Reviewed, UniProtKB/Swiss-Prot O14639 (ABLM1_HUMAN)

Names and origin

Protein names

Recommended name:
    Actin-binding LIM protein 1
Alternative name(s):
    Actin-binding LIM protein family member 1
      Short name=abLIM-1
    Actin-binding double zinc finger protein
    LIMAB1
    Limatin

Gene names

Name:	ABLIM1
Synonyms:	ABLIM, KIAA0059, LIMAB1

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	778 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May act as scaffold protein By similarity. May play a role in the development of the retina. Has been suggested to play a role in axon guidance.
Subunit structure	Binds F-actin. Interacts with ABRA. Ref.7
Subcellular location	CytoplasmBy similarity. Cytoplasm › cytoskeletonBy similarity. Note= Associated with the cytoskeleton By similarity.
Tissue specificity	Detected in liver, heart, skeletal muscle, brain and retina, where it is concentrated in the inner segment and in the outer plexiform layers. Ref.1
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Sequence similarities	Contains 1 HP (headpiece) domain. Contains 4 LIM zinc-binding domains.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil LIM domain Repeat
Ligand	Actin-binding Metal-binding Zinc
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cytoskeleton organization Inferred from electronic annotation. Source: InterPro organ morphogenesis Ref.1 Traceable author statement. Source: ProtInc visual perception Ref.1 Traceable author statement. Source: ProtInc
Cellular component	actin cytoskeleton Ref.1 Traceable author statement. Source: ProtInc cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	actin binding Ref.1 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LDOC1	O95751	1	EBI-487024,EBI-740738

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O14639-1)

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: O14639-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: MPAFLGLKCL...GRVCNSVDPF → MLMTLEMTELTDPHHTMGDYK

Isoform 3 (identifier: O14639-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-316: Missing.
     480-514: Missing.

Isoform 4 (identifier: O14639-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-316: Missing.
     348-373: Missing.
     480-514: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 778	778	Actin-binding LIM protein 1		PRO_0000075697
Regions
	Domain	97 – 156	60	LIM zinc-binding 1
	Domain	156 – 216	61	LIM zinc-binding 2
	Domain	224 – 283	60	LIM zinc-binding 3
	Domain	283 – 343	61	LIM zinc-binding 4
	Domain	710 – 778	69	HP
	Coiled coil	590 – 614	25	Potential
Amino acid modifications
	Modified residue	216	1	Phosphoserine By similarity
	Modified residue	353	1	Phosphoserine By similarity
	Modified residue	357	1	Phosphotyrosine Ref.8
	Modified residue	367	1	Phosphoserine By similarity
	Modified residue	373	1	Phosphotyrosine Ref.8
	Modified residue	396	1	Phosphotyrosine Ref.10
	Modified residue	406	1	Phosphotyrosine Ref.10
	Modified residue	410	1	Phosphotyrosine Ref.10
	Modified residue	431	1	Phosphoserine Ref.9 Ref.14 Ref.15
	Modified residue	435	1	Phosphoserine Ref.8 Ref.15
	Modified residue	439	1	Phosphotyrosine Ref.8
	Modified residue	450	1	Phosphoserine By similarity
	Modified residue	452	1	Phosphoserine Ref.9 Ref.13
	Modified residue	455	1	Phosphoserine Ref.15
	Modified residue	458	1	Phosphoserine Ref.13 Ref.15
	Modified residue	461	1	Phosphotyrosine Ref.8 Ref.11
	Modified residue	473	1	Phosphoserine Ref.12
	Modified residue	587	1	Phosphoserine Ref.15
	Modified residue	640	1	Phosphoserine Ref.15
	Modified residue	655	1	Phosphoserine Ref.9 Ref.15
	Modified residue	706	1	Phosphoserine Ref.9 Ref.15
Natural variations
	Alternative sequence	1 – 316	316	Missing in isoform 3 and isoform 4.		VSP_012099
	Alternative sequence	1 – 81	81	MPAFL…SVDPF → MLMTLEMTELTDPHHTMGDY K in isoform 2.		VSP_012100
	Alternative sequence	348 – 373	26	Missing in isoform 4.		VSP_012101
	Alternative sequence	480 – 514	35	Missing in isoform 3 and isoform 4.		VSP_012102
	Natural variant	434	1	P → T: dbSNP rs11593544.		VAR_050141
	Natural variant	637	1	R → G: dbSNP rs7091419.		VAR_050142
Experimental info
	Sequence conflict	499	1	R → L in AAC51676. Ref.1
	Sequence conflict	532	1	A → R in AAC51676. Ref.1
	Sequence conflict	563	1	K → E in BAA06681. Ref.2
	Sequence conflict	578	1	V → I in BAA06681. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 23, 2008. Version 3. Checksum: EBC2F14BE558752B	FASTA	778	87,688
	10 20 30 40 50 60 MPAFLGLKCL GKLCSSEKSK VTSSERTSAR GSNRKRLIVE DRRVSGTSFT AHRRATITHL 70 80 90 100 110 120 LYLCPKDYCP RGRVCNSVDP FVAHPQDPHH PSEKPVIHCH KCGEPCKGEV LRVQTKHFHI 130 140 150 160 170 180 KCFTCKVCGC DLAQGGFFIK NGEYLCTLDY QRMYGTRCHG CGEFVEGEVV TALGKTYHPN 190 200 210 220 230 240 CFACTICKRP FPPGDRVTFN GRDCLCQLCA QPMSSSPKET TFSSNCAGCG RDIKNGQALL 250 260 270 280 290 300 ALDKQWHLGC FKCKSCGKVL TGEYISKDGA PYCEKDYQGL FGVKCEACHQ FITGKVLEAG 310 320 330 340 350 360 DKHYHPSCAR CSRCNQMFTE GEEMYLQGST VWHPDCKQST KTEEKLRPTR TSSESIYSRP 370 380 390 400 410 420 GSSIPGSPGH TIYAKVDNEI LDYKDLAAIP KVKAIYDIER PDLITYEPFY TSGYDDKQER 430 440 450 460 470 480 QSLGESPRTL SPTPSAEGYQ DVRDRMIHRS TSQGSINSPV YSRHSYTPTT SRSPQHFHRP 490 500 510 520 530 540 GNEPSSGRNS PLPYRPDSRP LTPTYAQAPK HFHVPDQGIN IYRKPPIYKQ HAALAAQSKS 550 560 570 580 590 600 SEDIIKFSKF PAAQAPDPSE TPKIETDHWP GPPSFAVVGP DMKRRSSGRE EDDEELLRRR 610 620 630 640 650 660 QLQEEQLMKL NSGLGQLILK EEMEKESRER SSLLASRYDS PINSASHIPS SKTASLPGYG 670 680 690 700 710 720 RNGLHRPVST DFAQYNSYGD VSGGVRDYQT LPDGHMPAMR MDRGVSMPNM LEPKIFPYEM 730 740 750 760 770 LMVTNRGRNK ILREVDRTRL ERHLAPEVFR EIFGMSIQEF DRLPLWRRND MKKKAKLF
	Isoform 2. Checksum: A9CAEEBA95BDF15E		718	81,121
	10 20 30 40 50 60 MLMTLEMTEL TDPHHTMGDY KVAHPQDPHH PSEKPVIHCH KCGEPCKGEV LRVQTKHFHI 70 80 90 100 110 120 KCFTCKVCGC DLAQGGFFIK NGEYLCTLDY QRMYGTRCHG CGEFVEGEVV TALGKTYHPN 130 140 150 160 170 180 CFACTICKRP FPPGDRVTFN GRDCLCQLCA QPMSSSPKET TFSSNCAGCG RDIKNGQALL 190 200 210 220 230 240 ALDKQWHLGC FKCKSCGKVL TGEYISKDGA PYCEKDYQGL FGVKCEACHQ FITGKVLEAG 250 260 270 280 290 300 DKHYHPSCAR CSRCNQMFTE GEEMYLQGST VWHPDCKQST KTEEKLRPTR TSSESIYSRP 310 320 330 340 350 360 GSSIPGSPGH TIYAKVDNEI LDYKDLAAIP KVKAIYDIER PDLITYEPFY TSGYDDKQER 370 380 390 400 410 420 QSLGESPRTL SPTPSAEGYQ DVRDRMIHRS TSQGSINSPV YSRHSYTPTT SRSPQHFHRP 430 440 450 460 470 480 GNEPSSGRNS PLPYRPDSRP LTPTYAQAPK HFHVPDQGIN IYRKPPIYKQ HAALAAQSKS 490 500 510 520 530 540 SEDIIKFSKF PAAQAPDPSE TPKIETDHWP GPPSFAVVGP DMKRRSSGRE EDDEELLRRR 550 560 570 580 590 600 QLQEEQLMKL NSGLGQLILK EEMEKESRER SSLLASRYDS PINSASHIPS SKTASLPGYG 610 620 630 640 650 660 RNGLHRPVST DFAQYNSYGD VSGGVRDYQT LPDGHMPAMR MDRGVSMPNM LEPKIFPYEM 670 680 690 700 710 LMVTNRGRNK ILREVDRTRL ERHLAPEVFR EIFGMSIQEF DRLPLWRRND MKKKAKLF
	Isoform 3. Checksum: 1721FB3EC1D99994		427	48,804
	10 20 30 40 50 60 MFTEGEEMYL QGSTVWHPDC KQSTKTEEKL RPTRTSSESI YSRPGSSIPG SPGHTIYAKV 70 80 90 100 110 120 DNEILDYKDL AAIPKVKAIY DIERPDLITY EPFYTSGYDD KQERQSLGES PRTLSPTPSA 130 140 150 160 170 180 EGYQDVRDRM IHRSTSQGSI NSPVYSRHSY TPTTSRSPQH FHRPDQGINI YRKPPIYKQH 190 200 210 220 230 240 AALAAQSKSS EDIIKFSKFP AAQAPDPSET PKIETDHWPG PPSFAVVGPD MKRRSSGREE 250 260 270 280 290 300 DDEELLRRRQ LQEEQLMKLN SGLGQLILKE EMEKESRERS SLLASRYDSP INSASHIPSS 310 320 330 340 350 360 KTASLPGYGR NGLHRPVSTD FAQYNSYGDV SGGVRDYQTL PDGHMPAMRM DRGVSMPNML 370 380 390 400 410 420 EPKIFPYEML MVTNRGRNKI LREVDRTRLE RHLAPEVFRE IFGMSIQEFD RLPLWRRNDM KKKAKLF
	Isoform 4. Checksum: 0B2AC94C24A5D72F		401	46,087
	10 20 30 40 50 60 MFTEGEEMYL QGSTVWHPDC KQSTKTEEKL RAKVDNEILD YKDLAAIPKV KAIYDIERPD 70 80 90 100 110 120 LITYEPFYTS GYDDKQERQS LGESPRTLSP TPSAEGYQDV RDRMIHRSTS QGSINSPVYS 130 140 150 160 170 180 RHSYTPTTSR SPQHFHRPDQ GINIYRKPPI YKQHAALAAQ SKSSEDIIKF SKFPAAQAPD 190 200 210 220 230 240 PSETPKIETD HWPGPPSFAV VGPDMKRRSS GREEDDEELL RRRQLQEEQL MKLNSGLGQL 250 260 270 280 290 300 ILKEEMEKES RERSSLLASR YDSPINSASH IPSSKTASLP GYGRNGLHRP VSTDFAQYNS 310 320 330 340 350 360 YGDVSGGVRD YQTLPDGHMP AMRMDRGVSM PNMLEPKIFP YEMLMVTNRG RNKILREVDR 370 380 390 400 TRLERHLAPE VFREIFGMSI QEFDRLPLWR RNDMKKKAKL F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein." Roof D.J., Hayes A., Adamian M., Chishti A.H., Li T. J. Cell Biol. 138:575-588(1997) [PubMed: 9245787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY. Tissue: Retina.
[2]	"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed: 7584044] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Bone marrow.
[3]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[4]	The German cDNA consortium Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Retina.
[5]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Kidney.
[7]	"Two novel members of the ABLIM protein family, ABLIM-2 and -3, associate with STARS and directly bind F-actin." Barrientos T., Frank D., Kuwahara K., Bezprozvannaya S., Pipes G.C.T., Bassel-Duby R., Richardson J.A., Katus H.A., Olson E.N., Frey N. J. Biol. Chem. 282:8393-8403(2007) [PubMed: 17194709] [Abstract] Cited for: INTERACTION WITH ABRA.
[8]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-357; TYR-373; SER-435; TYR-439 AND TYR-461, MASS SPECTROMETRY. Tissue: T-cell.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-452; SER-655 AND SER-706, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-396; TYR-406 AND TYR-410, MASS SPECTROMETRY.
[11]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-461, MASS SPECTROMETRY. Tissue: T-cell.
[12]	"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 SER-473, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452 AND SER-458, MASS SPECTROMETRY.
[14]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, MASS SPECTROMETRY. Tissue: Platelet.
[15]	"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-431; SER-435; SER-455; SER-458; SER-587; SER-640; SER-655 AND SER-706, MASS SPECTROMETRY.