Q9UHB6 (LIMA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	759 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10
Subcellular location	Cytoplasm. Cell junction › focal adhesion. Cytoplasm › cytoskeleton. Note: This cytoskeletal protein co-localizes with actin stress fibers and focal adhesion plaques. Ref.1 Ref.8
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.9
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.

Ontologies

Keywords
Cellular component	Cell junction Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative promoter usage Alternative splicing
Domain	LIM domain
Ligand	Actin-binding Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament bundle assembly Inferred from direct assay Ref.10. Source: UniProtKB negative regulation of actin filament depolymerization Inferred from direct assay Ref.10. Source: UniProtKB ruffle organization Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA focal adhesion Inferred from direct assay Ref.1. Source: UniProtKB plasma membrane Inferred from direct assay. Source: HPA stress fiber Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	actin filament binding Inferred from direct assay Ref.10. Source: UniProtKB actin monomer binding Inferred from direct assay Ref.10. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 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. Contains a phosphoserine at position 343.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 759

759

LIM domain and actin-binding protein 1

PRO_0000075730

Regions

Domain

388 – 448

61

LIM zinc-binding

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.17

Modified residue

4

1

Phosphoserine Ref.17

Modified residue

15

1

Phosphoserine Ref.15

Modified residue

132

1

Phosphoserine Ref.12 Ref.17 Ref.19

Modified residue

225

1

Phosphoserine Ref.15 Ref.17

Modified residue

229

1

Phosphotyrosine Ref.15

Modified residue

230

1

Phosphoserine By similarity

Modified residue

263

1

Phosphoserine Ref.17

Modified residue

343

1

Phosphoserine Ref.17

Modified residue

350

1

Phosphoserine Ref.19

Modified residue

362

1

Phosphoserine Ref.11 Ref.12 Ref.15 Ref.17 Ref.19

Modified residue

365

1

Phosphoserine Ref.19

Modified residue

369

1

Phosphoserine Ref.19

Modified residue

374

1

Phosphoserine Ref.15 Ref.17 Ref.19

Modified residue

490

1

Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19

Modified residue

541

1

Phosphoserine By similarity

Modified residue

604

1

Phosphoserine Ref.15 Ref.16 Ref.17

Modified residue

609

1

Phosphoserine Ref.15

Modified residue

617

1

Phosphoserine Ref.15 Ref.16

Modified residue

686

1

Phosphoserine Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19

Modified residue

692

1

Phosphoserine Ref.11 Ref.14 Ref.15 Ref.17

Modified residue

698

1

Phosphoserine Ref.15 Ref.17 Ref.19

Modified residue

726

1

Phosphoserine Ref.19

Modified residue

741

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 302

302

Missing in isoform 3.

VSP_003117

Alternative sequence

1 – 160

160

Missing in isoform Alpha.

VSP_003116

Alternative sequence

344

1

R → PG in isoform 4.

VSP_040136

Experimental info

Sequence conflict

381

1

Missing in BAA90914. Ref.4

Sequence conflict

381

1

Missing in AAH01247. Ref.6

Sequence conflict

415

1

F → L in AAG17267. Ref.7

Sequence conflict

463

1

D → G in BAA90914. Ref.4

Sequence conflict

491

1

P → Q in AAF67491. Ref.2

Sequence conflict

520 – 521

2

DK → NR in AAF67491. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

759

Helix Strand Turn

Details...

Beta strand

384 – 387

4

Turn

391 – 393

3

Beta strand

401 – 404

4

Beta strand

406 – 411

6

Turn

412 – 414

3

Turn

418 – 420

3

Turn

426 – 428

3

Beta strand

432 – 434

3

Helix

439 – 445

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 996378AFD3B003D5	FASTA	759	85,226
	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
	Isoform Alpha [UniParc]. Checksum: DE0AE1D7A916BE30	FASTA	599	67,119
	10 20 30 40 50 60 MENCLGESRH EVEKSEISEN TDASGKIEKY NVPLNRLKMM FEKGEPTQTK ILRAQSRSAS 70 80 90 100 110 120 GRKISENSYS LDDLEIGPGQ LSSSTFDSEK NESRRNLELP RLSETSIKDR MAKYQAAVSK 130 140 150 160 170 180 QSSSTNYTNE LKASGGEIKI HKMEQKENVP PGPEVCITHQ EGEKISANEN SLAVRSTPAE 190 200 210 220 230 240 DDSRDSQVKS EVQQPVHPKP LSPDSRASSL SESSPPKAMK KFQAPARETC VECQKTVYPM 250 260 270 280 290 300 ERLLANQQVF HISCFRCSYC NNKLSLGTYA SLHGRIYCKP HFNQLFKSKG NYDEGFGHRP 310 320 330 340 350 360 HKDLWASKNE NEEILERPAQ LANARETPHS PGVEDAPIAK VGVLAASMEA KASSQQEKED 370 380 390 400 410 420 KPAETKKLRI AWPPPTELGS SGSALEEGIK MSKPKWPPED EISKPEVPED VDLDLKKLRR 430 440 450 460 470 480 SSSLKERSRP FTVAASFQST SVKSPKTVSP PIRKGWSMSE QSEESVGGRV AERKQVENAK 490 500 510 520 530 540 ASKKNGNVGK TTWQNKESKG ETGKRSKEGH SLEMENENLV ENGADSDEDD NSFLKQQSPQ 550 560 570 580 590 EPKSLNWSSF VDNTFAEEFT TQNQKSQDVE LWEGEVVKEL SVEEQIKRNR YYDEDEDEE
	Isoform 3 [UniParc]. Checksum: DD730BA1D2FB8E2E	FASTA	457	51,219
	10 20 30 40 50 60 MEQKENVPPG PEVCITHQEG EKISANENSL AVRSTPAEDD SRDSQVKSEV QQPVHPKPLS 70 80 90 100 110 120 PDSRASSLSE SSPPKAMKKF QAPARETCVE CQKTVYPMER LLANQQVFHI SCFRCSYCNN 130 140 150 160 170 180 KLSLGTYASL HGRIYCKPHF NQLFKSKGNY DEGFGHRPHK DLWASKNENE EILERPAQLA 190 200 210 220 230 240 NARETPHSPG VEDAPIAKVG VLAASMEAKA SSQQEKEDKP AETKKLRIAW PPPTELGSSG 250 260 270 280 290 300 SALEEGIKMS KPKWPPEDEI SKPEVPEDVD LDLKKLRRSS SLKERSRPFT VAASFQSTSV 310 320 330 340 350 360 KSPKTVSPPI RKGWSMSEQS EESVGGRVAE RKQVENAKAS KKNGNVGKTT WQNKESKGET 370 380 390 400 410 420 GKRSKEGHSL EMENENLVEN GADSDEDDNS FLKQQSPQEP KSLNWSSFVD NTFAEEFTTQ 430 440 450 NQKSQDVELW EGEVVKELSV EEQIKRNRYY DEDEDEE
	Isoform 4 [UniParc]. Checksum: 5FD64F6E2ECEFAE2	FASTA	760	85,224
	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 DDSPGDSQVK SEVQQPVHPK 370 380 390 400 410 420 PLSPDSRASS LSESSPPKAM KKFQAPARET CVECQKTVYP MERLLANQQV FHISCFRCSY 430 440 450 460 470 480 CNNKLSLGTY ASLHGRIYCK PHFNQLFKSK GNYDEGFGHR PHKDLWASKN ENEEILERPA 490 500 510 520 530 540 QLANARETPH SPGVEDAPIA KVGVLAASME AKASSQQEKE DKPAETKKLR IAWPPPTELG 550 560 570 580 590 600 SSGSALEEGI KMSKPKWPPE DEISKPEVPE DVDLDLKKLR RSSSLKERSR PFTVAASFQS 610 620 630 640 650 660 TSVKSPKTVS PPIRKGWSMS EQSEESVGGR VAERKQVENA KASKKNGNVG KTTWQNKESK 670 680 690 700 710 720 GETGKRSKEG HSLEMENENL VENGADSDED DNSFLKQQSP QEPKSLNWSS FVDNTFAEEF 730 740 750 760 TTQNQKSQDV ELWEGEVVKE LSVEEQIKRN RYYDEDEDEE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	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. , 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].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA). Tissue: Brain, Cervix, Colon and Placenta.
[7]	"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. , 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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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, MASS SPECTROMETRY. Tissue: Platelet.
[14]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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].
[19]	"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, MASS SPECTROMETRY.
[20]	"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.
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.

IPI

IPI00008918.
IPI00220466.
IPI00883896.
IPI01023024.

RefSeq

NP_001107018.1. NM_001113546.1.
NP_001107019.1. NM_001113547.1.
NP_001230704.1. NM_001243775.1.
NP_057441.1. NM_016357.4.

UniGene

Hs.525419.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D8Y	NMR	-	A	381-457	[»]

ProteinModelPortal

Q9UHB6.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29633N.

IntAct

Q9UHB6. 7 interactions.

MINT

MINT-1132272.

PTM databases

PhosphoSite

Q9UHB6.

Polymorphism databases

DMDM

20138067.

Proteomic databases

PaxDb

Q9UHB6.

PRIDE

Q9UHB6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000341247; ENSP00000340184; ENSG00000050405.
ENST00000394943; ENSP00000378400; ENSG00000050405.
ENST00000547825; ENSP00000448706; ENSG00000050405.
ENST00000552783; ENSP00000448779; ENSG00000050405.
ENST00000552823; ENSP00000450266; ENSG00000050405.

GeneID

51474.

KEGG

hsa:51474.

UCSC

uc001rwg.4. human.
uc001rwi.4. human.

Organism-specific databases

CTD

51474.

GeneCards

GC12M050569.

H-InvDB

HIX0171649.

HGNC

HGNC:24636. LIMA1.

HPA

HPA023871.

MIM

608364. gene.

neXtProt

NX_Q9UHB6.

PharmGKB

PA143485527.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG238020.

HOVERGEN

HBG051492.

OMA

WPPEDEI.

PhylomeDB

Q9UHB6.

Gene expression databases

ArrayExpress

Q9UHB6.

Bgee

Q9UHB6.

Genevestigator

Q9UHB6.

GermOnline

ENSG00000050405. Homo sapiens.

Family and domain databases

Gene3D

2.10.110.10. 1 hit.

InterPro

IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00412. LIM. 1 hit.
[Graphical view]

SMART

SM00132. LIM. 1 hit.
[Graphical view]

PROSITE

PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

LIMA1. human.

EvolutionaryTrace

Q9UHB6.

GenomeRNAi

51474.

NextBio

55109.

SOURCE

Search...

Entry information

Entry name

LIMA1_HUMAN

Accession

Primary (citable) accession number: Q9UHB6
Secondary accession number(s): B2RB09 , Q2TAN7, 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:	May 1, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.