Phospho-ACTN1/2/3/4 (Ser159) Antibody - #AF3766

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Product: Phospho-ACTN1/2/3/4 (Ser159) Antibody
Catalog: AF3766
Description: Rabbit polyclonal antibody to Phospho-ACTN1/2/3/4 (Ser159)
Application: WB
Reactivity: Human, Mouse, Rat
Mol.Wt.: 103kD,104kD,105kD(Calculated).
Uniprot: P12814 | P35609 | Q08043 | O43707
RRID: AB_2847080

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MSDS
Data Sheet
COA
Protocols
WB Handbook
IHC Protocol
IF/ICC Protocol

Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Clonality:
Polyclonal
Specificity:
Phospho-ACTN1/2/3/4 (Ser159) Antibody detects endogenous levels of ACTN1/2/3/4 only when phosphorylated at Ser159.
RRID:
AB_2847080
Cite Format: Affinity Biosciences Cat# AF3766, RRID:AB_2847080.
Conjugate:
Unconjugated.
Purification:
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

actinin 4; Actinin alpha 4; actinin4; ACTN 4; ACTN4; ACTN4_HUMAN; Alpha-actinin-4; DKFZp686K23158; F actin cross linking protein; F-actin cross-linking protein; Focal segmental glomerulosclerosis 1; FSGS 1; FSGS; FSGS1; Non muscle alpha actinin 4; Non-muscle alpha-actinin 4; actinin 1 smooth muscle; Actinin alpha 1; actinin, alpha 1; ACTN 1; Actn1; ACTN1_HUMAN; Alpha Actinin 1; Alpha actinin cytoskeletal isoform; Alpha-actinin cytoskeletal isoform; Alpha-actinin-1; BDPLT15; F actin cross linking protein; F-actin cross-linking protein; FLJ40884; FLJ54432; Non muscle alpha actinin 1; Non-muscle alpha-actinin-1; Actin binding protein; Actinin alpha 2; ACTN 2; ACTN2; ACTN2_HUMAN; Alpha actinin 2; Alpha actinin skeletal muscle; Alpha actinin skeletal muscle isoform 2; Alpha-actinin skeletal muscle isoform 2; Alpha-actinin-2; CMD1AA; F actin cross linking protein; F-actin cross-linking protein; Actinin alpha 3; actinin, alpha; ACTN 3; ACTN3; ACTN3_HUMAN; Alpha actinin skeletal muscle; Alpha actinin skeletal muscle

Immunogens

Immunogen:

A synthesized peptide derived from human ACTN1/2/3/4 around the phosphorylation site of Ser159.

Uniprot:

P12814(ACTN1_HUMAN) >>Visit HPA database.

P35609(ACTN2_HUMAN) >>Visit HPA database.

Q08043(ACTN3_HUMAN) >>Visit HPA database.

O43707(ACTN4_HUMAN) >>Visit HPA database.

Gene(ID):
ACTN4(81) | ACTN2(88) | ACTN3(89) | ACTN1(87)
Expression:
P35609 ACTN2_HUMAN:

Expressed in both skeletal and cardiac muscle.

Q08043 ACTN3_HUMAN:

Expressed only in a subset of type 2 skeletal muscle fibers.

O43707 ACTN4_HUMAN:

Widely expressed.

Sequence:
MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRVPENTMHAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQVEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHARQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDPQGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITMDELRRELPPDQAEYCIARMAPYTGPDSVPGALDYMSFSTALYGESDL

MNQIEPGVQYNYVYDEDEYMIQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENERLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQKKLEDFRDYRRKHKPPKVQEKCQLEINFNTLQTKLRISNRPAFMPSEGKMVSDIAGAWQRLEQAEKGYEEWLLNEIRRLERLEHLAEKFRQKASTHETWAYGKEQILLQKDYESASLTEVRALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYHDAVNVNDRCQKICDQWDRLGTLTQKRREALERMEKLLETIDQLHLEFAKRAAPFNNWMEGAMEDLQDMFIVHSIEEIQSLITAHEQFKATLPEADGERQSIMAIQNEVEKVIQSYNIRISSSNPYSTVTMDELRTKWDKVKQLVPIRDQSLQEELARQHANERLRRQFAAQANAIGPWIQNKMEEIARSSIQITGALEDQMNQLKQYEHNIINYKNNIDKLEGDHQLIQEALVFDNKHTNYTMEHIRVGWELLLTTIARTINEVETQILTRDAKGITQEQMNEFRASFNHFDRRKNGLMDHEDFRACLISMGYDLGEAEFARIMTLVDPNGQGTVTFQSFIDFMTRETADTDTAEQVIASFRILASDKPYILAEELRRELPPDQAQYCIKRMPAYSGPGSVPGALDYAAFSSALYGESDL

MMMVMQPEGLGAGEGRFAGGGGGGEYMEQEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENEKLMEEYEKLASELLEWIRRTVPWLENRVGEPSMSAMQRKLEDFRDYRRLHKPPRIQEKCQLEINFNTLQTKLRLSHRPAFMPSEGKLVSDIANAWRGLEQVEKGYEDWLLSEIRRLQRLQHLAEKFRQKASLHEAWTRGKEEMLSQRDYDSALLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVNSRCQAICDQWDNLGTLTQKRRDALERMEKLLETIDRLQLEFARRAAPFNNWLDGAVEDLQDVWLVHSVEETQSLLTAHDQFKATLPEADRERGAIMGIQGEIQKICQTYGLRPCSTNPYITLSPQDINTKWDMVRKLVPSCDQTLQEELARQQVNERLRRQFAAQANAIGPWIQAKVEEVGRLAAGLAGSLEEQMAGLRQQEQNIINYKTNIDRLEGDHQLLQESLVFDNKHTVYSMEHIRVGWEQLLTSIARTINEVENQVLTRDAKGLSQEQLNEFRASFNHFDRKQNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDFMTRETAETDTTEQVVASFKILAGDKNYITPEELRRELPAKQAEYCIRRMVPYKGSGAPAGALDYVAFSSALYGESDL

MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL

PTMs - P12814/P35609/Q08043/O43707 As Substrate

Site PTM Type Enzyme
K38 Ubiquitination
K42 Ubiquitination
K54 Ubiquitination
T57 Phosphorylation
R83 Methylation
K86 Methylation
Y106 Phosphorylation
S116 Phosphorylation
T130 Phosphorylation
S147 Phosphorylation
T151 Phosphorylation
S152 Phosphorylation
K181 Acetylation
Y200 Phosphorylation
S201 Phosphorylation
T237 Phosphorylation
S250 Phosphorylation
Y253 Phosphorylation
R268 Methylation
S291 Phosphorylation
Y326 Phosphorylation
K338 Ubiquitination
T347 Phosphorylation
T350 Phosphorylation
S355 Phosphorylation
Y385 Phosphorylation
S431 Phosphorylation
S433 Phosphorylation
T435 Phosphorylation
K443 Acetylation
K443 Ubiquitination
S449 Phosphorylation
K499 Acetylation
K523 Acetylation
S588 Phosphorylation
Y589 Phosphorylation
S594 Phosphorylation
S595 Phosphorylation
S596 Phosphorylation
Y599 Phosphorylation
Y681 Phosphorylation
Y715 Phosphorylation
S840 Phosphorylation
Y844 Phosphorylation
Y861 Phosphorylation
S892 Phosphorylation
Site PTM Type Enzyme
M1 Acetylation
K45 Ubiquitination
K49 Ubiquitination
K61 Ubiquitination
T64 Phosphorylation
R90 Methylation
R93 Methylation
S116 Phosphorylation
K117 Ubiquitination
T137 Phosphorylation
S154 Phosphorylation
T158 Phosphorylation
S159 Phosphorylation
K209 Sumoylation
K212 Sumoylation
Y229 Phosphorylation
K250 Acetylation
S257 Phosphorylation
Y260 Phosphorylation
R275 Methylation
K278 Acetylation
S298 Phosphorylation
S319 Phosphorylation
S321 Phosphorylation
Y333 Phosphorylation
T354 Phosphorylation
T357 Phosphorylation
S376 Phosphorylation
S418 Phosphorylation
Y436 Phosphorylation
S438 Phosphorylation
S456 Phosphorylation
K506 Acetylation
S737 Phosphorylation
Y851 Phosphorylation
Y876 Phosphorylation
Site PTM Type Enzyme
M1 Acetylation
Y4 Phosphorylation
S6 Phosphorylation
T9 Phosphorylation
Y12 Phosphorylation A0A059VC25 (FAK) , Q05397 (PTK2)
K31 Ubiquitination
K35 Ubiquitination
K47 Ubiquitination
T50 Phosphorylation
S73 Phosphorylation
K89 Ubiquitination
S91 Phosphorylation
K95 Acetylation
S102 Phosphorylation
K103 Ubiquitination
S109 Phosphorylation
T123 Phosphorylation
S140 Phosphorylation
T144 Phosphorylation
S145 Phosphorylation
C154 S-Nitrosylation
K162 Ubiquitination
S172 Phosphorylation
Y193 Phosphorylation
K195 Acetylation
K195 Ubiquitination
K198 Acetylation
K198 Ubiquitination
K214 Ubiquitination
Y215 Phosphorylation
K220 Ubiquitination
T230 Phosphorylation
Y241 Phosphorylation
S243 Phosphorylation
S244 Phosphorylation
Y246 Phosphorylation
S250 Phosphorylation
R261 Methylation
Y279 Phosphorylation
S284 Phosphorylation
R291 Methylation
Y319 Phosphorylation
K324 Ubiquitination
K327 Ubiquitination
K331 Ubiquitination
C332 S-Nitrosylation
T340 Phosphorylation
T343 Phosphorylation
S348 Phosphorylation
S356 Phosphorylation
S362 Phosphorylation
Y378 Phosphorylation
K398 Acetylation
K398 Ubiquitination
K402 Ubiquitination
S404 Phosphorylation
T410 Phosphorylation
K413 Ubiquitination
Y422 Phosphorylation
T426 Phosphorylation
S428 Phosphorylation
K431 Ubiquitination
K436 Acetylation
K436 Ubiquitination
S442 Phosphorylation
Y466 Phosphorylation
Y467 Phosphorylation
S471 Phosphorylation
K478 Ubiquitination
C480 S-Nitrosylation
K492 Acetylation
K492 Ubiquitination
K502 Ubiquitination
Y511 Phosphorylation
Y514 Phosphorylation
S576 Phosphorylation
Y582 Phosphorylation
K633 Ubiquitination
S669 Phosphorylation
Y674 Phosphorylation
K676 Acetylation
K676 Ubiquitination
S677 Phosphorylation
Y681 Phosphorylation
K684 Ubiquitination
Y708 Phosphorylation
T722 Phosphorylation
T727 Phosphorylation
T737 Phosphorylation
S744 Phosphorylation
S763 Phosphorylation
T765 Phosphorylation
S797 Phosphorylation
T820 Phosphorylation
T823 Phosphorylation
T825 Phosphorylation
S832 Phosphorylation
Y842 Phosphorylation
T844 Phosphorylation
Y859 Phosphorylation
Y887 Phosphorylation
S890 Phosphorylation
Site PTM Type Enzyme
Y4 Phosphorylation Q05397 (PTK2)
Y11 Phosphorylation
Y13 Phosphorylation
Y31 Phosphorylation Q05397 (PTK2)
K50 Ubiquitination
K54 Ubiquitination
K66 Ubiquitination
T69 Phosphorylation
S92 Phosphorylation
K108 Ubiquitination
K114 Acetylation
S121 Phosphorylation
K122 Ubiquitination
K125 Ubiquitination
T142 Phosphorylation
S159 Phosphorylation
T163 Phosphorylation
S164 Phosphorylation
K181 Ubiquitination
S191 Phosphorylation
Y212 Phosphorylation
K214 Acetylation
K214 Ubiquitination
K217 Acetylation
K217 Ubiquitination
K233 Acetylation
K233 Ubiquitination
Y234 Phosphorylation
K239 Ubiquitination
T249 Phosphorylation
Y260 Phosphorylation
S262 Phosphorylation
S263 Phosphorylation
Y265 Phosphorylation Q05397 (PTK2)
S269 Phosphorylation
R280 Methylation
K283 Acetylation
Y298 Phosphorylation
S303 Phosphorylation
R310 Methylation
T312 Phosphorylation
R319 Methylation
K323 Ubiquitination
T324 Phosphorylation
K331 Acetylation
K331 Ubiquitination
Y338 Phosphorylation
K346 Ubiquitination
K350 Ubiquitination
C351 S-Nitrosylation
T359 Phosphorylation
T362 Phosphorylation
S367 Phosphorylation
K378 Ubiquitination
S381 Phosphorylation
Y397 Phosphorylation
K417 Acetylation
K417 Ubiquitination
K421 Ubiquitination
S423 Phosphorylation
T429 Phosphorylation
K432 Acetylation
K432 Ubiquitination
K437 Acetylation
Y441 Phosphorylation
T445 Phosphorylation
S447 Phosphorylation
K450 Ubiquitination
K455 Acetylation
K455 Ubiquitination
S461 Phosphorylation
R469 Methylation
Y485 Phosphorylation
Y486 Phosphorylation
S488 Phosphorylation
T493 Phosphorylation
K497 Ubiquitination
C499 S-Nitrosylation
S507 Phosphorylation
T509 Phosphorylation
S511 Phosphorylation
K521 Ubiquitination
Y533 Phosphorylation
K592 Acetylation
K592 Ubiquitination
K604 Ubiquitination
S608 Phosphorylation
Y611 Phosphorylation
T612 Phosphorylation
T615 Phosphorylation
S621 Phosphorylation
K622 Acetylation
K622 Ubiquitination
K625 Acetylation
K625 Ubiquitination
K632 Ubiquitination
S642 Phosphorylation
K643 Ubiquitination
S656 Phosphorylation
T667 Phosphorylation
T682 Phosphorylation
Y693 Phosphorylation
S696 Phosphorylation
Y700 Phosphorylation
K701 Ubiquitination
Y727 Phosphorylation
T741 Phosphorylation
T746 Phosphorylation
T756 Phosphorylation
K760 Ubiquitination
S763 Phosphorylation
S773 Phosphorylation
K779 Acetylation
K779 Methylation
K779 Ubiquitination
C793 S-Nitrosylation
S796 Phosphorylation
R805 Methylation
T839 Phosphorylation
T840 Phosphorylation
T842 Phosphorylation
T844 Phosphorylation
K853 Acetylation
K859 Acetylation
K859 Ubiquitination
R868 Methylation
Y878 Phosphorylation
Y898 Phosphorylation
K899 Acetylation
Y906 Phosphorylation
S909 Phosphorylation

Research Backgrounds

Function:

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.

Subcellular Location:

Cytoplasm>Cytoskeleton. Cytoplasm>Myofibril>Sarcomere>Z line. Cell membrane. Cell junction. Cell projection>Ruffle.
Note: Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Homodimer; antiparallel. Interacts with MYOZ2, TTID and LPP. Interacts with DDN. Interacts with PSD. Interacts with MICALL2 (By similarity). Interacts with DNM2 and CTTN. Interacts with PDLIM1. Interacts with PDLIM2. Interacts with PDLIM4 (via PDZ domain) (By similarity).

Family&Domains:

Belongs to the alpha-actinin family.

Function:

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.

PTMs:

Ubiquitinated by FBXL22, leading to proteasomal degradation.

Subcellular Location:

Cytoplasm>Myofibril>Sarcomere>Z line.
Note: Colocalizes with MYOZ1 and FLNC at the Z-lines of skeletal muscle.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed in both skeletal and cardiac muscle.

Subunit Structure:

Homodimer; antiparallel. Also forms heterodimers with ACTN3. Interacts with ADAM12, MYOZ1, MYOZ2 and MYOZ3. Interacts via its C-terminal region with the LDB3 PDZ domain. Interacts with XIRP2. Interacts with DST isoform 1 (via N-terminus). Interacts with PARVB. Interacts with SYNPO2.

Family&Domains:

Belongs to the alpha-actinin family.

Function:

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.

Tissue Specificity:

Expressed only in a subset of type 2 skeletal muscle fibers.

Subunit Structure:

Homodimer; antiparallel. Also forms heterodimers with ACTN2. Interacts with MYOZ1.

Family&Domains:

Belongs to the alpha-actinin family.

Function:

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA.

Subcellular Location:

Nucleus. Cytoplasm. Cell junction. Cytoplasm>Cytoskeleton>Stress fiber.
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Nuclear translocation can be induced by the PI3 kinase inhibitor wortmannin or by cytochalasin D. Exclusively localized in the nucleus in a limited number of cell lines (breast cancer cell line MCF-7, oral floor cancer IMC-2, and bladder cancer KU-7).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Widely expressed.

Subunit Structure:

Homodimer; antiparallel (By similarity). Binds TRIM3 at the N-terminus (By similarity). Interacts with MICALL2 (preferentially in opened conformation); stimulated by RAB13 activation (By similarity). Identified in a complex with CASK, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1 (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and TRIM3. Interacts with BAIAP1 and PDLIM2. Interacts with PPARG and RARA. Binds to VCL; this interaction triggers VCL conformational changes.

Family&Domains:

Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif that mediates interaction with nuclear receptors.

Belongs to the alpha-actinin family.

Research Fields

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Adherens junction.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Tight junction.   (View pathway)

· Cellular Processes > Cell motility > Regulation of actin cytoskeleton.   (View pathway)

· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.

· Human Diseases > Cancers: Overview > Viral carcinogenesis.

· Human Diseases > Immune diseases > Systemic lupus erythematosus.

· Human Diseases > Cardiovascular diseases > Arrhythmogenic right ventricular cardiomyopathy (ARVC).

· Organismal Systems > Immune system > Leukocyte transendothelial migration.   (View pathway)

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