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Q14847

- LASP1_HUMAN

UniProt

Q14847 - LASP1_HUMAN

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Protein

LIM and SH3 domain protein 1

Gene

LASP1

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

Functioni

Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types (By similarity).By similarity

GO - Molecular functioni

  1. ion transmembrane transporter activity Source: UniProtKB
  2. SH3/SH2 adaptor activity Source: ProtInc
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. ion transport Source: UniProtKB
  2. positive regulation of signal transduction Source: GOC
Complete GO annotation...

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Actin-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
LIM and SH3 domain protein 1
Short name:
LASP-1
Alternative name(s):
Metastatic lymph node gene 50 protein
Short name:
MLN 50
Gene namesi
Name:LASP1
Synonyms:MLN50
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:6513. LASP1.

Subcellular locationi

Cytoplasmcell cortex By similarity. Cytoplasmcytoskeleton By similarity
Note: Associated with the F-actin rich cortical cytoskeleton.By similarity

GO - Cellular componenti

  1. cortical actin cytoskeleton Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. focal adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30298.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261LIM and SH3 domain protein 1PRO_0000075761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei42 – 421N6-acetyllysine1 Publication
Modified residuei68 – 681Phosphothreonine3 Publications
Modified residuei104 – 1041Phosphothreonine4 Publications
Modified residuei112 – 1121N6-succinyllysineBy similarity
Modified residuei118 – 1181Phosphoserine1 Publication
Modified residuei146 – 1461Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14847.
PaxDbiQ14847.
PRIDEiQ14847.

2D gel databases

OGPiQ14847.
SWISS-2DPAGEQ14847.

PTM databases

PhosphoSiteiQ14847.

Expressioni

Gene expression databases

BgeeiQ14847.
CleanExiHS_LASP1.
ExpressionAtlasiQ14847. baseline and differential.
GenevestigatoriQ14847.

Organism-specific databases

HPAiCAB022049.
HPA012072.

Interactioni

Subunit structurei

Interacts with F-actin (By similarity). Interacts with ANKRD54 (By similarity). Interacts with KBTBD10.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
LPPQ930523EBI-742828,EBI-718388
MDFIQ997503EBI-742828,EBI-724076
TJP2Q9UDY29EBI-742828,EBI-1042602
TRIP13Q156454EBI-742828,EBI-358993
ZDHHC17Q8IUH53EBI-9088686,EBI-524753
ZYXQ159425EBI-742828,EBI-444225

Protein-protein interaction databases

BioGridi110120. 29 interactions.
IntActiQ14847. 15 interactions.
MINTiMINT-5001286.
STRINGi9606.ENSP00000325240.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi207 – 2115
Beta strandi228 – 2369
Beta strandi239 – 2446
Turni245 – 2484
Beta strandi249 – 2546
Helixi255 – 2573
Beta strandi258 – 2603

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3I35X-ray1.40A202-261[»]
ProteinModelPortaliQ14847.
SMRiQ14847. Positions 1-54, 205-261.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14847.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 5652LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati61 – 9535Nebulin 1Add
BLAST
Repeati97 – 13135Nebulin 2Add
BLAST
Domaini202 – 26160SH3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi201 – 2044Poly-Gly

Sequence similaritiesi

Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation
Contains 2 nebulin repeats.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG259964.
GeneTreeiENSGT00530000062924.
HOGENOMiHOG000006616.
HOVERGENiHBG054636.
InParanoidiQ14847.
OMAiYWHKACF.
OrthoDBiEOG771280.
PhylomeDBiQ14847.
TreeFamiTF319104.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
InterProiIPR000900. Nebulin_repeat.
IPR001452. SH3_domain.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 1 hit.
PF00880. Nebulin. 2 hits.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00132. LIM. 1 hit.
SM00227. NEBU. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
PS51216. NEBULIN. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14847-1) [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
MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK
60 70 80 90 100
PYCNAHYPKQ SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV
110 120 130 140 150
VADTPELQRI KKTQDQISNI KYHEEFEKSR MGPSGGEGME PERRDSQDGS
160 170 180 190 200
SYRRPLEQQQ PHHIPTSAPV YQQPQQQPVA QSYGGYKEPA APVSIQRSAP
210 220 230 240 250
GGGGKRYRAV YDYSAADEDE VSFQDGDTIV NVQQIDDGWM YGTVERTGDT
260
GMLPANYVEA I
Length:261
Mass (Da):29,717
Last modified:January 1, 1998 - v2
Checksum:i3B89B988605B3639
GO
Isoform 2 (identifier: Q14847-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     201-261: GGGGKRYRAV...MLPANYVEAI → ICLQHIPRHR...LTYPHIPGLG

Note: No experimental confirmation available.

Show »
Length:323
Mass (Da):36,014
Checksum:iB6A28D1D97AB2C69
GO
Isoform 3 (identifier: Q14847-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: MNPNCARCGK...LKQQSELQSQ → MLPLRDLQDDTEHEELQGLREEALLQR

Note: No experimental confirmation available.

Show »
Length:205
Mass (Da):23,181
Checksum:i4CD6D2622F74CCF4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791E → R in AAH12460. (PubMed:15489334)Curated
Sequence conflicti210 – 2101V → A in AAH12460. (PubMed:15489334)Curated
Sequence conflicti220 – 2201E → A in AAH12460. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8383MNPNC…ELQSQ → MLPLRDLQDDTEHEELQGLR EEALLQR in isoform 3. 1 PublicationVSP_054611Add
BLAST
Alternative sequencei201 – 26161GGGGK…YVEAI → ICLQHIPRHRIRPGRDPSIL QCLCFLKPATACDSYPSSSF FCQLKPSSATSAGSLLWQAS PLIDFLVFSLDGTGMGLSGG GRGPWGRAGMGDLLACGPHL PLCSLPSHPPAQLLTYPHIP GLG in isoform 2. 1 PublicationVSP_016554Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X82456 mRNA. Translation: CAA57833.1.
AK294704 mRNA. Translation: BAG57861.1.
AC006441 Genomic DNA. No translation available.
AC110749 Genomic DNA. No translation available.
BC007560 mRNA. Translation: AAH07560.1.
BC012460 mRNA. Translation: AAH12460.1.
CCDSiCCDS11331.1. [Q14847-1]
CCDS62164.1. [Q14847-3]
PIRiS68234.
RefSeqiNP_001258537.1. NM_001271608.1. [Q14847-3]
NP_006139.1. NM_006148.3. [Q14847-1]
UniGeneiHs.741156.

Genome annotation databases

EnsembliENST00000318008; ENSP00000325240; ENSG00000002834. [Q14847-1]
ENST00000433206; ENSP00000401048; ENSG00000002834. [Q14847-3]
ENST00000435347; ENSP00000392853; ENSG00000002834. [Q14847-1]
GeneIDi3927.
KEGGihsa:3927.
UCSCiuc002hra.3. human. [Q14847-1]
uc010wdz.2. human.

Polymorphism databases

DMDMi3122342.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X82456 mRNA. Translation: CAA57833.1 .
AK294704 mRNA. Translation: BAG57861.1 .
AC006441 Genomic DNA. No translation available.
AC110749 Genomic DNA. No translation available.
BC007560 mRNA. Translation: AAH07560.1 .
BC012460 mRNA. Translation: AAH12460.1 .
CCDSi CCDS11331.1. [Q14847-1 ]
CCDS62164.1. [Q14847-3 ]
PIRi S68234.
RefSeqi NP_001258537.1. NM_001271608.1. [Q14847-3 ]
NP_006139.1. NM_006148.3. [Q14847-1 ]
UniGenei Hs.741156.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3I35 X-ray 1.40 A 202-261 [» ]
ProteinModelPortali Q14847.
SMRi Q14847. Positions 1-54, 205-261.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110120. 29 interactions.
IntActi Q14847. 15 interactions.
MINTi MINT-5001286.
STRINGi 9606.ENSP00000325240.

PTM databases

PhosphoSitei Q14847.

Polymorphism databases

DMDMi 3122342.

2D gel databases

OGPi Q14847.
SWISS-2DPAGE Q14847.

Proteomic databases

MaxQBi Q14847.
PaxDbi Q14847.
PRIDEi Q14847.

Protocols and materials databases

DNASUi 3927.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000318008 ; ENSP00000325240 ; ENSG00000002834 . [Q14847-1 ]
ENST00000433206 ; ENSP00000401048 ; ENSG00000002834 . [Q14847-3 ]
ENST00000435347 ; ENSP00000392853 ; ENSG00000002834 . [Q14847-1 ]
GeneIDi 3927.
KEGGi hsa:3927.
UCSCi uc002hra.3. human. [Q14847-1 ]
uc010wdz.2. human.

Organism-specific databases

CTDi 3927.
GeneCardsi GC17P037026.
HGNCi HGNC:6513. LASP1.
HPAi CAB022049.
HPA012072.
MIMi 602920. gene.
neXtProti NX_Q14847.
PharmGKBi PA30298.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG259964.
GeneTreei ENSGT00530000062924.
HOGENOMi HOG000006616.
HOVERGENi HBG054636.
InParanoidi Q14847.
OMAi YWHKACF.
OrthoDBi EOG771280.
PhylomeDBi Q14847.
TreeFami TF319104.

Miscellaneous databases

ChiTaRSi LASP1. human.
EvolutionaryTracei Q14847.
GeneWikii LASP1.
GenomeRNAii 3927.
NextBioi 15423.
PROi Q14847.
SOURCEi Search...

Gene expression databases

Bgeei Q14847.
CleanExi HS_LASP1.
ExpressionAtlasi Q14847. baseline and differential.
Genevestigatori Q14847.

Family and domain databases

Gene3Di 2.10.110.10. 1 hit.
InterProi IPR000900. Nebulin_repeat.
IPR001452. SH3_domain.
IPR001781. Znf_LIM.
[Graphical view ]
Pfami PF00412. LIM. 1 hit.
PF00880. Nebulin. 2 hits.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00132. LIM. 1 hit.
SM00227. NEBU. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
PS51216. NEBULIN. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17."
    Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G., Chenard M.-P., Lidereau R., Basset P., Rio M.-C.
    Genomics 28:367-376(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary carcinoma.
  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] (ISOFORM 3).
    Tissue: Brain.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Liver and Skin.
  5. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-7, ACETYLATION AT MET-1.
    Tissue: Platelet.
  6. "Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the association of LIM and SH3 domains."
    Tomasetto C., Moog-Lutz C., Regnier C.H., Schreiber V., Basset P., Rio M.-C.
    FEBS Lett. 373:245-249(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.
  7. "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 THR-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; THR-104 AND SER-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Novel beta-propeller of the BTB-Kelch protein Krp1 provides a binding site for Lasp-1 that is necessary for pseudopodial extension."
    Gray C.H., McGarry L.C., Spence H.J., Riboldi-Tunnicliffe A., Ozanne B.W.
    J. Biol. Chem. 284:30498-30507(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KBTBD10.
  11. "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 THR-68 AND THR-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; THR-104; SER-118 AND SER-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLASP1_HUMAN
AccessioniPrimary (citable) accession number: Q14847
Secondary accession number(s): B4DGQ0, Q96ED2, Q96IG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 145 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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