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Protein

Plastin-3

Gene

PLS3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi25 – 36121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi65 – 76122PROSITE-ProRule annotationAdd
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

Osteoporosis1 Publication

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:166710
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-3PRO_0000073747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101PhosphoserineBy similarity
Modified residuei91 – 911N6-acetyllysineBy similarity
Modified residuei127 – 1271PhosphotyrosineBy similarity
Cross-linki168 – 168Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei293 – 2931Phosphoserine1 Publication
Modified residuei297 – 2971N6-acetyllysineBy similarity
Modified residuei300 – 3001N6-acetyllysineBy similarity
Modified residuei326 – 3261Phosphoserine2 Publications
Modified residuei339 – 3391Phosphoserine1 Publication
Modified residuei364 – 3641N6-acetyllysineBy similarity
Modified residuei391 – 3911Phosphothreonine2 Publications
Modified residuei409 – 4091PhosphoserineBy similarity
Modified residuei475 – 4751N6-acetyllysineBy similarity
Modified residuei545 – 5451N6-acetyllysineBy similarity
Modified residuei582 – 5821N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, 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

BgeeiP13797.
CleanExiHS_PLS3.
ExpressionAtlasiP13797. baseline and differential.
GenevestigatoriP13797.

Organism-specific databases

HPAiHPA020433.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi111372. 26 interactions.
IntActiP13797. 10 interactions.
MINTiMINT-3008106.
STRINGi9606.ENSP00000348163.

Structurei

Secondary structure

1
630
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi123 – 13614Combined sources
Turni137 – 1393Combined sources
Turni144 – 1463Combined sources
Turni151 – 1544Combined sources
Helixi155 – 1595Combined sources
Helixi160 – 1623Combined sources
Helixi164 – 17310Combined sources
Helixi180 – 1823Combined sources
Helixi190 – 20617Combined sources
Helixi216 – 2205Combined sources
Helixi224 – 24421Combined sources
Helixi261 – 2655Combined sources
Helixi269 – 28315Combined sources
Turni294 – 2985Combined sources
Helixi300 – 30910Combined sources
Beta strandi315 – 3173Combined sources
Turni326 – 3294Combined sources
Helixi333 – 34412Combined sources
Turni345 – 3484Combined sources
Helixi355 – 3595Combined sources
Helixi363 – 37412Combined sources
Helixi522 – 53514Combined sources
Helixi549 – 5513Combined sources
Helixi553 – 56210Combined sources
Turni569 – 5713Combined sources
Helixi579 – 59517Combined sources
Helixi604 – 6096Combined sources
Turni612 – 6165Combined sources
Helixi617 – 6259Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP13797.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 2 actin-binding domains.Curated
Contains 4 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00390000005691.
HOGENOMiHOG000213447.
HOVERGENiHBG003082.
InParanoidiP13797.
KOiK17336.
OMAiNAGWHKI.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P13797-1) [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
MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG
60 70 80 90 100
YKVREIIQKL MLDGDRNKDG KISFDEFVYI FQEVKSSDIA KTFRKAINRK
110 120 130 140 150
EGICALGGTS ELSSEGTQHS YSEEEKYAFV NWINKALEND PDCRHVIPMN
160 170 180 190 200
PNTDDLFKAV GDGIVLCKMI NLSVPDTIDE RAINKKKLTP FIIQENLNLA
210 220 230 240 250
LNSASAIGCH VVNIGAEDLR AGKPHLVLGL LWQIIKIGLF ADIELSRNEA
260 270 280 290 300
LAALLRDGET LEELMKLSPE ELLLRWANFH LENSGWQKIN NFSADIKDSK
310 320 330 340 350
AYFHLLNQIA PKGQKEGEPR IDINMSGFNE TDDLKRAESM LQQADKLGCR
360 370 380 390 400
QFVTPADVVS GNPKLNLAFV ANLFNKYPAL TKPENQDIDW TLLEGETREE
410 420 430 440 450
RTFRNWMNSL GVNPHVNHLY ADLQDALVIL QLYERIKVPV DWSKVNKPPY
460 470 480 490 500
PKLGANMKKL ENCNYAVELG KHPAKFSLVG IGGQDLNDGN QTLTLALVWQ
510 520 530 540 550
LMRRYTLNVL EDLGDGQKAN DDIIVNWVNR TLSEAGKSTS IQSFKDKTIS
560 570 580 590 600
SSLAVVDLID AIQPGCINYD LVKSGNLTED DKHNNAKYAV SMARRIGARV
610 620 630
YALPEDLVEV KPKMVMTVFA CLMGRGMKRV
Length:630
Mass (Da):70,811
Last modified:April 14, 2009 - v4
Checksum:i631E6F803DC56A56
GO
Isoform 2 (identifier: P13797-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MDEMATTQISKDELDELKEAFAKV → ME
     296-296: I → IKLIDFSNSV

Note: No experimental confirmation available.

Show »
Length:617
Mass (Da):69,350
Checksum:i7DD45809B012DE95
GO
Isoform 3 (identifier: P13797-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.

Note: No experimental confirmation available.

Show »
Length:585
Mass (Da):65,632
Checksum:i9291617EAC62FA5F
GO

Sequence cautioni

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

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4545Missing in isoform 3. CuratedVSP_056235Add
BLAST
Alternative sequencei1 – 2424MDEMA…AFAKV → ME in isoform 2. 1 PublicationVSP_056236Add
BLAST
Alternative sequencei296 – 2961I → IKLIDFSNSV in isoform 2. 1 PublicationVSP_056237

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22299 mRNA. Translation: AAB02844.1.
M34427 mRNA. Translation: AAA36759.1.
AK291194 mRNA. Translation: BAF83883.1.
AK294509 mRNA. Translation: BAG57725.1.
AK300575 mRNA. Translation: BAH13307.1.
AK312391 mRNA. Translation: BAG35308.1.
AC003983 Genomic DNA. No translation available.
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. [P13797-1]
CCDS65312.1. [P13797-3]
PIRiA34789.
RefSeqiNP_001129497.1. NM_001136025.4. [P13797-1]
NP_001165806.1. NM_001172335.2.
NP_001269266.1. NM_001282337.1. [P13797-2]
NP_001269267.1. NM_001282338.1. [P13797-3]
NP_005023.2. NM_005032.6. [P13797-1]
UniGeneiHs.496622.

Genome annotation databases

EnsembliENST00000355899; ENSP00000348163; ENSG00000102024. [P13797-1]
ENST00000539310; ENSP00000445339; ENSG00000102024. [P13797-3]
GeneIDi5358.
KEGGihsa:5358.
UCSCiuc004eqd.3. human. [P13797-1]

Polymorphism databases

DMDMi226694201.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22299 mRNA. Translation: AAB02844.1.
M34427 mRNA. Translation: AAA36759.1.
AK291194 mRNA. Translation: BAF83883.1.
AK294509 mRNA. Translation: BAG57725.1.
AK300575 mRNA. Translation: BAH13307.1.
AK312391 mRNA. Translation: BAG35308.1.
AC003983 Genomic DNA. No translation available.
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. [P13797-1]
CCDS65312.1. [P13797-3]
PIRiA34789.
RefSeqiNP_001129497.1. NM_001136025.4. [P13797-1]
NP_001165806.1. NM_001172335.2.
NP_001269266.1. NM_001282337.1. [P13797-2]
NP_001269267.1. NM_001282338.1. [P13797-3]
NP_005023.2. NM_005032.6. [P13797-1]
UniGeneiHs.496622.

3D structure databases

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

Protein-protein interaction databases

BioGridi111372. 26 interactions.
IntActiP13797. 10 interactions.
MINTiMINT-3008106.
STRINGi9606.ENSP00000348163.

PTM databases

PhosphoSiteiP13797.

Polymorphism databases

DMDMi226694201.

Proteomic databases

MaxQBiP13797.
PaxDbiP13797.
PRIDEiP13797.

Protocols and materials databases

DNASUi5358.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355899; ENSP00000348163; ENSG00000102024. [P13797-1]
ENST00000539310; ENSP00000445339; ENSG00000102024. [P13797-3]
GeneIDi5358.
KEGGihsa:5358.
UCSCiuc004eqd.3. human. [P13797-1]

Organism-specific databases

CTDi5358.
GeneCardsiGC0XP114795.
HGNCiHGNC:9091. PLS3.
HPAiHPA020433.
MIMi166710. phenotype.
300131. gene.
300910. phenotype.
neXtProtiNX_P13797.
Orphaneti391330. X-linked osteoporosis with fractures.
PharmGKBiPA33418.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00390000005691.
HOGENOMiHOG000213447.
HOVERGENiHBG003082.
InParanoidiP13797.
KOiK17336.
OMAiNAGWHKI.
PhylomeDBiP13797.
TreeFamiTF300680.

Miscellaneous databases

ChiTaRSiPLS3. human.
EvolutionaryTraceiP13797.
GeneWikiiPLS3.
GenomeRNAii5358.
NextBioi20770.
PROiP13797.
SOURCEiSearch...

Gene expression databases

BgeeiP13797.
CleanExiHS_PLS3.
ExpressionAtlasiP13797. baseline and differential.
GenevestigatoriP13797.

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]
ProtoNetiSearch...

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] (ISOFORM 1), 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] (ISOFORMS 1 AND 2).
    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] (ISOFORM 1).
    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. "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.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: POSSIBLE FUNCTION AS REGULATOR OF BONE DEVELOPMENT, POLYMORPHISM, VARIANT OSTEOP ASN-253 INS.
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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, B4DGB4, B7Z6M1, Q86YI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 14, 2009
Last modified: March 4, 2015
This is version 167 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

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.