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P42167

- LAP2B_HUMAN

UniProt

P42167 - LAP2B_HUMAN

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Protein

Lamina-associated polypeptide 2, isoforms beta/gamma

Gene

TMPO

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

Functioni

May help direct the assembly of the nuclear lamina and thereby help maintain the structural organization of the nuclear envelope. Possible receptor for attachment of lamin filaments to the inner nuclear membrane. May be involved in the control of initiation of DNA replication through its interaction with NAKAP95.
Thymopoietin (TP) and Thymopentin (TP5) may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. lamin binding Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
REACT_200828. Depolymerisation of the Nuclear Lamina.

Names & Taxonomyi

Protein namesi
Recommended name:
Lamina-associated polypeptide 2, isoforms beta/gamma
Alternative name(s):
Thymopoietin, isoforms beta/gamma
Short name:
TP beta/gamma
Thymopoietin-related peptide isoforms beta/gamma
Short name:
TPRP isoforms beta/gamma
Cleaved into the following 2 chains:
Thymopoietin
Short name:
TP
Alternative name(s):
Splenin
Alternative name(s):
TP5
Gene namesi
Name:TMPO
Synonyms:LAP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:11875. TMPO.

Subcellular locationi

Nucleus inner membrane; Single-pass type II membrane protein
Note: Tightly associated with the nuclear lamina.
Isoform Zeta : Cytoplasm 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei411 – 43424Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini435 – 45420LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
  4. nuclear envelope Source: ProtInc
  5. nuclear membrane Source: HPA
  6. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Pharmaceutical usei

TP5 is available under the names Timunox (Cilag), Sintomodulina (Italofarmaco) and Mepentil (Recordati). Used in primary and secondary immune deficiencies, autoimmunity, infections and cancer.

Organism-specific databases

PharmGKBiPA36576.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Lamina-associated polypeptide 2, isoforms beta/gammaPRO_0000045841Add
BLAST
Peptidei1 – 5050ThymopoietinPRO_0000017677Add
BLAST
Peptidei33 – 375ThymopentinPRO_0000017678

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571Phosphothreonine1 Publication
Modified residuei59 – 591Phosphoserine1 Publication
Modified residuei66 – 661Phosphoserine2 Publications
Modified residuei67 – 671Phosphoserine2 Publications
Modified residuei74 – 741Phosphothreonine6 Publications
Modified residuei79 – 791Phosphoserine2 Publications
Modified residuei154 – 1541Phosphothreonine1 Publication
Modified residuei156 – 1561Phosphoserine1 Publication
Modified residuei160 – 1601Phosphothreonine3 Publications
Modified residuei164 – 1641Phosphothreonine1 Publication
Modified residuei177 – 1771Phosphoserine1 Publication
Modified residuei180 – 1801Phosphoserine1 Publication
Modified residuei184 – 1841Phosphoserine1 Publication
Modified residuei207 – 2071N6-acetyllysineBy similarity
Modified residuei211 – 2111Phosphothreonine1 Publication
Modified residuei265 – 2651Phosphoserine1 Publication
Modified residuei292 – 2921Phosphoserine1 Publication
Modified residuei306 – 3061Phosphoserine8 Publications
Modified residuei312 – 3121Phosphothreonine1 Publication
Modified residuei315 – 3151Phosphoserine3 Publications
Modified residuei320 – 3201CitrullineBy similarity
Modified residuei362 – 3621Phosphoserine1 Publication
Modified residuei385 – 3851Phosphoserine1 Publication
Modified residuei389 – 3891N6-acetyllysineBy similarity

Post-translational modificationi

Mitosis-specific phosphorylation specifically abolishes its binding to lamin B and chromosomes.By similarity
Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

MaxQBiP42167.
PeptideAtlasiP42167.
PRIDEiP42167.

PTM databases

PhosphoSiteiP42167.

Miscellaneous databases

PMAP-CutDBP42167.

Expressioni

Tissue specificityi

Expressed in many tissues. Most abundant in adult thymus and fetal liver.

Gene expression databases

BgeeiP42167.
CleanExiHS_TMPO.
ExpressionAtlasiP42167. baseline and differential.
GenevestigatoriP42167.

Organism-specific databases

HPAiCAB009847.
HPA008150.

Interactioni

Subunit structurei

Interacts with LMNB1, LMNB2, BANF1, AKAP8L, GMCL and chromosomes (By similarity). Isoform Zeta interacts with BANF1/BAF and may sequester it in the cytoplasm.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-455283,EBI-389883

Protein-protein interaction databases

BioGridi112967. 51 interactions.
IntActiP42167. 8 interactions.
MINTiMINT-2839042.

Structurei

3D structure databases

ProteinModelPortaliP42167.
SMRiP42167. Positions 2-57, 103-159.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 4844LEM-likePROSITE-ProRule annotationAdd
BLAST
Domaini109 – 15345LEMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 410410NucleoplasmicSequence AnalysisAdd
BLAST
Regioni49 – 10860LinkerAdd
BLAST
Regioni138 – 243106NAKAP95-binding NAdd
BLAST
Regioni299 – 37173Binds lamins BAdd
BLAST
Regioni300 – 37475NAKAP95-binding CAdd
BLAST

Domaini

Has two structurally independent, non-interacting domains: LEM-like (also called LAP2-N or LEM-D) and LEM (also called LAP2-C or LEM-B). LEM-like binds DNA while LEM interacts with BANF1.

Sequence similaritiesi

Belongs to the LEM family.Curated
Contains 1 LEM domain.PROSITE-ProRule annotation
Contains 1 LEM-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00510000048934.
HOGENOMiHOG000113280.
HOVERGENiHBG000166.
OMAiTGNFKHA.

Family and domain databases

Gene3Di1.10.720.40. 2 hits.
InterProiIPR013146. LEM-like_dom.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view]
PfamiPF03020. LEM. 1 hit.
PF08198. Thymopoietin. 1 hit.
[Graphical view]
SMARTiSM00540. LEM. 1 hit.
[Graphical view]
SUPFAMiSSF63451. SSF63451. 2 hits.
PROSITEiPS50954. LEM. 1 hit.
PS50955. LEM_LIKE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform Beta (identifier: P42167-1) [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
MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR
60 70 80 90 100
PPLPAGTNSK GPPDFSSDEE REPTPVLGSG AAAAGRSRAA VGRKATKKTD
110 120 130 140 150
KPRQEDKDDL DVTELTNEDL LDQLVKYGVN PGPIVGTTRK LYEKKLLKLR
160 170 180 190 200
EQGTESRSST PLPTISSSAE NTRQNGSNDS DRYSDNEEDS KIELKLEKRE
210 220 230 240 250
PLKGRAKTPV TLKQRRVEHN QSYSQAGITE TEWTSGSSKG GPLQALTRES
260 270 280 290 300
TRGSRRTPRK RVETSEHFRI DGPVISESTP IAETIMASSN ESLVVNRVTG
310 320 330 340 350
NFKHASPILP ITEFSDIPRR APKKPLTRAE VGEKTEERRV ERDILKEMFP
360 370 380 390 400
YEASTPTGIS ASCRRPIKGA AGRPLELSDF RMEESFSSKY VPKYVPLADV
410 420 430 440 450
KSEKTKKGRS IPVWIKILLF VVVAVFLFLV YQAMETNQVN PFSNFLHVDP

RKSN
Length:454
Mass (Da):50,670
Last modified:January 23, 2007 - v2
Checksum:i03277C5723117909
GO
Isoform Alpha (identifier: P42166-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry P42166.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:694
Mass (Da):75,492
GO
Isoform Gamma (identifier: P42167-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     222-330: Missing.

Show »
Length:345
Mass (Da):38,738
Checksum:iF0669D9AEF97B32E
GO
Isoform Zeta (identifier: P42167-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     222-248: SYSQAGITETEWTSGSSKGGPLQALTR → VSLVLLPPCTGINNLLTTLIHVLAFNG
     249-454: Missing.

Note: Inhibits LAP2beta-mediated repression.

Show »
Length:248
Mass (Da):27,388
Checksum:iC3CDE62D4C0B0590
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti287 – 2871A → P.
Corresponds to variant rs7133258 [ dbSNP | Ensembl ].
VAR_049779
Natural varianti427 – 4271L → F.
Corresponds to variant rs1058288 [ dbSNP | Ensembl ].
VAR_014786

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei222 – 330109Missing in isoform Gamma. 2 PublicationsVSP_004456Add
BLAST
Alternative sequencei222 – 24827SYSQA…QALTR → VSLVLLPPCTGINNLLTTLI HVLAFNG in isoform Zeta. 1 PublicationVSP_056162Add
BLAST
Alternative sequencei249 – 454206Missing in isoform Zeta. 1 PublicationVSP_056163Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09087 mRNA. Translation: AAB60330.1.
U09088 mRNA. Translation: AAB60331.1.
EF028063 mRNA. Translation: ABL61272.1.
AF070631 mRNA. Translation: AAC25390.1.
BC053675 mRNA. Translation: AAH53675.1.
U18269
, U18266, U18267, U18268, U18270 Genomic DNA. Translation: AAB60434.1.
U18271 Genomic DNA. Translation: AAB60435.1.
CCDSiCCDS31879.1. [P42167-1]
CCDS31880.1. [P42167-2]
PIRiB55741.
C55741.
RefSeqiNP_001027454.1. NM_001032283.2. [P42167-1]
NP_001027455.1. NM_001032284.2. [P42167-2]
UniGeneiHs.11355.

Genome annotation databases

EnsembliENST00000261210; ENSP00000261210; ENSG00000120802. [P42167-3]
ENST00000393053; ENSP00000376773; ENSG00000120802. [P42167-2]
ENST00000556029; ENSP00000450627; ENSG00000120802. [P42167-1]
GeneIDi7112.
KEGGihsa:7112.
UCSCiuc001tfj.3. human. [P42167-1]
uc001tfk.3. human. [P42167-2]

Polymorphism databases

DMDMi1174690.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09087 mRNA. Translation: AAB60330.1 .
U09088 mRNA. Translation: AAB60331.1 .
EF028063 mRNA. Translation: ABL61272.1 .
AF070631 mRNA. Translation: AAC25390.1 .
BC053675 mRNA. Translation: AAH53675.1 .
U18269
, U18266 , U18267 , U18268 , U18270 Genomic DNA. Translation: AAB60434.1 .
U18271 Genomic DNA. Translation: AAB60435.1 .
CCDSi CCDS31879.1. [P42167-1 ]
CCDS31880.1. [P42167-2 ]
PIRi B55741.
C55741.
RefSeqi NP_001027454.1. NM_001032283.2. [P42167-1 ]
NP_001027455.1. NM_001032284.2. [P42167-2 ]
UniGenei Hs.11355.

3D structure databases

ProteinModelPortali P42167.
SMRi P42167. Positions 2-57, 103-159.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112967. 51 interactions.
IntActi P42167. 8 interactions.
MINTi MINT-2839042.

PTM databases

PhosphoSitei P42167.

Polymorphism databases

DMDMi 1174690.

Proteomic databases

MaxQBi P42167.
PeptideAtlasi P42167.
PRIDEi P42167.

Protocols and materials databases

DNASUi 7112.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261210 ; ENSP00000261210 ; ENSG00000120802 . [P42167-3 ]
ENST00000393053 ; ENSP00000376773 ; ENSG00000120802 . [P42167-2 ]
ENST00000556029 ; ENSP00000450627 ; ENSG00000120802 . [P42167-1 ]
GeneIDi 7112.
KEGGi hsa:7112.
UCSCi uc001tfj.3. human. [P42167-1 ]
uc001tfk.3. human. [P42167-2 ]

Organism-specific databases

CTDi 7112.
GeneCardsi GC12P098909.
GeneReviewsi TMPO.
HGNCi HGNC:11875. TMPO.
HPAi CAB009847.
HPA008150.
MIMi 188380. gene.
neXtProti NX_P42167.
PharmGKBi PA36576.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00510000048934.
HOGENOMi HOG000113280.
HOVERGENi HBG000166.
OMAi TGNFKHA.

Enzyme and pathway databases

Reactomei REACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
REACT_200828. Depolymerisation of the Nuclear Lamina.

Miscellaneous databases

ChiTaRSi TMPO. human.
GenomeRNAii 7112.
NextBioi 27839.
PMAP-CutDB P42167.
PROi P42167.
SOURCEi Search...

Gene expression databases

Bgeei P42167.
CleanExi HS_TMPO.
ExpressionAtlasi P42167. baseline and differential.
Genevestigatori P42167.

Family and domain databases

Gene3Di 1.10.720.40. 2 hits.
InterProi IPR013146. LEM-like_dom.
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view ]
Pfami PF03020. LEM. 1 hit.
PF08198. Thymopoietin. 1 hit.
[Graphical view ]
SMARTi SM00540. LEM. 1 hit.
[Graphical view ]
SUPFAMi SSF63451. SSF63451. 2 hits.
PROSITEi PS50954. LEM. 1 hit.
PS50955. LEM_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Three distinct human thymopoietins are derived from alternatively spliced mRNAs."
    Harris C.A., Andryuk P.J., Cline S.W., Chan H.K., Natarajan A., Siekierka J.J., Goldstein G.
    Proc. Natl. Acad. Sci. U.S.A. 91:6283-6287(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
    Tissue: Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZETA), SUBCELLULAR LOCATION (ISOFORM ZETA).
  3. Yu W., Gibbs R.A.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA).
    Tissue: Brain.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 BETA).
    Tissue: Eye.
  6. "Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO beta to rat lamin-associated polypeptide 2."
    Harris C.A., Andryuk P.J., Cline S.W., Siekierka J.J., Goldstein G.
    Genomics 28:198-205(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-237 AND 313-454 (ISOFORMS BETA AND GAMMA).
  7. "Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin."
    Furukawa K., Kondo T.
    Eur. J. Biochem. 251:729-733(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LMNB1.
  8. "HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication."
    Martins S., Eikvar S., Furukawa K., Collas P.
    J. Cell Biol. 160:177-188(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKAP8L.
  9. "Review: lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics."
    Dechat T., Vlcek S., Foisner R.
    J. Struct. Biol. 129:335-345(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  10. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  12. "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 SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-306 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  16. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74 AND SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-66; SER-67; THR-74; SER-79; THR-160; THR-164; SER-177; SER-180; SER-306; SER-315; SER-362 AND SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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].
  20. "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 SER-66; SER-67; THR-74; SER-79; THR-154; THR-160; SER-292 AND SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "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-74; SER-156; THR-160; THR-211; SER-265; SER-306; THR-312 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; THR-74 AND SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA."
    Cai M., Huang Y., Ghirlando R., Wilson K.L., Craigie R., Clore G.M.
    EMBO J. 20:4399-4407(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-169.
  25. "Structural characterization of the LEM motif common to three human inner nuclear membrane proteins."
    Laguri C., Gilquin B., Wolff N., Romi-Lebrun R., Courchay K., Callebaut I., Worman H.J., Zinn-Justin S.
    Structure 9:503-511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-57 AND 103-159.

Entry informationi

Entry nameiLAP2B_HUMAN
AccessioniPrimary (citable) accession number: P42167
Secondary accession number(s): A2T926, Q14861
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 152 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

Complete proteome, Pharmaceutical, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families

External Data

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