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Protein

LIM domain and actin-binding protein 1

Gene

LIMA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. actin filament binding Source: UniProtKB
  2. actin monomer binding Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. actin filament bundle assembly Source: UniProtKB
  2. negative regulation of actin filament depolymerization Source: UniProtKB
  3. ruffle organization Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
LIM domain and actin-binding protein 1
Alternative name(s):
Epithelial protein lost in neoplasm
Gene namesi
Name:LIMA1
Synonyms:EPLIN, SREBP3
ORF Names:PP624
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:24636. LIMA1.

Subcellular locationi

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

GO - Cellular componenti

  1. actin cytoskeleton Source: LIFEdb
  2. cleavage furrow Source: UniProtKB
  3. cytoplasm Source: HPA
  4. focal adhesion Source: UniProtKB
  5. plasma membrane Source: HPA
  6. stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485527.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 759759LIM domain and actin-binding protein 1PRO_0000075730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei4 – 41Phosphoserine1 Publication
Modified residuei15 – 151Phosphoserine1 Publication
Modified residuei132 – 1321Phosphoserine3 Publications
Modified residuei225 – 2251Phosphoserine3 Publications
Modified residuei229 – 2291Phosphotyrosine1 Publication
Modified residuei230 – 2301PhosphoserineBy similarity
Modified residuei263 – 2631Phosphoserine1 Publication
Modified residuei343 – 3431Phosphoserine1 Publication
Modified residuei350 – 3501Phosphoserine1 Publication
Modified residuei362 – 3621Phosphoserine6 Publications
Modified residuei365 – 3651Phosphoserine2 Publications
Modified residuei369 – 3691Phosphoserine1 Publication
Modified residuei374 – 3741Phosphoserine4 Publications
Modified residuei439 – 4391N6-succinyllysineBy similarity
Modified residuei490 – 4901Phosphoserine8 Publications
Modified residuei604 – 6041Phosphoserine3 Publications
Modified residuei609 – 6091Phosphoserine1 Publication
Modified residuei617 – 6171Phosphoserine2 Publications
Modified residuei686 – 6861Phosphoserine6 Publications
Modified residuei692 – 6921Phosphoserine4 Publications
Modified residuei698 – 6981Phosphoserine2 Publications
Modified residuei726 – 7261Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UHB6.
PaxDbiQ9UHB6.
PRIDEiQ9UHB6.

PTM databases

PhosphoSiteiQ9UHB6.

Expressioni

Tissue specificityi

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.

Inductioni

Down-regulated in some cancer cell lines. Isoform Alpha is induced by serum. Isoform Beta is constitutively expressed.1 Publication

Gene expression databases

BgeeiQ9UHB6.
ExpressionAtlasiQ9UHB6. baseline and differential.
GenevestigatoriQ9UHB6.

Organism-specific databases

HPAiHPA023871.
HPA052645.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SVILO463853EBI-351479,EBI-6995105From a different organism.

Protein-protein interaction databases

BioGridi119559. 32 interactions.
DIPiDIP-29633N.
IntActiQ9UHB6. 12 interactions.
MINTiMINT-1132272.

Structurei

Secondary structure

1
759
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi384 – 3874Combined sources
Turni391 – 3933Combined sources
Beta strandi401 – 4044Combined sources
Beta strandi406 – 4116Combined sources
Turni412 – 4143Combined sources
Turni418 – 4203Combined sources
Turni426 – 4283Combined sources
Beta strandi432 – 4343Combined sources
Helixi439 – 4457Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8YNMR-A381-457[»]
ProteinModelPortaliQ9UHB6.
SMRiQ9UHB6. Positions 381-460.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UHB6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini388 – 44861LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST

Domaini

Sequence similaritiesi

Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain

Phylogenomic databases

eggNOGiNOG238020.
GeneTreeiENSGT00510000046839.
HOGENOMiHOG000059621.
HOVERGENiHBG051492.
InParanoidiQ9UHB6.
OMAiQNQKSQD.
OrthoDBiEOG7PCJH8.
PhylomeDBiQ9UHB6.
TreeFamiTF350273.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
InterProiIPR028740. EPLIN.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24206:SF27. PTHR24206:SF27. 1 hit.
PfamiPF00412. LIM. 1 hit.
[Graphical view]
SMARTiSM00132. LIM. 1 hit.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform Beta (identifier: Q9UHB6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MESSPFNRRQ WTSLSLRVTA KELSLVNKNK SSAIVEIFSK YQKAAEETNM
60 70 80 90 100
EKKRSNTENL SQHFRKGTLT VLKKKWENPG LGAESHTDSL RNSSTEIRHR
110 120 130 140 150
ADHPPAEVTS HAASGAKADQ EEQIHPRSRL RSPPEALVQG RYPHIKDGED
160 170 180 190 200
LKDHSTESKK MENCLGESRH EVEKSEISEN TDASGKIEKY NVPLNRLKMM
210 220 230 240 250
FEKGEPTQTK ILRAQSRSAS GRKISENSYS LDDLEIGPGQ LSSSTFDSEK
260 270 280 290 300
NESRRNLELP RLSETSIKDR MAKYQAAVSK QSSSTNYTNE LKASGGEIKI
310 320 330 340 350
HKMEQKENVP PGPEVCITHQ EGEKISANEN SLAVRSTPAE DDSRDSQVKS
360 370 380 390 400
EVQQPVHPKP LSPDSRASSL SESSPPKAMK KFQAPARETC VECQKTVYPM
410 420 430 440 450
ERLLANQQVF HISCFRCSYC NNKLSLGTYA SLHGRIYCKP HFNQLFKSKG
460 470 480 490 500
NYDEGFGHRP HKDLWASKNE NEEILERPAQ LANARETPHS PGVEDAPIAK
510 520 530 540 550
VGVLAASMEA KASSQQEKED KPAETKKLRI AWPPPTELGS SGSALEEGIK
560 570 580 590 600
MSKPKWPPED EISKPEVPED VDLDLKKLRR SSSLKERSRP FTVAASFQST
610 620 630 640 650
SVKSPKTVSP PIRKGWSMSE QSEESVGGRV AERKQVENAK ASKKNGNVGK
660 670 680 690 700
TTWQNKESKG ETGKRSKEGH SLEMENENLV ENGADSDEDD NSFLKQQSPQ
710 720 730 740 750
EPKSLNWSSF VDNTFAEEFT TQNQKSQDVE LWEGEVVKEL SVEEQIKRNR

YYDEDEDEE

Note: Produced by alternative promoter usage.

Length:759
Mass (Da):85,226
Last modified:April 30, 2000 - v1
Checksum:i996378AFD3B003D5
GO
Isoform Alpha (identifier: Q9UHB6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.

Note: Produced by alternative promoter usage. Contains a N-acetylmethionine at position 1.1 Publication

Show »
Length:599
Mass (Da):67,119
Checksum:iDE0AE1D7A916BE30
GO
Isoform 3 (identifier: Q9UHB6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-302: Missing.

Note: Produced by alternative splicing of isoform Beta.

Show »
Length:457
Mass (Da):51,219
Checksum:iDD730BA1D2FB8E2E
GO
Isoform 4 (identifier: Q9UHB6-4) [UniParc]FASTAAdd to basket

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 343.1 Publication

Show »
Length:760
Mass (Da):85,224
Checksum:i5FD64F6E2ECEFAE2
GO
Isoform 5 (identifier: Q9UHB6-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     344-344: R → PG

Note: No experimental confirmation available. Contains a phosphoserine at position 183. Contains a N-acetylmethionine at position 1.2 Publications

Show »
Length:600
Mass (Da):67,117
Checksum:iDAE126F756B45C5F
GO

Sequence cautioni

The sequence AAG17267.1 differs from that shown. Reason: Frameshift at positions 365 and 662. Curated
The sequence BAA91120.1 differs from that shown. Reason: Frameshift at position 697. Curated
The sequence BAD92749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti381 – 3811Missing in BAA90914 (PubMed:14702039).Curated
Sequence conflicti381 – 3811Missing in AAH01247 (PubMed:15489334).Curated
Sequence conflicti415 – 4151F → L in AAG17267 (PubMed:15498874).Curated
Sequence conflicti463 – 4631D → G in BAA90914 (PubMed:14702039).Curated
Sequence conflicti491 – 4911P → Q in AAF67491 (PubMed:10931946).Curated
Sequence conflicti520 – 5212DK → NR in AAF67491 (PubMed:10931946).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 302302Missing in isoform 3. 2 PublicationsVSP_003117Add
BLAST
Alternative sequencei1 – 160160Missing in isoform Alpha and isoform 5. 2 PublicationsVSP_003116Add
BLAST
Alternative sequencei344 – 3441R → PG in isoform 4 and isoform 5. 2 PublicationsVSP_040136

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44877.1. [Q9UHB6-4]
CCDS55826.1. [Q9UHB6-5]
CCDS58230.1. [Q9UHB6-3]
CCDS8802.1. [Q9UHB6-1]
RefSeqiNP_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]
UniGeneiHs.525419.

Genome annotation databases

EnsembliENST00000341247; ENSP00000340184; ENSG00000050405. [Q9UHB6-1]
ENST00000394943; ENSP00000378400; ENSG00000050405. [Q9UHB6-4]
ENST00000547825; ENSP00000448706; ENSG00000050405. [Q9UHB6-3]
ENST00000552783; ENSP00000448779; ENSG00000050405. [Q9UHB6-5]
ENST00000552823; ENSP00000450266; ENSG00000050405. [Q9UHB6-2]
GeneIDi51474.
KEGGihsa:51474.
UCSCiuc001rwg.4. human. [Q9UHB6-1]
uc001rwi.4. human. [Q9UHB6-4]

Polymorphism databases

DMDMi20138067.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44877.1. [Q9UHB6-4]
CCDS55826.1. [Q9UHB6-5]
CCDS58230.1. [Q9UHB6-3]
CCDS8802.1. [Q9UHB6-1]
RefSeqiNP_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]
UniGeneiHs.525419.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8YNMR-A381-457[»]
ProteinModelPortaliQ9UHB6.
SMRiQ9UHB6. Positions 381-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119559. 32 interactions.
DIPiDIP-29633N.
IntActiQ9UHB6. 12 interactions.
MINTiMINT-1132272.

PTM databases

PhosphoSiteiQ9UHB6.

Polymorphism databases

DMDMi20138067.

Proteomic databases

MaxQBiQ9UHB6.
PaxDbiQ9UHB6.
PRIDEiQ9UHB6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341247; ENSP00000340184; ENSG00000050405. [Q9UHB6-1]
ENST00000394943; ENSP00000378400; ENSG00000050405. [Q9UHB6-4]
ENST00000547825; ENSP00000448706; ENSG00000050405. [Q9UHB6-3]
ENST00000552783; ENSP00000448779; ENSG00000050405. [Q9UHB6-5]
ENST00000552823; ENSP00000450266; ENSG00000050405. [Q9UHB6-2]
GeneIDi51474.
KEGGihsa:51474.
UCSCiuc001rwg.4. human. [Q9UHB6-1]
uc001rwi.4. human. [Q9UHB6-4]

Organism-specific databases

CTDi51474.
GeneCardsiGC12M050569.
H-InvDBHIX0171649.
HGNCiHGNC:24636. LIMA1.
HPAiHPA023871.
HPA052645.
MIMi608364. gene.
neXtProtiNX_Q9UHB6.
PharmGKBiPA143485527.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG238020.
GeneTreeiENSGT00510000046839.
HOGENOMiHOG000059621.
HOVERGENiHBG051492.
InParanoidiQ9UHB6.
OMAiQNQKSQD.
OrthoDBiEOG7PCJH8.
PhylomeDBiQ9UHB6.
TreeFamiTF350273.

Miscellaneous databases

ChiTaRSiLIMA1. human.
EvolutionaryTraceiQ9UHB6.
GeneWikiiLIMA1.
GenomeRNAii51474.
NextBioi55109.
PROiQ9UHB6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UHB6.
ExpressionAtlasiQ9UHB6. baseline and differential.
GenevestigatoriQ9UHB6.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
InterProiIPR028740. EPLIN.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24206:SF27. PTHR24206:SF27. 1 hit.
PfamiPF00412. LIM. 1 hit.
[Graphical view]
SMARTiSM00132. LIM. 1 hit.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "EPLIN, epithelial protein lost in neoplasm."
    Maul R.S., Chang D.D.
    Oncogene 18:7838-7841(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), SUBCELLULAR LOCATION.
    Tissue: Cervix carcinoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
    Tissue: Hypothalamus.
  3. 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(2003) [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 (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Brain.
  6. 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(2003) [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.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2003) [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(1999) [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(1999) [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(2002) [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(2005) [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(2006) [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. 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(2007) [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. 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(2008) [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(2008) [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(2009) [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 AND SER-692, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. 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(2010) [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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 5 AND ALPHA), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-362; SER-365; SER-374 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "Solution structure of the LIM domain of epithelial protein lost in neoplasm."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAY-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 381-460.

Entry informationi

Entry nameiLIMA1_HUMAN
AccessioniPrimary (citable) accession number: Q9UHB6
Secondary accession number(s): B2RB09
, Q2TAN7, Q59FE8, Q9BVF2, Q9H8J1, Q9HBN5, Q9NX96, Q9NXC3, Q9NXU6, Q9P0H8, Q9UHB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 4, 2002
Last sequence update: April 30, 2000
Last modified: March 3, 2015
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.