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O14639 (ABLM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin-binding LIM protein 1

Short name=abLIM-1
Alternative name(s):
Actin-binding LIM protein family member 1
Actin-binding double zinc finger protein
LIMAB1
Limatin
Gene names
Name:ABLIM1
Synonyms:ABLIM, KIAA0059, LIMAB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length778 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.1

Subunit structure

Binds F-actin. Interacts with ABRA. Ref.10

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton By 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

Sequence similarities

Contains 1 HP (headpiece) domain.

Contains 4 LIM zinc-binding domains.

Sequence caution

The sequence BAA06681.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LDOC1O957512EBI-487024,EBI-740738

Alternative products

This entry describes 5 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.
Isoform 5 (identifier: O14639-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-316: Missing.
     347-347: R → RLPNIRRSSSDFFYSKSLIRRTGRSPSLQ
     480-514: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 778778Actin-binding LIM protein 1
PRO_0000075697

Regions

Domain97 – 15660LIM zinc-binding 1
Domain156 – 21661LIM zinc-binding 2
Domain224 – 28360LIM zinc-binding 3
Domain283 – 34361LIM zinc-binding 4
Domain710 – 77869HP
Coiled coil590 – 61425 Potential

Amino acid modifications

Modified residue3671Phosphoserine Ref.15
Modified residue3731Phosphotyrosine Ref.15
Modified residue3961Phosphotyrosine Ref.9
Modified residue4261Phosphoserine Ref.15
Modified residue4311Phosphoserine Ref.13 Ref.15
Modified residue4331Phosphothreonine Ref.15
Modified residue4351Phosphoserine Ref.13 Ref.15 Ref.16 Ref.17
Modified residue4391Phosphotyrosine Ref.8
Modified residue4551Phosphoserine Ref.13
Modified residue4581Phosphoserine Ref.13
Modified residue5871Phosphoserine Ref.13
Modified residue6401Phosphoserine Ref.13 Ref.16
Modified residue6551Phosphoserine Ref.13

Natural variations

Alternative sequence1 – 316316Missing in isoform 3, isoform 4 and isoform 5.
VSP_012099
Alternative sequence1 – 8181MPAFL…SVDPF → MLMTLEMTELTDPHHTMGDY K in isoform 2.
VSP_012100
Alternative sequence3471R → RLPNIRRSSSDFFYSKSLIR RTGRSPSLQ in isoform 5.
VSP_041185
Alternative sequence348 – 37326Missing in isoform 4.
VSP_012101
Alternative sequence480 – 51435Missing in isoform 3, isoform 4 and isoform 5.
VSP_012102
Natural variant4341P → T.
Corresponds to variant rs11593544 [ dbSNP | Ensembl ].
VAR_050141
Natural variant6371R → G.
Corresponds to variant rs7091419 [ dbSNP | Ensembl ].
VAR_050142

Experimental info

Sequence conflict4991R → L in AAC51676. Ref.1
Sequence conflict5321A → R in AAC51676. Ref.1
Sequence conflict5631K → E in BAA06681. Ref.2
Sequence conflict5781V → I in BAA06681. Ref.2

Sequences

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

Last modified September 23, 2008. Version 3.
Checksum: EBC2F14BE558752B

FASTA77887,688
        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 

« Hide

Isoform 2 [UniParc].

Checksum: A9CAEEBA95BDF15E
Show »

FASTA71881,121
Isoform 3 [UniParc].

Checksum: 1721FB3EC1D99994
Show »

FASTA42748,804
Isoform 4 [UniParc].

Checksum: 0B2AC94C24A5D72F
Show »

FASTA40146,087
Isoform 5 [UniParc].

Checksum: CA7E610D14878674
Show »

FASTA45552,056

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[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. 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 5).
Tissue: Uterus.
[5]"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] (ISOFORM 3).
Tissue: Retina.
[6]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Kidney.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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: INTERACTION WITH ABRA.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[12]"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.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-435; SER-455; SER-458; SER-587; SER-640 AND SER-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; TYR-373; SER-426; SER-431; THR-433 AND SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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-435 AND SER-640, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF005654 mRNA. Translation: AAC51676.1.
D31883 mRNA. Translation: BAA06681.2. Different initiation.
AK098277 mRNA. Translation: BAG53605.1.
CR749819 mRNA. Translation: CAH18679.1.
AL133384 Genomic DNA. Translation: CAI40135.1.
AL133384 Genomic DNA. Translation: CAI40136.1.
AL133384, AL354873 Genomic DNA. Translation: CAI40140.1.
AL133384, AL354873 Genomic DNA. Translation: CAI40141.1.
AL354873, AL133384 Genomic DNA. Translation: CAI10908.1.
AL354873, AL133384 Genomic DNA. Translation: CAI10910.1.
AL590109 Genomic DNA. No translation available.
BC002448 mRNA. Translation: AAH02448.1.
CCDSCCDS31288.1. [O14639-2]
CCDS31289.1. [O14639-5]
CCDS7590.1. [O14639-1]
RefSeqNP_001003407.1. NM_001003407.1. [O14639-2]
NP_001003408.1. NM_001003408.1.
NP_002304.3. NM_002313.5. [O14639-1]
NP_006711.3. NM_006720.3. [O14639-5]
XP_005269885.1. XM_005269828.2. [O14639-3]
UniGeneHs.438236.
Hs.538331.
Hs.593868.

3D structure databases

ProteinModelPortalO14639.
SMRO14639. Positions 89-344, 714-778.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110171. 21 interactions.
IntActO14639. 17 interactions.
MINTMINT-1447354.
STRING9606.ENSP00000338190.

PTM databases

PhosphoSiteO14639.

Proteomic databases

MaxQBO14639.
PaxDbO14639.
PRIDEO14639.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000277895; ENSP00000277895; ENSG00000099204. [O14639-1]
ENST00000369252; ENSP00000358256; ENSG00000099204. [O14639-2]
ENST00000369253; ENSP00000358257; ENSG00000099204. [O14639-4]
ENST00000392952; ENSP00000376679; ENSG00000099204. [O14639-5]
GeneID3983.
KEGGhsa:3983.
UCSCuc021pyu.1. human. [O14639-5]
uc021pyw.1. human. [O14639-1]
uc021pyz.1. human. [O14639-2]
uc021pzc.1. human. [O14639-4]

Organism-specific databases

CTD3983.
GeneCardsGC10M116190.
HGNCHGNC:78. ABLIM1.
HPAHPA038951.
HPA038952.
MIM602330. gene.
neXtProtNX_O14639.
PharmGKBPA35023.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG302299.
HOVERGENHBG031499.
KOK07520.
OMAHHPSEKP.
PhylomeDBO14639.
TreeFamTF318042.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressO14639.
BgeeO14639.
CleanExHS_ABLIM1.
GenevestigatorO14639.

Family and domain databases

Gene3D1.10.950.10. 1 hit.
2.10.110.10. 4 hits.
InterProIPR028448. ABLIM1.
IPR003128. Villin_headpiece.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERPTHR24213:SF18. PTHR24213:SF18. 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

ChiTaRSABLIM1. human.
GeneWikiABLIM1.
GenomeRNAi3983.
NextBio15616.
PROO14639.
SOURCESearch...

Entry information

Entry nameABLM1_HUMAN
AccessionPrimary (citable) accession number: O14639
Secondary accession number(s): A6NI16 expand/collapse secondary AC list , A6NJ06, A8MXA9, Q15039, Q5JVV1, Q5JVV2, Q5T6N3, Q5T6N5, Q68CQ9, Q9BUP1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 136 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

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 10

Human chromosome 10: entries, gene names and cross-references to MIM