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Q05682

- CALD1_HUMAN

UniProt

Q05682 - CALD1_HUMAN

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Protein

Caldesmon

Gene

CALD1

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

Functioni

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).By similarity

GO - Molecular functioni

  1. actin binding Source: ProtInc
  2. calmodulin binding Source: ProtInc
  3. tropomyosin binding Source: ProtInc

GO - Biological processi

  1. cellular component movement Source: UniProtKB
  2. muscle contraction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_20558. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Caldesmon
Short name:
CDM
Gene namesi
Name:CALD1
Synonyms:CAD, CDM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:1441. CALD1.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Cytoplasmmyofibril By similarity
Note: On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle).By similarity

GO - Cellular componenti

  1. actin cap Source: Ensembl
  2. actin cytoskeleton Source: HPA
  3. cytoskeleton Source: UniProtKB
  4. cytosol Source: Reactome
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26034.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 793793CaldesmonPRO_0000089288Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731Phosphoserine1 Publication
Modified residuei643 – 6431Phosphoserine1 Publication
Modified residuei724 – 7241Phosphoserine2 Publications
Modified residuei730 – 7301Phosphothreonine4 Publications
Modified residuei753 – 7531Phosphothreonine2 Publications
Modified residuei759 – 7591PhosphoserineBy similarity
Modified residuei789 – 7891Phosphoserine2 Publications

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ05682.
PaxDbiQ05682.
PRIDEiQ05682.

2D gel databases

OGPiQ05682.

PTM databases

PhosphoSiteiQ05682.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ05682.
CleanExiHS_CAD.
HS_CALD1.
ExpressionAtlasiQ05682. baseline and differential.
GenevestigatoriQ05682.

Organism-specific databases

HPAiCAB000006.
HPA008066.
HPA017330.

Interactioni

Protein-protein interaction databases

BioGridi107251. 25 interactions.
IntActiQ05682. 7 interactions.
STRINGi9606.ENSP00000354826.

Structurei

3D structure databases

ProteinModelPortaliQ05682.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati319 – 332141Add
BLAST
Repeati333 – 346142Add
BLAST
Repeati347 – 360143Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 207182Myosin and calmodulin-bindingBy similarityAdd
BLAST
Regioni319 – 375573 X 14 AA tandem repeats of E-E-E-K-R-A-A-E-E-R-Q-R-I-KAdd
BLAST
Regioni564 – 62158Tropomyosin-bindingSequence AnalysisAdd
BLAST
Regioni653 – 68634Strong actin-bindingBy similarityAdd
BLAST
Regioni664 – 67411Tropomyosin-bindingSequence AnalysisAdd
BLAST
Regioni716 – 7227Calmodulin-bindingBy similarity
Regioni768 – 79326Weak actin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 468Poly-Arg
Compositional biasi81 – 866Poly-Thr
Compositional biasi189 – 1968Poly-Glu
Compositional biasi376 – 3794Poly-Glu
Compositional biasi540 – 5434Poly-Arg
Compositional biasi580 – 5834Poly-Glu
Compositional biasi597 – 6004Poly-Glu

Domaini

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.

Sequence similaritiesi

Belongs to the caldesmon family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG253189.
GeneTreeiENSGT00730000111125.
HOGENOMiHOG000013012.
HOVERGENiHBG050785.
InParanoidiQ05682.
KOiK12327.
OMAiTHKLKHA.
OrthoDBiEOG7FNC7W.
PhylomeDBiQ05682.
TreeFamiTF331771.

Family and domain databases

InterProiIPR006017. Caldesmon.
IPR006018. Caldesmon_LSP.
[Graphical view]
PANTHERiPTHR18949. PTHR18949. 1 hit.
PTHR18949:SF0. PTHR18949:SF0. 1 hit.
PfamiPF02029. Caldesmon. 2 hits.
[Graphical view]
PRINTSiPR01076. CALDESMON.

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q05682-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDDFERRREL RRQKREEMRL EAERIAYQRN DDDEEEAARE RRRRARQERL
60 70 80 90 100
RQKQEEESLG QVTDQVEVNA QNSVPDEEAK TTTTNTQVEG DDEAAFLERL
110 120 130 140 150
ARREERRQKR LQEALERQKE FDPTITDASL SLPSRRMQND TAENETTEKE
160 170 180 190 200
EKSESRQERY EIEETETVTK SYQKNDWRDA EENKKEDKEK EEEEEEKPKR
210 220 230 240 250
GSIGENQVEV MVEEKTTESQ EETVVMSLKN GQISSEEPKQ EEEREQGSDE
260 270 280 290 300
ISHHEKMEEE DKERAEAERA RLEAEERERI KAEQDKKIAD ERARIEAEEK
310 320 330 340 350
AAAQERERRE AEERERMREE EKRAAEERQR IKEEEKRAAE ERQRIKEEEK
360 370 380 390 400
RAAEERQRIK EEEKRAAEER QRARAEEEEK AKVEEQKRNK QLEEKKHAMQ
410 420 430 440 450
ETKIKGEKVE QKIEGKWVNE KKAQEDKLQT AVLKKQGEEK GTKVQAKREK
460 470 480 490 500
LQEDKPTFKK EEIKDEKIKK DKEPKEEVKS FMDRKKGFTE VKSQNGEFMT
510 520 530 540 550
HKLKHTENTF SRPGGRASVD TKEAEGAPQV EAGKRLEELR RRRGETESEE
560 570 580 590 600
FEKLKQKQQE AALELEELKK KREERRKVLE EEEQRRKQEE ADRKLREEEE
610 620 630 640 650
KRRLKEEIER RRAEAAEKRQ KMPEDGLSDD KKPFKCFTPK GSSLKIEERA
660 670 680 690 700
EFLNKSVQKS SGVKSTHQAA IVSKIDSRLE QYTSAIEGTK SAKPTKPAAS
710 720 730 740 750
DLPVPAEGVR NIKSMWEKGN VFSSPTAAGT PNKETAGLKV GVSSRINEWL
760 770 780 790
TKTPDGNKSP APKPSDLRPG DVSSKRNLWE KQSVDKVTSP TKV
Length:793
Mass (Da):93,231
Last modified:June 28, 2011 - v3
Checksum:i7468E2C3E40BF697
GO
Isoform 2 (identifier: Q05682-2) [UniParc]FASTAAdd to Basket

Also known as: WI-38 L-CAD I

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

Note: Contains a phosphoserine at position 202.

Show »
Length:564
Mass (Da):65,707
Checksum:i57791B75720D2902
GO
Isoform 3 (identifier: Q05682-3) [UniParc]FASTAAdd to Basket

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.

Note: Contains a phosphoserine at position 196. Contains a phosphoserine at position 12. Contains a phosphotyrosine at position 21.

Show »
Length:558
Mass (Da):64,256
Checksum:iAA511974B9C483DC
GO
Isoform 4 (identifier: Q05682-4) [UniParc]FASTAAdd to Basket

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.

Note: Contains a phosphoserine at position 202.

Show »
Length:538
Mass (Da):62,663
Checksum:i7EBF78B53217E77A
GO
Isoform 5 (identifier: Q05682-5) [UniParc]FASTAAdd to Basket

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.

Note: Contains a phosphoserine at position 196. Contains a phosphoserine at position 12. Contains a phosphotyrosine at position 21.

Show »
Length:532
Mass (Da):61,213
Checksum:i2A222B2C1AD79975
GO
Isoform 6 (identifier: Q05682-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     208-436: Missing.
     660-660: Missing.

Note: No experimental confirmation available. Contains a phosphoserine at position 202.

Show »
Length:563
Mass (Da):65,620
Checksum:iFF15BFCFCF19C248
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti530 – 5301V → M in AAA35636. (PubMed:1885618)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti397 – 3971H → R.1 Publication
Corresponds to variant rs6973420 [ dbSNP | Ensembl ].
VAR_065254

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2424MDDFE…LEAER → MLGGSGSHGRRSLAALSQ in isoform 3 and isoform 5. 1 PublicationVSP_004154Add
BLAST
Alternative sequencei208 – 462255Missing in isoform 4 and isoform 5. 4 PublicationsVSP_004156Add
BLAST
Alternative sequencei208 – 436229Missing in isoform 2, isoform 3 and isoform 6. 2 PublicationsVSP_004155Add
BLAST
Alternative sequencei660 – 6601Missing in isoform 6. 1 PublicationVSP_043292

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK289686 mRNA. Translation: BAF82375.1.
AC019014 Genomic DNA. No translation available.
AC083870 Genomic DNA. No translation available.
BC040354 mRNA. Translation: AAH40354.1.
CCDSiCCDS47716.1. [Q05682-3]
CCDS47717.1. [Q05682-5]
CCDS5834.1. [Q05682-4]
CCDS5835.1. [Q05682-1]
CCDS5836.2. [Q05682-6]
PIRiJH0628.
RefSeqiNP_004333.1. NM_004342.6. [Q05682-4]
NP_149129.2. NM_033138.3. [Q05682-1]
NP_149130.1. NM_033139.3. [Q05682-3]
NP_149131.1. NM_033140.3. [Q05682-5]
NP_149347.2. NM_033157.3. [Q05682-6]
UniGeneiHs.490203.

Genome annotation databases

EnsembliENST00000361675; ENSP00000354826; ENSG00000122786. [Q05682-1]
ENST00000361901; ENSP00000354513; ENSG00000122786. [Q05682-4]
ENST00000393118; ENSP00000376826; ENSG00000122786. [Q05682-3]
ENST00000417172; ENSP00000398826; ENSG00000122786. [Q05682-4]
ENST00000422748; ENSP00000395710; ENSG00000122786. [Q05682-6]
ENST00000424922; ENSP00000393621; ENSG00000122786. [Q05682-5]
GeneIDi800.
KEGGihsa:800.
UCSCiuc003vrz.3. human. [Q05682-1]
uc003vsb.3. human. [Q05682-4]
uc003vsc.3. human. [Q05682-3]
uc003vsd.3. human. [Q05682-5]
uc010lmm.3. human. [Q05682-6]

Polymorphism databases

DMDMi338817891.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
AK289686 mRNA. Translation: BAF82375.1 .
AC019014 Genomic DNA. No translation available.
AC083870 Genomic DNA. No translation available.
BC040354 mRNA. Translation: AAH40354.1 .
CCDSi CCDS47716.1. [Q05682-3 ]
CCDS47717.1. [Q05682-5 ]
CCDS5834.1. [Q05682-4 ]
CCDS5835.1. [Q05682-1 ]
CCDS5836.2. [Q05682-6 ]
PIRi JH0628.
RefSeqi NP_004333.1. NM_004342.6. [Q05682-4 ]
NP_149129.2. NM_033138.3. [Q05682-1 ]
NP_149130.1. NM_033139.3. [Q05682-3 ]
NP_149131.1. NM_033140.3. [Q05682-5 ]
NP_149347.2. NM_033157.3. [Q05682-6 ]
UniGenei Hs.490203.

3D structure databases

ProteinModelPortali Q05682.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107251. 25 interactions.
IntActi Q05682. 7 interactions.
STRINGi 9606.ENSP00000354826.

PTM databases

PhosphoSitei Q05682.

Polymorphism databases

DMDMi 338817891.

2D gel databases

OGPi Q05682.

Proteomic databases

MaxQBi Q05682.
PaxDbi Q05682.
PRIDEi Q05682.

Protocols and materials databases

DNASUi 800.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361675 ; ENSP00000354826 ; ENSG00000122786 . [Q05682-1 ]
ENST00000361901 ; ENSP00000354513 ; ENSG00000122786 . [Q05682-4 ]
ENST00000393118 ; ENSP00000376826 ; ENSG00000122786 . [Q05682-3 ]
ENST00000417172 ; ENSP00000398826 ; ENSG00000122786 . [Q05682-4 ]
ENST00000422748 ; ENSP00000395710 ; ENSG00000122786 . [Q05682-6 ]
ENST00000424922 ; ENSP00000393621 ; ENSG00000122786 . [Q05682-5 ]
GeneIDi 800.
KEGGi hsa:800.
UCSCi uc003vrz.3. human. [Q05682-1 ]
uc003vsb.3. human. [Q05682-4 ]
uc003vsc.3. human. [Q05682-3 ]
uc003vsd.3. human. [Q05682-5 ]
uc010lmm.3. human. [Q05682-6 ]

Organism-specific databases

CTDi 800.
GeneCardsi GC07P134429.
HGNCi HGNC:1441. CALD1.
HPAi CAB000006.
HPA008066.
HPA017330.
MIMi 114213. gene.
neXtProti NX_Q05682.
PharmGKBi PA26034.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG253189.
GeneTreei ENSGT00730000111125.
HOGENOMi HOG000013012.
HOVERGENi HBG050785.
InParanoidi Q05682.
KOi K12327.
OMAi THKLKHA.
OrthoDBi EOG7FNC7W.
PhylomeDBi Q05682.
TreeFami TF331771.

Enzyme and pathway databases

Reactomei REACT_20558. Smooth Muscle Contraction.

Miscellaneous databases

ChiTaRSi CALD1. human.
GeneWikii Caldesmon.
GenomeRNAii 800.
NextBioi 3252.
PROi Q05682.
SOURCEi Search...

Gene expression databases

Bgeei Q05682.
CleanExi HS_CAD.
HS_CALD1.
ExpressionAtlasi Q05682. baseline and differential.
Genevestigatori Q05682.

Family and domain databases

InterProi IPR006017. Caldesmon.
IPR006018. Caldesmon_LSP.
[Graphical view ]
PANTHERi PTHR18949. PTHR18949. 1 hit.
PTHR18949:SF0. PTHR18949:SF0. 1 hit.
Pfami PF02029. Caldesmon. 2 hits.
[Graphical view ]
PRINTSi PR01076. CALDESMON.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    Tissue: Lung fibroblast.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), VARIANT ARG-397.
    Tissue: Aorta.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    Tissue: Amygdala.
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 4).
    Tissue: Skin.
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 497-793, FUNCTION.
    Tissue: Fetal liver.
  8. "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 THR-730, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-730, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724; THR-730; THR-753 AND SER-789, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-724; THR-730 AND THR-753, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; TYR-21 AND SER-196 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-643 AND SER-789, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCALD1_HUMAN
AccessioniPrimary (citable) accession number: Q05682
Secondary accession number(s): A8K0X1
, Q13978, Q13979, Q14741, Q14742, Q9UD91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 28, 2011
Last modified: October 29, 2014
This is version 143 of the entry and version 3 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 7
    Human chromosome 7: 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