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P13797

- PLST_HUMAN

UniProt

P13797 - PLST_HUMAN

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Protein
Plastin-3
Gene
PLS3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. May play a role in the regulation of bone development.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi25 – 36121 By similarity
Add
BLAST
Calcium bindingi65 – 76122 By similarity
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. bone development Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Plastin-3
Alternative name(s):
T-plastin
Gene namesi
Name:PLS3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:9091. PLS3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti253 – 2531A → AN in OSTEOP; associated with disease susceptibility. 1 Publication
VAR_070278

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi166710. phenotype.
300910. phenotype.
Orphaneti391330. X-linked osteoporosis with fractures.
PharmGKBiPA33418.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 630630Plastin-3
PRO_0000073747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki168 – 168Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei293 – 2931Phosphoserine1 Publication
Modified residuei326 – 3261Phosphoserine2 Publications
Modified residuei391 – 3911Phosphothreonine2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP13797.
PaxDbiP13797.
PRIDEiP13797.

PTM databases

PhosphoSiteiP13797.

Expressioni

Tissue specificityi

Expressed in a variety of organs, including muscle, brain, uterus and esophagus.

Gene expression databases

ArrayExpressiP13797.
BgeeiP13797.
CleanExiHS_PLS3.
GenevestigatoriP13797.

Organism-specific databases

HPAiHPA020433.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi111372. 25 interactions.
IntActiP13797. 10 interactions.
MINTiMINT-3008106.
STRINGi9606.ENSP00000348163.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi123 – 13614
Turni137 – 1393
Turni144 – 1463
Turni151 – 1544
Helixi155 – 1595
Helixi160 – 1623
Helixi164 – 17310
Helixi180 – 1823
Helixi190 – 20617
Helixi216 – 2205
Helixi224 – 24421
Helixi261 – 2655
Helixi269 – 28315
Turni294 – 2985
Helixi300 – 30910
Beta strandi315 – 3173
Turni326 – 3294
Helixi333 – 34412
Turni345 – 3484
Helixi355 – 3595
Helixi363 – 37412
Helixi522 – 53514
Helixi549 – 5513
Helixi553 – 56210
Turni569 – 5713
Helixi579 – 59517
Helixi604 – 6096
Turni612 – 6165
Helixi617 – 6259

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOAX-ray2.40A101-375[»]
1WJONMR-A520-630[»]
ProteinModelPortaliP13797.
SMRiP13797. Positions 15-83, 121-375, 399-630.

Miscellaneous databases

EvolutionaryTraceiP13797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 4736EF-hand 1
Add
BLAST
Domaini52 – 8736EF-hand 2
Add
BLAST
Domaini109 – 382274Actin-binding 1
Add
BLAST
Domaini123 – 239117CH 1
Add
BLAST
Domaini267 – 378112CH 2
Add
BLAST
Domaini383 – 627245Actin-binding 2
Add
BLAST
Domaini397 – 506110CH 3
Add
BLAST
Domaini518 – 627110CH 4
Add
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
HOGENOMiHOG000213447.
HOVERGENiHBG003082.
InParanoidiP13797.
KOiK17336.
OMAiEPQIDIN.
PhylomeDBiP13797.
TreeFamiTF300680.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 4 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF00307. CH. 4 hits.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 4 hits.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 2 hits.
PS00020. ACTININ_2. 2 hits.
PS50021. CH. 4 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13797-1 [UniParc]FASTAAdd to Basket

« Hide

MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG    50
YKVREIIQKL MLDGDRNKDG KISFDEFVYI FQEVKSSDIA KTFRKAINRK 100
EGICALGGTS ELSSEGTQHS YSEEEKYAFV NWINKALEND PDCRHVIPMN 150
PNTDDLFKAV GDGIVLCKMI NLSVPDTIDE RAINKKKLTP FIIQENLNLA 200
LNSASAIGCH VVNIGAEDLR AGKPHLVLGL LWQIIKIGLF ADIELSRNEA 250
LAALLRDGET LEELMKLSPE ELLLRWANFH LENSGWQKIN NFSADIKDSK 300
AYFHLLNQIA PKGQKEGEPR IDINMSGFNE TDDLKRAESM LQQADKLGCR 350
QFVTPADVVS GNPKLNLAFV ANLFNKYPAL TKPENQDIDW TLLEGETREE 400
RTFRNWMNSL GVNPHVNHLY ADLQDALVIL QLYERIKVPV DWSKVNKPPY 450
PKLGANMKKL ENCNYAVELG KHPAKFSLVG IGGQDLNDGN QTLTLALVWQ 500
LMRRYTLNVL EDLGDGQKAN DDIIVNWVNR TLSEAGKSTS IQSFKDKTIS 550
SSLAVVDLID AIQPGCINYD LVKSGNLTED DKHNNAKYAV SMARRIGARV 600
YALPEDLVEV KPKMVMTVFA CLMGRGMKRV 630
Length:630
Mass (Da):70,811
Last modified:April 14, 2009 - v4
Checksum:i631E6F803DC56A56
GO

Sequence cautioni

The sequence CAI39884.1 differs from that shown. Reason: Erroneous initiation.

Polymorphismi

Genetic variations in PLS3 define the bone mineral density quantitative trait locus 18 (BMND18) [MIMi:300910]. Variance in bone mineral density influences bone mass, contributes to size determination in the general population, and is a susceptibility factor for osteoporotic fractures.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti253 – 2531A → AN in OSTEOP; associated with disease susceptibility. 1 Publication
VAR_070278
Natural varianti488 – 4881D → A in a breast cancer sample; somatic mutation. 1 Publication
VAR_035462

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22299 mRNA. Translation: AAB02844.1.
M34427 mRNA. Translation: AAA36759.1.
AK291194 mRNA. Translation: BAF83883.1.
AK312391 mRNA. Translation: BAG35308.1.
AL589842, AC005000 Genomic DNA. Translation: CAI39884.1. Different initiation.
CH471120 Genomic DNA. Translation: EAX02614.1.
BC039049 mRNA. Translation: AAH39049.1.
BC056898 mRNA. Translation: AAH56898.1.
L05491 Genomic DNA. Translation: AAA61214.1.
CCDSiCCDS14568.1.
PIRiA34789.
RefSeqiNP_001129497.1. NM_001136025.4.
NP_001165806.1. NM_001172335.2.
NP_001269266.1. NM_001282337.1.
NP_001269267.1. NM_001282338.1.
NP_005023.2. NM_005032.6.
UniGeneiHs.496622.

Genome annotation databases

EnsembliENST00000355899; ENSP00000348163; ENSG00000102024.
ENST00000420625; ENSP00000398945; ENSG00000102024.
ENST00000595829; ENSP00000472532; ENSG00000268767.
ENST00000602045; ENSP00000473121; ENSG00000268767.
GeneIDi5358.
KEGGihsa:5358.
UCSCiuc004eqd.3. human.

Polymorphism databases

DMDMi226694201.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22299 mRNA. Translation: AAB02844.1 .
M34427 mRNA. Translation: AAA36759.1 .
AK291194 mRNA. Translation: BAF83883.1 .
AK312391 mRNA. Translation: BAG35308.1 .
AL589842 , AC005000 Genomic DNA. Translation: CAI39884.1 . Different initiation.
CH471120 Genomic DNA. Translation: EAX02614.1 .
BC039049 mRNA. Translation: AAH39049.1 .
BC056898 mRNA. Translation: AAH56898.1 .
L05491 Genomic DNA. Translation: AAA61214.1 .
CCDSi CCDS14568.1.
PIRi A34789.
RefSeqi NP_001129497.1. NM_001136025.4.
NP_001165806.1. NM_001172335.2.
NP_001269266.1. NM_001282337.1.
NP_001269267.1. NM_001282338.1.
NP_005023.2. NM_005032.6.
UniGenei Hs.496622.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AOA X-ray 2.40 A 101-375 [» ]
1WJO NMR - A 520-630 [» ]
ProteinModelPortali P13797.
SMRi P13797. Positions 15-83, 121-375, 399-630.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111372. 25 interactions.
IntActi P13797. 10 interactions.
MINTi MINT-3008106.
STRINGi 9606.ENSP00000348163.

PTM databases

PhosphoSitei P13797.

Polymorphism databases

DMDMi 226694201.

Proteomic databases

MaxQBi P13797.
PaxDbi P13797.
PRIDEi P13797.

Protocols and materials databases

DNASUi 5358.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355899 ; ENSP00000348163 ; ENSG00000102024 .
ENST00000420625 ; ENSP00000398945 ; ENSG00000102024 .
ENST00000595829 ; ENSP00000472532 ; ENSG00000268767 .
ENST00000602045 ; ENSP00000473121 ; ENSG00000268767 .
GeneIDi 5358.
KEGGi hsa:5358.
UCSCi uc004eqd.3. human.

Organism-specific databases

CTDi 5358.
GeneCardsi GC0XP114795.
HGNCi HGNC:9091. PLS3.
HPAi HPA020433.
MIMi 166710. phenotype.
300131. gene.
300910. phenotype.
neXtProti NX_P13797.
Orphaneti 391330. X-linked osteoporosis with fractures.
PharmGKBi PA33418.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
HOGENOMi HOG000213447.
HOVERGENi HBG003082.
InParanoidi P13797.
KOi K17336.
OMAi EPQIDIN.
PhylomeDBi P13797.
TreeFami TF300680.

Miscellaneous databases

ChiTaRSi PLS3. human.
EvolutionaryTracei P13797.
GeneWikii PLS3.
GenomeRNAii 5358.
NextBioi 20770.
PROi P13797.
SOURCEi Search...

Gene expression databases

ArrayExpressi P13797.
Bgeei P13797.
CleanExi HS_PLS3.
Genevestigatori P13797.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.10.418.10. 4 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
Pfami PF00307. CH. 4 hits.
PF13499. EF-hand_7. 1 hit.
[Graphical view ]
SMARTi SM00033. CH. 4 hits.
SM00054. EFh. 2 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
PROSITEi PS00019. ACTININ_1. 2 hits.
PS00020. ACTININ_2. 2 hits.
PS50021. CH. 4 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts."
    Lin C.-S., Aebersold R.H., Kent S.B., Varma M., Leavitt J.
    Mol. Cell. Biol. 8:4659-4668(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Correction of the N-terminal sequences of the human plastin isoforms by using anchored polymerase chain reaction: identification of a potential calcium-binding domain."
    Lin C.-S., Aebersold R.H., Leavitt J.
    Mol. Cell. Biol. 10:1818-1821(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "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: Amygdala.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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].
    Tissue: Placenta and Skin.
  7. "Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells."
    Lin C.-S., Park T., Chen Z.P., Leavitt J.
    J. Biol. Chem. 268:2781-2792(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 588-630.
  8. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-168.
    Tissue: Mammary cancer.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND THR-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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 SER-293; SER-326 AND THR-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: POSSIBLE FUNCTION AS REGULATOR OF BONE DEVELOPMENT, POLYMORPHISM, VARIANT OSTEOP ASN-253 INS.
  14. "The structure of an actin-crosslinking domain from human fimbrin."
    Goldsmith S.C., Pokala N., Shen W., Fedorov A.A., Matsudaira P., Almo S.C.
    Nat. Struct. Biol. 4:708-712(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 101-375.
  15. "Solution structure of the fourth CH domain from human plastin 3 T-isoform."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 520-630.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-488.

Entry informationi

Entry nameiPLST_HUMAN
AccessioniPrimary (citable) accession number: P13797
Secondary accession number(s): A8K579, B1AQ09, Q86YI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 14, 2009
Last modified: July 9, 2014
This is version 162 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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