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Protein

Four and a half LIM domains protein 3

Gene

FHL3

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

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3125C4-typeSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. zinc ion binding Source: InterPro

GO - Biological processi

  1. actin cytoskeleton organization Source: Ensembl
  2. muscle organ development Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ13643.

Names & Taxonomyi

Protein namesi
Recommended name:
Four and a half LIM domains protein 3
Short name:
FHL-3
Alternative name(s):
Skeletal muscle LIM-protein 2
Short name:
SLIM-2
Gene namesi
Name:FHL3
Synonyms:SLIM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3704. FHL3.

Subcellular locationi

GO - Cellular componenti

  1. focal adhesion Source: UniProtKB
  2. nucleus Source: Ensembl
  3. stress fiber Source: Ensembl
  4. Z disc Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28142.

Polymorphism and mutation databases

BioMutaiFHL3.
DMDMi209572768.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 280279Four and a half LIM domains protein 3PRO_0000075740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei157 – 1571N6-acetyllysineBy similarity
Modified residuei235 – 2351N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ13643.
PaxDbiQ13643.
PRIDEiQ13643.

PTM databases

PhosphoSiteiQ13643.

Expressioni

Tissue specificityi

Expressed only in skeletal muscle.

Gene expression databases

BgeeiQ13643.
CleanExiHS_FHL3.
ExpressionAtlasiQ13643. baseline and differential.
GenevestigatoriQ13643.

Organism-specific databases

HPAiHPA045723.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
A1CFQ9NQ943EBI-741101,EBI-2809489
ADAM15Q134443EBI-741101,EBI-77818
AIMP2Q131555EBI-741101,EBI-745226
AMBPP027603EBI-741101,EBI-2115136
C14orf105Q17R993EBI-741101,EBI-10238351
C16orf35Q9BTE23EBI-741101,EBI-10298364
C9orf116Q5BN463EBI-741101,EBI-10243636
C9orf138A8K8803EBI-741101,EBI-10174528
CNNM3Q8NE014EBI-741101,EBI-741032
CNNM3Q8NE01-33EBI-741101,EBI-10269984
CSF1P096033EBI-741101,EBI-2872294
DCDC2BA2VCK23EBI-741101,EBI-10173222
E2F8A0AVK63EBI-741101,EBI-7779316
EFCAB12Q6NXP03EBI-741101,EBI-10251535
EPHA10Q5JZY3-33EBI-741101,EBI-10244652
EPM2AIP1Q7L7753EBI-741101,EBI-6255981
FAM71CQ8NEG03EBI-741101,EBI-752049
FAM90A1Q86YD73EBI-741101,EBI-6658203
FBXL18Q96D163EBI-741101,EBI-744419
FOSL2P154083EBI-741101,EBI-3893419
GATA2P237693EBI-741101,EBI-2806671
GCM2O756033EBI-741101,EBI-10188645
HIPK1Q86Z023EBI-741101,EBI-692891
HYAL2Q128913EBI-741101,EBI-2806068
KIRREL2Q6UWL63EBI-741101,EBI-10254473
KLF3P576824EBI-741101,EBI-8472267
KRTAP12-1P599903EBI-741101,EBI-10210845
KRTAP12-2P599913EBI-741101,EBI-10176379
KTI12Q96EK93EBI-741101,EBI-7951092
LMO2P257913EBI-741101,EBI-739696
MRPL27Q9P0M93EBI-741101,EBI-5325236
MYBPHLA2RUH73EBI-741101,EBI-9088235
P4HA2O15460-23EBI-741101,EBI-10182841
PATL1Q86TB93EBI-741101,EBI-2562092
PHF21AQ96BD53EBI-741101,EBI-745085
PTPN6P293503EBI-741101,EBI-78260
QRICH1Q2TAL83EBI-741101,EBI-2798044
RAD21O602163EBI-741101,EBI-80739
RFX3P483803EBI-741101,EBI-742557
RHEBL1Q8TAI73EBI-741101,EBI-746555
RNMTL1Q9HC363EBI-741101,EBI-1045440
SAP30BPQ9UHR53EBI-741101,EBI-751683
SLAIN1Q8ND833EBI-741101,EBI-10269374
SLC25A46Q96AG33EBI-741101,EBI-10281975
SLC44A3Q8N4M13EBI-741101,EBI-10265585
SNRPGP623083EBI-741101,EBI-624585
TMX3Q96JJ73EBI-741101,EBI-2514069
TROG5E9N23EBI-741101,EBI-10178070
TTLL10Q6ZVT03EBI-741101,EBI-7844656
TYK2P295973EBI-741101,EBI-1383454
TYMSOSQ8TAI13EBI-741101,EBI-742060
UBE2Q1Q7Z7E8-23EBI-741101,EBI-10258181
ZNF417Q8TAU33EBI-741101,EBI-740727
ZNF512BQ96KM63EBI-741101,EBI-1049952

Protein-protein interaction databases

BioGridi108566. 110 interactions.
DIPiDIP-42030N.
IntActiQ13643. 67 interactions.
MINTiMINT-155453.
STRINGi9606.ENSP00000362107.

Structurei

Secondary structure

1
280
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni41 – 433Combined sources
Turni63 – 653Combined sources
Turni69 – 713Combined sources
Beta strandi80 – 834Combined sources
Beta strandi86 – 894Combined sources
Turni90 – 923Combined sources
Helixi97 – 993Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi110 – 1123Combined sources
Turni124 – 1263Combined sources
Turni130 – 1323Combined sources
Turni136 – 1383Combined sources
Beta strandi141 – 1444Combined sources
Beta strandi147 – 1504Combined sources
Helixi151 – 1577Combined sources
Turni163 – 1653Combined sources
Beta strandi174 – 1818Combined sources
Turni183 – 1853Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi204 – 2096Combined sources
Helixi210 – 2167Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYHNMR-A101-159[»]
2CUQNMR-A152-218[»]
2EHENMR-A30-99[»]
ProteinModelPortaliQ13643.
SMRiQ13643. Positions 1-277.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13643.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 9253LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini101 – 15353LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 21251LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST
Domaini221 – 27555LIM zinc-binding 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 LIM zinc-binding domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3125C4-typeSequence AnalysisAdd
BLAST

Keywords - Domaini

LIM domain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG314122.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000231075.
HOVERGENiHBG074526.
InParanoidiQ13643.
OMAiYEDRHYH.
OrthoDBiEOG7P8P7M.
PhylomeDBiQ13643.
TreeFamiTF314113.

Family and domain databases

Gene3Di2.10.110.10. 5 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 4 hits.
[Graphical view]
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q13643-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESFDCAKC NESLYGRKYI QTDSGPYCVP CYDNTFANTC AECQQLIGHD
60 70 80 90 100
SRELFYEDRH FHEGCFRCCR CQRSLADEPF TCQDSELLCN DCYCSAFSSQ
110 120 130 140 150
CSACGETVMP GSRKLEYGGQ TWHEHCFLCS GCEQPLGSRS FVPDKGAHYC
160 170 180 190 200
VPCYENKFAP RCARCSKTLT QGGVTYRDQP WHRECLVCTG CQTPLAGQQF
210 220 230 240 250
TSRDEDPYCV ACFGELFAPK CSSCKRPIVG LGGGKYVSFE DRHWHHNCFS
260 270 280
CARCSTSLVG QGFVPDGDQV LCQGCSQAGP
Length:280
Mass (Da):31,192
Last modified:October 14, 2008 - v4
Checksum:iD1A037C260370DFD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821C → R in AAC04466 (PubMed:10049693).Curated
Sequence conflicti130 – 1301S → I in AAC04466 (PubMed:10049693).Curated
Sequence conflicti140 – 1401S → P in AAC04466 (PubMed:10049693).Curated
Sequence conflicti157 – 1571K → N in AAC04466 (PubMed:10049693).Curated
Sequence conflicti166 – 1661S → T in AAC04466 (PubMed:10049693).Curated
Sequence conflicti174 – 1741V → L in AAC04466 (PubMed:10049693).Curated
Sequence conflicti179 – 1791Q → L in AAC04466 (PubMed:10049693).Curated
Sequence conflicti183 – 1842RE → PK in AAC04466 (PubMed:10049693).Curated
Sequence conflicti250 – 2523SCA → TCD in AAC04466 (PubMed:10049693).Curated
Sequence conflicti252 – 2521A → D in CAG33706 (Ref. 4) Curated
Sequence conflicti256 – 2561T → N in AAC04466 (PubMed:10049693).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60116 mRNA. Translation: AAC04466.2.
AK290641 mRNA. Translation: BAF83330.1.
BT007052 mRNA. Translation: AAP35701.1.
CR457425 mRNA. Translation: CAG33706.1.
AL603790 Genomic DNA. Translation: CAH69931.1.
CH471059 Genomic DNA. Translation: EAX07301.1.
CH471059 Genomic DNA. Translation: EAX07302.1.
BC001351 mRNA. Translation: AAH01351.1.
BC011697 mRNA. Translation: AAH11697.1.
CCDSiCCDS30678.1.
PIRiT09504.
RefSeqiNP_001230807.1. NM_001243878.1.
NP_004459.2. NM_004468.4.
UniGeneiHs.57687.

Genome annotation databases

EnsembliENST00000373016; ENSP00000362107; ENSG00000183386.
GeneIDi2275.
KEGGihsa:2275.
UCSCiuc001cck.3. human.

Polymorphism and mutation databases

BioMutaiFHL3.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60116 mRNA. Translation: AAC04466.2.
AK290641 mRNA. Translation: BAF83330.1.
BT007052 mRNA. Translation: AAP35701.1.
CR457425 mRNA. Translation: CAG33706.1.
AL603790 Genomic DNA. Translation: CAH69931.1.
CH471059 Genomic DNA. Translation: EAX07301.1.
CH471059 Genomic DNA. Translation: EAX07302.1.
BC001351 mRNA. Translation: AAH01351.1.
BC011697 mRNA. Translation: AAH11697.1.
CCDSiCCDS30678.1.
PIRiT09504.
RefSeqiNP_001230807.1. NM_001243878.1.
NP_004459.2. NM_004468.4.
UniGeneiHs.57687.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYHNMR-A101-159[»]
2CUQNMR-A152-218[»]
2EHENMR-A30-99[»]
ProteinModelPortaliQ13643.
SMRiQ13643. Positions 1-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108566. 110 interactions.
DIPiDIP-42030N.
IntActiQ13643. 67 interactions.
MINTiMINT-155453.
STRINGi9606.ENSP00000362107.

PTM databases

PhosphoSiteiQ13643.

Polymorphism and mutation databases

BioMutaiFHL3.
DMDMi209572768.

Proteomic databases

MaxQBiQ13643.
PaxDbiQ13643.
PRIDEiQ13643.

Protocols and materials databases

DNASUi2275.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373016; ENSP00000362107; ENSG00000183386.
GeneIDi2275.
KEGGihsa:2275.
UCSCiuc001cck.3. human.

Organism-specific databases

CTDi2275.
GeneCardsiGC01M038462.
HGNCiHGNC:3704. FHL3.
HPAiHPA045723.
MIMi602790. gene.
neXtProtiNX_Q13643.
PharmGKBiPA28142.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG314122.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000231075.
HOVERGENiHBG074526.
InParanoidiQ13643.
OMAiYEDRHYH.
OrthoDBiEOG7P8P7M.
PhylomeDBiQ13643.
TreeFamiTF314113.

Enzyme and pathway databases

SignaLinkiQ13643.

Miscellaneous databases

ChiTaRSiFHL3. human.
EvolutionaryTraceiQ13643.
GeneWikiiFHL3.
GenomeRNAii2275.
NextBioi9257.
PROiQ13643.
SOURCEiSearch...

Gene expression databases

BgeeiQ13643.
CleanExiHS_FHL3.
ExpressionAtlasiQ13643. baseline and differential.
GenevestigatoriQ13643.

Family and domain databases

Gene3Di2.10.110.10. 5 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 4 hits.
[Graphical view]
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The LIM proteins FHL1 and FHL3 are expressed differently in skeletal muscle."
    Morgan M.J., Madgwick A.J.A.
    Biochem. Biophys. Res. Commun. 255:245-250(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "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].
    Tissue: Embryo.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.
  8. "Slim defines a novel family of LIM-proteins expressed in skeletal muscle."
    Morgan M.J., Madgwick A.J.A.
    Biochem. Biophys. Res. Commun. 225:632-638(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 16-280.
    Tissue: Skeletal muscle.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "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(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Solution structure of LIM domains from human skeletal muscle LIM-protein 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 98-218 IN COMPLEX WITH ZINC IONS.

Entry informationi

Entry nameiFHL3_HUMAN
AccessioniPrimary (citable) accession number: Q13643
Secondary accession number(s): D3DPT6, Q6I9T0, Q9BVA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 14, 2008
Last modified: April 29, 2015
This is version 132 of the entry and version 4 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 1
    Human chromosome 1: 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.