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O94929 (ABLM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin-binding LIM protein 3

Short name=abLIM-3
Alternative name(s):
Actin-binding LIM protein family member 3
Gene names
Name:ABLIM3
Synonyms:KIAA0843
ORF Names:HMFN1661
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length683 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. Ref.1

Subunit structure

Directly interacts with F-actin and ABRA. Ref.1

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed predominantly in heart and brain. Ref.1

Sequence similarities

Contains 1 HP (headpiece) domain.

Contains 4 LIM zinc-binding domains.

Sequence caution

The sequence BAA74866.2 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O94929-1)

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: O94929-2)

The sequence of this isoform differs from the canonical sequence as follows:
     297-358: Missing.
     402-450: Missing.
     647-683: RHLSQEEFYQVFGMTISEFDRLALWKRNELKKQARLF → GNFWKSGCL
Note: No experimental confirmation available.
Isoform 3 (identifier: O94929-3)

The sequence of this isoform differs from the canonical sequence as follows:
     297-358: Missing.
     402-434: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: O94929-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-514: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 683683Actin-binding LIM protein 3
PRO_0000075702

Regions

Domain21 – 8060LIM zinc-binding 1
Domain80 – 14061LIM zinc-binding 2
Domain149 – 20860LIM zinc-binding 3
Domain208 – 26861LIM zinc-binding 4
Domain615 – 68369HP

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10
Modified residue2771Phosphoserine By similarity
Modified residue2801Phosphoserine By similarity
Modified residue5031Phosphoserine Ref.7 Ref.9
Modified residue5041Phosphoserine Ref.7 Ref.9
Modified residue5431Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 514514Missing in isoform 4.
VSP_012126
Alternative sequence297 – 35862Missing in isoform 2 and isoform 3.
VSP_012127
Alternative sequence402 – 45049Missing in isoform 2.
VSP_012128
Alternative sequence402 – 43433Missing in isoform 3.
VSP_012129
Alternative sequence647 – 68337RHLSQ…QARLF → GNFWKSGCL in isoform 2.
VSP_012130
Natural variant1251G → D.
Corresponds to variant rs35907283 [ dbSNP | Ensembl ].
VAR_050143

Experimental info

Sequence conflict2271K → R in BAF82425. Ref.3

Secondary structure

................................ 683
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 7, 2004. Version 3.
Checksum: 0392DBD9065EE08A

FASTA68377,802
        10         20         30         40         50         60 
MNTSIPYQQN PYNPRGSSNV IQCYRCGDTC KGEVVRVHNN HFHIRCFTCQ VCGCGLAQSG 

        70         80         90        100        110        120 
FFFKNQEYIC TQDYQQLYGT RCDSCRDFIT GEVISALGRT YHPKCFVCSL CRKPFPIGDK 

       130        140        150        160        170        180 
VTFSGKECVC QTCSQSMASS KPIKIRGPSH CAGCKEEIKH GQSLLALDKQ WHVSCFKCQT 

       190        200        210        220        230        240 
CSVILTGEYI SKDGVPYCES DYHAQFGIKC ETCDRYISGR VLEAGGKHYH PTCARCVRCH 

       250        260        270        280        290        300 
QMFTEGEEMY LTGSEVWHPI CKQAARAEKK LKHRRTSETS ISPPGSSIGS PNRVICAKVD 

       310        320        330        340        350        360 
NEILNYKDLA ALPKVKSIYE VQRPDLISYE PHSRYMSDEM LERCGYGESL GTLSPYSQDI 

       370        380        390        400        410        420 
YENLDLRQRR ASSPGYIDSP TYSRQGMSPT FSRSPHHYYR SGPESGRSSP YHSQLDVRSS 

       430        440        450        460        470        480 
TPTSYQAPKH FHIPAGDSNI YRKPPIYKRH GDLSTATKSK TSEDISQTSK YSPIYSPDPY 

       490        500        510        520        530        540 
YASESEYWTY HGSPKVPRAR RFSSGGEEDD FDRSMHKLQS GIGRLILKEE MKARSSSYAD 

       550        560        570        580        590        600 
PWTPPRSSTS SREALHTAGY EMSLNGSPRS HYLADSDPLI SKSASLPAYR RNGLHRTPSA 

       610        620        630        640        650        660 
DLFHYDSMNA VNWGMREYKI YPYELLLVTT RGRNRLPKDV DRTRLERHLS QEEFYQVFGM 

       670        680 
TISEFDRLAL WKRNELKKQA RLF 

« Hide

Isoform 2 [UniParc].

Checksum: E6A19F001BF02176
Show »

FASTA54461,570
Isoform 3 [UniParc].

Checksum: 858F0D8EA50B1A57
Show »

FASTA58867,073
Isoform 4 [UniParc].

Checksum: 18F1F045422E1552
Show »

FASTA16919,695

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH F-ACTIN AND ABRA.
Tissue: Heart.
[2]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"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. expand/collapse author list , 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 1).
[4]"Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."
Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.
Oncogene 23:5901-5911(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Hepatoblastoma.
[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 2).
Tissue: Colon.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-683 (ISOFORM 3).
Tissue: Stomach.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[9]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Solution structure of the villin headpiece domain of human actin-binding LIM protein homologue (KIAA0843 protein)."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 610-683.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ413174 mRNA. Translation: ABD83327.1.
AB020650 mRNA. Translation: BAA74866.2. Different initiation.
AK289736 mRNA. Translation: BAF82425.1.
AB075881 mRNA. Translation: BAD38663.1.
BC001665 mRNA. Translation: AAH01665.1.
AL833021 mRNA. Translation: CAH56270.1.
RefSeqNP_055760.1. NM_014945.2.
XP_005268449.1. XM_005268392.1.
XP_005268452.1. XM_005268395.1.
UniGeneHs.49688.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJSNMR-A609-683[»]
2DJ7NMR-A141-207[»]
ProteinModelPortalO94929.
SMRO94929. Positions 22-268, 607-683.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116552. 3 interactions.
IntActO94929. 4 interactions.
MINTMINT-4657493.
STRING9606.ENSP00000310309.

PTM databases

PhosphoSiteO94929.

Proteomic databases

PaxDbO94929.
PRIDEO94929.

Protocols and materials databases

DNASU22885.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309868; ENSP00000310309; ENSG00000173210. [O94929-1]
ENST00000326685; ENSP00000315841; ENSG00000173210. [O94929-3]
ENST00000356541; ENSP00000348938; ENSG00000173210. [O94929-2]
ENST00000504238; ENSP00000421183; ENSG00000173210. [O94929-2]
ENST00000506113; ENSP00000425394; ENSG00000173210. [O94929-1]
ENST00000508983; ENSP00000420855; ENSG00000173210.
ENST00000517451; ENSP00000430150; ENSG00000173210. [O94929-4]
GeneID22885.
KEGGhsa:22885.
UCSCuc003lpy.2. human. [O94929-1]
uc003lqa.1. human. [O94929-2]
uc003lqd.1. human. [O94929-3]

Organism-specific databases

CTD22885.
GeneCardsGC05P148501.
HGNCHGNC:29132. ABLIM3.
HPAHPA003245.
MIM611305. gene.
neXtProtNX_O94929.
PharmGKBPA134962761.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG302299.
HOGENOMHOG000285997.
HOVERGENHBG031499.
InParanoidO94929.
KOK07520.
OMADPYYASE.
OrthoDBEOG71CFKF.
PhylomeDBO94929.
TreeFamTF318042.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressO94929.
BgeeO94929.
CleanExHS_ABLIM3.
GenevestigatorO94929.

Family and domain databases

Gene3D1.10.950.10. 1 hit.
2.10.110.10. 4 hits.
InterProIPR028449. ABLIM3.
IPR003128. Villin_headpiece.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERPTHR24213:SF1. PTHR24213:SF1. 1 hit.
PfamPF00412. LIM. 4 hits.
PF02209. VHP. 1 hit.
[Graphical view]
SMARTSM00132. LIM. 4 hits.
SM00153. VHP. 1 hit.
[Graphical view]
SUPFAMSSF47050. SSF47050. 1 hit.
PROSITEPS51089. HP. 1 hit.
PS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO94929.
GeneWikiABLIM3.
GenomeRNAi22885.
NextBio43475.
PROO94929.
SOURCESearch...

Entry information

Entry nameABLM3_HUMAN
AccessionPrimary (citable) accession number: O94929
Secondary accession number(s): A8K121 expand/collapse secondary AC list , Q19VH3, Q658S1, Q68CI5, Q9BV32
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 7, 2004
Last modified: April 16, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM