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Q9UHB6 (LIMA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
LIM domain and actin-binding protein 1
Alternative name(s):
Epithelial protein lost in neoplasm
Gene names
Name:LIMA1
Synonyms:EPLIN, SREBP3
ORF Names:PP624
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length759 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to actin monomers and filaments. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments. Ref.11

Subcellular location

Cytoplasm. Cell junctionfocal adhesion. Cytoplasmcytoskeleton. Note: This cytoskeletal protein co-localizes with actin stress fibers and focal adhesion plaques. Ref.1 Ref.9

Tissue specificity

Highly expressed in placenta, kidney, pancreas, prostate, ovary, spleen and heart. Also detected in lung, liver, brain, skeletal muscle, thymus, testis and intestine. Not detected in leukocytes. Isoform Beta expressed generally at very low levels. Isoform Alpha abundant in epithelial cells from mammary gland, prostate and in normal oral keratinocytes. Low levels in aortic endothelial cells and dermal fibroblasts. Not detectable in myocardium.

Induction

Down-regulated in some cancer cell lines. Isoform Alpha is induced by serum. Isoform Beta is constitutively expressed. Ref.10

Domain

Contains at least 2 actin-binding domains, one on each side of the LIM domain. Both domains bind actin monomers and filaments. The C-terminal domain binds filaments more efficiently than the N-terminus.

Sequence similarities

Contains 1 LIM zinc-binding domain.

Sequence caution

The sequence AAG17267.1 differs from that shown. Reason: Frameshift at positions 365 and 662.

The sequence BAA91120.1 differs from that shown. Reason: Frameshift at position 697.

The sequence BAD92749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SVILO463853EBI-351479,EBI-6995105From a different organism.

Alternative products

This entry describes 5 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform Beta (identifier: Q9UHB6-1)

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.
Note: Produced by alternative promoter usage.
Isoform Alpha (identifier: Q9UHB6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
Note: Produced by alternative promoter usage.
Isoform 3 (identifier: Q9UHB6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-302: Missing.
Note: Produced by alternative splicing of isoform Beta.
Isoform 4 (identifier: Q9UHB6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     344-344: R → PG
Note: Produced by alternative splicing.
Isoform 5 (identifier: Q9UHB6-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     344-344: R → PG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 759759LIM domain and actin-binding protein 1
PRO_0000075730

Regions

Domain388 – 44861LIM zinc-binding

Amino acid modifications

Modified residue11N-acetylmethionine Ref.19
Modified residue41Phosphoserine Ref.19
Modified residue151Phosphoserine Ref.16
Modified residue1321Phosphoserine Ref.13 Ref.19 Ref.21
Modified residue2251Phosphoserine Ref.16 Ref.19
Modified residue2291Phosphotyrosine Ref.16
Modified residue2301Phosphoserine By similarity
Modified residue2631Phosphoserine Ref.19
Modified residue3431Phosphoserine Ref.19
Modified residue3501Phosphoserine Ref.21
Modified residue3621Phosphoserine Ref.12 Ref.13 Ref.16 Ref.19 Ref.21
Modified residue3651Phosphoserine Ref.21
Modified residue3691Phosphoserine Ref.21
Modified residue3741Phosphoserine Ref.16 Ref.19 Ref.21
Modified residue4391N6-succinyllysine By similarity
Modified residue4901Phosphoserine Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.21
Modified residue6041Phosphoserine Ref.16 Ref.18 Ref.19
Modified residue6091Phosphoserine Ref.16
Modified residue6171Phosphoserine Ref.16 Ref.18
Modified residue6861Phosphoserine Ref.12 Ref.15 Ref.16 Ref.18 Ref.19 Ref.21
Modified residue6921Phosphoserine Ref.12 Ref.15 Ref.16 Ref.19
Modified residue6981Phosphoserine Ref.16 Ref.19 Ref.21
Modified residue7261Phosphoserine Ref.21

Natural variations

Alternative sequence1 – 302302Missing in isoform 3.
VSP_003117
Alternative sequence1 – 160160Missing in isoform Alpha and isoform 5.
VSP_003116
Alternative sequence3441R → PG in isoform 4 and isoform 5.
VSP_040136

Experimental info

Sequence conflict3811Missing in BAA90914. Ref.4
Sequence conflict3811Missing in AAH01247. Ref.7
Sequence conflict4151F → L in AAG17267. Ref.8
Sequence conflict4631D → G in BAA90914. Ref.4
Sequence conflict4911P → Q in AAF67491. Ref.2
Sequence conflict520 – 5212DK → NR in AAF67491. Ref.2

Secondary structure

.................. 759
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 996378AFD3B003D5

FASTA75985,226
        10         20         30         40         50         60 
MESSPFNRRQ WTSLSLRVTA KELSLVNKNK SSAIVEIFSK YQKAAEETNM EKKRSNTENL 

        70         80         90        100        110        120 
SQHFRKGTLT VLKKKWENPG LGAESHTDSL RNSSTEIRHR ADHPPAEVTS HAASGAKADQ 

       130        140        150        160        170        180 
EEQIHPRSRL RSPPEALVQG RYPHIKDGED LKDHSTESKK MENCLGESRH EVEKSEISEN 

       190        200        210        220        230        240 
TDASGKIEKY NVPLNRLKMM FEKGEPTQTK ILRAQSRSAS GRKISENSYS LDDLEIGPGQ 

       250        260        270        280        290        300 
LSSSTFDSEK NESRRNLELP RLSETSIKDR MAKYQAAVSK QSSSTNYTNE LKASGGEIKI 

       310        320        330        340        350        360 
HKMEQKENVP PGPEVCITHQ EGEKISANEN SLAVRSTPAE DDSRDSQVKS EVQQPVHPKP 

       370        380        390        400        410        420 
LSPDSRASSL SESSPPKAMK KFQAPARETC VECQKTVYPM ERLLANQQVF HISCFRCSYC 

       430        440        450        460        470        480 
NNKLSLGTYA SLHGRIYCKP HFNQLFKSKG NYDEGFGHRP HKDLWASKNE NEEILERPAQ 

       490        500        510        520        530        540 
LANARETPHS PGVEDAPIAK VGVLAASMEA KASSQQEKED KPAETKKLRI AWPPPTELGS 

       550        560        570        580        590        600 
SGSALEEGIK MSKPKWPPED EISKPEVPED VDLDLKKLRR SSSLKERSRP FTVAASFQST 

       610        620        630        640        650        660 
SVKSPKTVSP PIRKGWSMSE QSEESVGGRV AERKQVENAK ASKKNGNVGK TTWQNKESKG 

       670        680        690        700        710        720 
ETGKRSKEGH SLEMENENLV ENGADSDEDD NSFLKQQSPQ EPKSLNWSSF VDNTFAEEFT 

       730        740        750 
TQNQKSQDVE LWEGEVVKEL SVEEQIKRNR YYDEDEDEE 

« Hide

Isoform Alpha [UniParc].

Checksum: DE0AE1D7A916BE30
Show »

FASTA59967,119
Isoform 3 [UniParc].

Checksum: DD730BA1D2FB8E2E
Show »

FASTA45751,219
Isoform 4 [UniParc].

Checksum: 5FD64F6E2ECEFAE2
Show »

FASTA76085,224
Isoform 5 [UniParc].

Checksum: DAE126F756B45C5F
Show »

FASTA60067,117

References

« Hide 'large scale' references
[1]"EPLIN, epithelial protein lost in neoplasm."
Maul R.S., Chang D.D.
Oncogene 18:7838-7841(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), SUBCELLULAR LOCATION.
Tissue: Cervix carcinoma.
[2]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
Tissue: Hypothalamus.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
Tissue: Uterus.
[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] (ISOFORMS ALPHA; BETA AND 3).
Tissue: Colon, Hepatoma and Placenta.
[5]"Homo sapiens protein coding cDNA."
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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 BETA).
Tissue: Brain, Cervix, Colon and Placenta.
[8]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 232-759.
[9]"Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing."
Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.
EMBO Rep. 1:287-292(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Characterization of the human EPLIN (Epithelial protein lost in neoplasm) gene reveals distinct promoters for the two EPLIN isoforms."
Chen S., Maul R.S., Kim H.R., Chang D.D.
Gene 248:69-76(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE PROMOTER USAGE, INDUCTION.
[11]"EPLIN regulates actin dynamics by cross-linking and stabilizing filaments."
Maul R.S., Song Y., Amann K.J., Gerbin S.C., Pollard T.D., Chang D.D.
J. Cell Biol. 160:399-407(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-490; SER-686 AND SER-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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 SER-132; SER-362 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[15]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490; SER-686 AND SER-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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-15; SER-225; TYR-229; SER-362; SER-374; SER-490; SER-604; SER-609; SER-617; SER-686; SER-692 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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].
[18]"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-604; SER-617 AND SER-686, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-132; SER-225; SER-263; SER-343; SER-362; SER-374; SER-490; SER-604; SER-686; SER-692 AND SER-698, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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-132; SER-350; SER-362; SER-365; SER-369; SER-374; SER-490; SER-686; SER-698 AND SER-726, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Solution structure of the LIM domain of epithelial protein lost in neoplasm."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 381-460.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF198454 mRNA. Translation: AAF23755.1.
AF198455 mRNA. Translation: AAF23756.1.
AF157325 mRNA. Translation: AAF67491.1.
AL136911 mRNA. Translation: CAB66845.1.
AK000372 mRNA. Translation: BAA91120.1. Frameshift.
AK000335 mRNA. Translation: BAA91092.1.
AK023649 mRNA. Translation: BAB14625.1.
AK000057 mRNA. Translation: BAA90914.1.
AK314447 mRNA. Translation: BAG37056.1.
AB209512 mRNA. Translation: BAD92749.1. Different initiation.
CH471111 Genomic DNA. Translation: EAW58135.1.
BC001247 mRNA. Translation: AAH01247.2.
BC010664 mRNA. Translation: AAH10664.1.
BC110815 mRNA. Translation: AAI10816.1.
BC136763 mRNA. Translation: AAI36764.1.
AF218025 mRNA. Translation: AAG17267.1. Frameshift.
CCDSCCDS44877.1. [Q9UHB6-4]
CCDS58230.1. [Q9UHB6-3]
CCDS8802.1. [Q9UHB6-1]
RefSeqNP_001107018.1. NM_001113546.1. [Q9UHB6-4]
NP_001107019.1. NM_001113547.1. [Q9UHB6-5]
NP_001230704.1. NM_001243775.1. [Q9UHB6-3]
NP_057441.1. NM_016357.4. [Q9UHB6-1]
UniGeneHs.525419.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8YNMR-A381-457[»]
ProteinModelPortalQ9UHB6.
SMRQ9UHB6. Positions 381-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119559. 22 interactions.
DIPDIP-29633N.
IntActQ9UHB6. 12 interactions.
MINTMINT-1132272.

PTM databases

PhosphoSiteQ9UHB6.

Polymorphism databases

DMDM20138067.

Proteomic databases

MaxQBQ9UHB6.
PaxDbQ9UHB6.
PRIDEQ9UHB6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341247; ENSP00000340184; ENSG00000050405. [Q9UHB6-1]
ENST00000394943; ENSP00000378400; ENSG00000050405. [Q9UHB6-4]
ENST00000547825; ENSP00000448706; ENSG00000050405. [Q9UHB6-3]
ENST00000552783; ENSP00000448779; ENSG00000050405.
ENST00000552823; ENSP00000450266; ENSG00000050405. [Q9UHB6-2]
GeneID51474.
KEGGhsa:51474.
UCSCuc001rwg.4. human. [Q9UHB6-1]
uc001rwi.4. human. [Q9UHB6-4]

Organism-specific databases

CTD51474.
GeneCardsGC12M050569.
H-InvDBHIX0171649.
HGNCHGNC:24636. LIMA1.
HPAHPA023871.
HPA052645.
MIM608364. gene.
neXtProtNX_Q9UHB6.
PharmGKBPA143485527.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238020.
HOGENOMHOG000059621.
HOVERGENHBG051492.
OMADEISKPE.
OrthoDBEOG7PCJH8.
PhylomeDBQ9UHB6.
TreeFamTF350273.

Gene expression databases

ArrayExpressQ9UHB6.
BgeeQ9UHB6.
GenevestigatorQ9UHB6.

Family and domain databases

Gene3D2.10.110.10. 1 hit.
InterProIPR028740. EPLIN.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERPTHR24206:SF27. PTHR24206:SF27. 1 hit.
PfamPF00412. LIM. 1 hit.
[Graphical view]
SMARTSM00132. LIM. 1 hit.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLIMA1. human.
EvolutionaryTraceQ9UHB6.
GeneWikiLIMA1.
GenomeRNAi51474.
NextBio55109.
PROQ9UHB6.
SOURCESearch...

Entry information

Entry nameLIMA1_HUMAN
AccessionPrimary (citable) accession number: Q9UHB6
Secondary accession number(s): B2RB09 expand/collapse secondary AC list , Q2TAN7, Q59FE8, Q9BVF2, Q9H8J1, Q9HBN5, Q9NX96, Q9NXC3, Q9NXU6, Q9P0H8, Q9UHB5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 138 of the entry and version 1 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 chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM