVQKSSGVKS THQAAIVSKI DSRLEQYTSA IEGTKSAKPT KPAASDLPVP AEGVRNIKSM 490 500 510 520 530 540 WEKGNVFSSP TAAGTPNKET AGLKVGVSSR INEWLTKTPD GNKSPAPKPS DLRPGDVSSK 550 RNLWEKQSVD KVTSPTKV
	Isoform 4 (WI-38 L-CAD II) (1-CAD) [UniParc]. Checksum: 7EBF78B53217E77A	FASTA	538	62,663
	10 20 30 40 50 60 MDDFERRREL RRQKREEMRL EAERIAYQRN DDDEEEAARE RRRRARQERL RQKQEEESLG 70 80 90 100 110 120 QVTDQVEVNA QNSVPDEEAK TTTTNTQVEG DDEAAFLERL ARREERRQKR LQEALERQKE 130 140 150 160 170 180 FDPTITDASL SLPSRRMQND TAENETTEKE EKSESRQERY EIEETETVTK SYQKNDWRDA 190 200 210 220 230 240 EENKKEDKEK EEEEEEKPKR GSIGENQIKD EKIKKDKEPK EEVKSFMDRK KGFTEVKSQN 250 260 270 280 290 300 GEFMTHKLKH TENTFSRPGG RASVDTKEAE GAPQVEAGKR LEELRRRRGE TESEEFEKLK 310 320 330 340 350 360 QKQQEAALEL EELKKKREER RKVLEEEEQR RKQEEADRKL REEEEKRRLK EEIERRRAEA 370 380 390 400 410 420 AEKRQKMPED GLSDDKKPFK CFTPKGSSLK IEERAEFLNK SVQKSSGVKS THQAAIVSKI 430 440 450 460 470 480 DSRLEQYTSA IEGTKSAKPT KPAASDLPVP AEGVRNIKSM WEKGNVFSSP TAAGTPNKET 490 500 510 520 530 AGLKVGVSSR INEWLTKTPD GNKSPAPKPS DLRPGDVSSK RNLWEKQSVD KVTSPTKV
	Isoform 5 (HELA L-CAD II) [UniParc]. Checksum: 2A222B2C1AD79975	FASTA	532	61,213
	10 20 30 40 50 60 MLGGSGSHGR RSLAALSQIA YQRNDDDEEE AARERRRRAR QERLRQKQEE ESLGQVTDQV 70 80 90 100 110 120 EVNAQNSVPD EEAKTTTTNT QVEGDDEAAF LERLARREER RQKRLQEALE RQKEFDPTIT 130 140 150 160 170 180 DASLSLPSRR MQNDTAENET TEKEEKSESR QERYEIEETE TVTKSYQKND WRDAEENKKE 190 200 210 220 230 240 DKEKEEEEEE KPKRGSIGEN QIKDEKIKKD KEPKEEVKSF MDRKKGFTEV KSQNGEFMTH 250 260 270 280 290 300 KLKHTENTFS RPGGRASVDT KEAEGAPQVE AGKRLEELRR RRGETESEEF EKLKQKQQEA 310 320 330 340 350 360 ALELEELKKK REERRKVLEE EEQRRKQEEA DRKLREEEEK RRLKEEIERR RAEAAEKRQK 370 380 390 400 410 420 MPEDGLSDDK KPFKCFTPKG SSLKIEERAE FLNKSVQKSS GVKSTHQAAI VSKIDSRLEQ 430 440 450 460 470 480 YTSAIEGTKS AKPTKPAASD LPVPAEGVRN IKSMWEKGNV FSSPTAAGTP NKETAGLKVG 490 500 510 520 530 VSSRINEWLT KTPDGNKSPA PKPSDLRPGD VSSKRNLWEK QSVDKVTSPT KV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of cDNA clones encoding a human fibroblast caldesmon isoform and analysis of caldesmon expression in normal and transformed cells." Novy R.E., Lin J.L.-C., Lin J.J.-C. J. Biol. Chem. 266:16917-16924(1991) [PubMed: 1885618] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). Tissue: Lung fibroblast.
[2]	"Cloning of cDNAs encoding human caldesmons." Humphrey M.B., Herrera-Sosa H., Gonzalez G., Lee R., Bryan J. Gene 112:197-204(1992) [PubMed: 1555769] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), VARIANT ARG-397. Tissue: Aorta.
[3]	"Genomic structure of the human caldesmon gene." Hayashi K., Yano H., Hashida T., Takeuchi R., Takeda O., Asada K., Takahashi E., Kato I., Sobue K. Proc. Natl. Acad. Sci. U.S.A. 89:12122-12126(1992) [PubMed: 1465449] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
[4]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Skin.
[6]	"Identification of functioning regulatory sites and a new myosin binding site in the C-terminal 288 amino acids of caldesmon expressed from a human clone." Huber P.A.J., Redwood C.S., Avent N.D., Tanner M.J.A., Marston S.B. J. Muscle Res. Cell Motil. 14:385-391(1993) [PubMed: 8227296] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 497-793, FUNCTION. Tissue: Fetal liver.
[7]	"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 TYR-27; SER-202; SER-724; THR-730 AND SER-759, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656; SER-723; SER-724 AND THR-730, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-759 AND SER-765, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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 SER-656; SER-724; THR-730; THR-735; THR-753; SER-759 AND SER-789, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-724; THR-726 AND THR-730, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-682, MASS SPECTROMETRY. Tissue: Mammary epithelium.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64110 mRNA. Translation: AAA35636.1. M83216 mRNA. Translation: AAA58420.1. M83216 mRNA. Translation: AAA58419.1. D90452 mRNA. Translation: BAA14418.1. D90453 mRNA. Translation: BAA14419.1. AC019014 Genomic DNA. No translation available. AC083870 Genomic DNA. No translation available. BC040354 mRNA. Translation: AAH40354.1.
IPI	IPI00014516. IPI00218694. IPI00218695. IPI00333771. IPI01013595.
PIR	JH0628.
RefSeq	NP_004333.1. NM_004342.6. NP_149129.2. NM_033138.3. NP_149130.1. NM_033139.3. NP_149131.1. NM_033140.3.
UniGene	Hs.490203.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q05682. 6 interactions.
STRING	Q05682.
PTM databases
PhosphoSite	Q05682.
Polymorphism databases
DMDM	2498204.
2D gel databases
OGP	Q05682.
Proteomic databases
PRIDE	Q05682.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361675; ENSP00000354826; ENSG00000122786.
GeneID	800.
KEGG	hsa:800.
UCSC	uc003vrz.1. human.
Organism-specific databases
CTD	800.
GeneCards	GC07P134429.
H-InvDB	HIX0007104.
HGNC	HGNC:1441. CALD1.
HPA	CAB000006. HPA008066. HPA017330.
MIM	114213. gene.
neXtProt	NX_Q05682.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10813.
HOGENOM	HBG278755.
HOVERGEN	HBG050785.
InParanoid	Q05682.
PhylomeDB	Q05682.
Enzyme and pathway databases
Reactome	REACT_17044. Muscle contraction.
Gene expression databases
ArrayExpress	Q05682.
Bgee	Q05682.
CleanEx	HS_CAD. HS_CALD1.
Genevestigator	Q05682.
GermOnline	ENSG00000122786. Homo sapiens.
Family and domain databases
InterPro	IPR006017. Caldesmon. IPR006018. Caldesmon_LSP. [Graphical view]
KO	K12327.
Pfam	PF02029. Caldesmon. 1 hit. [Graphical view]
PRINTS	PR01076. CALDESMON.
ProtoNet	Search...
Other
NextBio	3252.
SOURCE	Search...

Entry information

Entry name

CALD1_HUMAN

Accession

Primary (citable) accession number: Q05682
Secondary accession number(s): Q13978 , Q13979, Q14741, Q14742, Q9UD91

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	June 28, 2011
Last modified:	January 25, 2012
This is version 114 of the entry and version 3 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.