Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein LSM14 homolog A

Gene

LSM14A

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

Functioni

Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for non-translating mRNAs.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Repressor, Ribonucleoprotein

Keywords - Biological processi

Translation regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein LSM14 homolog A
Alternative name(s):
Protein FAM61A
Protein SCD6 homolog
Putative alpha-synuclein-binding protein
Short name:
AlphaSNBP
RNA-associated protein 55A
Short name:
hRAP55
Short name:
hRAP55A
Gene namesi
Name:LSM14A
Synonyms:C19orf13, FAM61A, RAP55, RAP55A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:24489. LSM14A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytoplasmic stress granule Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134989467.

Polymorphism and mutation databases

BioMutaiLSM14A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 463462Protein LSM14 homolog APRO_0000187090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei182 – 1821PhosphoserineCombined sources
Modified residuei183 – 1831PhosphoserineCombined sources
Modified residuei192 – 1921PhosphoserineCombined sources
Modified residuei194 – 1941PhosphothreonineCombined sources
Modified residuei216 – 2161PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8ND56.
MaxQBiQ8ND56.
PaxDbiQ8ND56.
PRIDEiQ8ND56.

PTM databases

iPTMnetiQ8ND56.
PhosphoSiteiQ8ND56.

Expressioni

Gene expression databases

BgeeiQ8ND56.
CleanExiHS_LSM14A.
ExpressionAtlasiQ8ND56. baseline and differential.
GenevisibleiQ8ND56. HS.

Organism-specific databases

HPAiHPA017961.

Interactioni

Subunit structurei

Component of a ribonucleoprotein (RNP) complex.By similarity

Protein-protein interaction databases

BioGridi117527. 20 interactions.
IntActiQ8ND56. 7 interactions.
MINTiMINT-5005437.
STRINGi9606.ENSP00000413964.

Structurei

3D structure databases

ProteinModelPortaliQ8ND56.
SMRiQ8ND56. Positions 2-83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini284 – 32037DFDFPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi361 – 37717FFD boxAdd
BLAST
Motifi380 – 40021TFG boxAdd
BLAST

Domaini

The LSM14 domain and the RGG repeats are required for accumulation in P-bodies, and the region containing the FDF motif is responsible for cytoplasmic retention.1 Publication

Sequence similaritiesi

Belongs to the LSM14 family.Curated
Contains 1 DFDF domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1073. Eukaryota.
ENOG41122RA. LUCA.
GeneTreeiENSGT00390000004174.
HOGENOMiHOG000231251.
HOVERGENiHBG054326.
InParanoidiQ8ND56.
KOiK18749.
OMAiPSYAHPM.
PhylomeDBiQ8ND56.
TreeFamiTF313514.

Family and domain databases

InterProiIPR025762. DFDF.
IPR019050. FDF_dom.
IPR025761. FFD_box.
IPR025609. Lsm14_N.
IPR010920. LSM_dom.
IPR025768. TFG_box.
[Graphical view]
PfamiPF09532. FDF. 1 hit.
PF12701. LSM14. 1 hit.
[Graphical view]
SMARTiSM01199. FDF. 1 hit.
SM01271. LSM14. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
PROSITEiPS51512. DFDF. 1 hit.
PS51513. FFD. 1 hit.
PS51536. TFG. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: Q8ND56-1) [UniParc]FASTAAdd to basket

Also known as: AlphaSNBP(A)

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
MSGGTPYIGS KISLISKAEI RYEGILYTID TENSTVALAK VRSFGTEDRP
60 70 80 90 100
TDRPIPPRDE VFEYIIFRGS DIKDLTVCEP PKPQCSLPQD PAIVQSSLGS
110 120 130 140 150
STSSFQSMGS YGPFGRMPTY SQFSPSSLVG QQFGAVGVAG SSLTSFGTET
160 170 180 190 200
SNSGTLPQSS AVGSAFTQDT RSLKTQLSQG RSSPQLDPLR KSPTMEQAVQ
210 220 230 240 250
TASAHLPAPA AVGRRSPVST RPLPSASQKA GENQEHRRAE VHKVSRPENE
260 270 280 290 300
QLRNDNKRQV APGAPSAPRR GRGGHRGGRG RFGIRRDGPM KFEKDFDFES
310 320 330 340 350
ANAQFNKEEI DREFHNKLKL KEDKLEKQEK PVNGEDKGDS GVDTQNSEGN
360 370 380 390 400
ADEEDPLGPN CYYDKTKSFF DNISCDDNRE RRPTWAEERR LNAETFGIPL
410 420 430 440 450
RPNRGRGGYR GRGGLGFRGG RGRGGGRGGT FTAPRGFRGG FRGGRGGREF
460
ADFEYRKTTA FGP
Length:463
Mass (Da):50,530
Last modified:August 2, 2005 - v3
Checksum:i703BE8E8C54799DF
GO
Isoform 2 (identifier: Q8ND56-2) [UniParc]FASTAAdd to basket

Also known as: AlphaSNBP(B)

The sequence of this isoform differs from the canonical sequence as follows:
     458-463: TTAFGP → DNKVAA

Show »
Length:463
Mass (Da):50,554
Checksum:i6A8E53E630BC99DF
GO
Isoform 3 (identifier: Q8ND56-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     139-179: Missing.

Note: No experimental confirmation available.
Show »
Length:422
Mass (Da):46,411
Checksum:iF28872726A8AC2D1
GO

Sequence cautioni

The sequence BAB55066.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171K → Q in CAD39060 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti238 – 2381R → Q.2 Publications
Corresponds to variant rs36006556 [ dbSNP | Ensembl ].
VAR_057532
Natural varianti448 – 4481R → Q.
Corresponds to variant rs2274896 [ dbSNP | Ensembl ].
VAR_022884

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei139 – 17941Missing in isoform 3. 1 PublicationVSP_057232Add
BLAST
Alternative sequencei458 – 4636TTAFGP → DNKVAA in isoform 2. 3 PublicationsVSP_014650

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB069974 mRNA. Translation: BAC99045.1.
AB069975 mRNA. Translation: BAC99046.1.
AK027369 mRNA. Translation: BAB55066.1. Different initiation.
AK027643 mRNA. Translation: BAB55259.1.
AK300208 mRNA. Translation: BAG61978.1.
AL834398 mRNA. Translation: CAD39060.2.
AL117499 mRNA. Translation: CAB55964.1.
AC010614 Genomic DNA. No translation available.
BC016842 mRNA. Translation: AAH16842.1.
CCDSiCCDS12435.1. [Q8ND56-2]
CCDS46040.1. [Q8ND56-1]
PIRiT17274.
RefSeqiNP_001107565.1. NM_001114093.1. [Q8ND56-1]
NP_056393.2. NM_015578.2. [Q8ND56-2]
UniGeneiHs.744009.

Genome annotation databases

EnsembliENST00000433627; ENSP00000413964; ENSG00000257103. [Q8ND56-1]
ENST00000540746; ENSP00000446451; ENSG00000257103. [Q8ND56-3]
ENST00000544216; ENSP00000446271; ENSG00000257103. [Q8ND56-2]
ENST00000570462; ENSP00000459843; ENSG00000262860. [Q8ND56-1]
ENST00000575811; ENSP00000461225; ENSG00000262860. [Q8ND56-2]
GeneIDi26065.
KEGGihsa:26065.
UCSCiuc002nva.5. human. [Q8ND56-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB069974 mRNA. Translation: BAC99045.1.
AB069975 mRNA. Translation: BAC99046.1.
AK027369 mRNA. Translation: BAB55066.1. Different initiation.
AK027643 mRNA. Translation: BAB55259.1.
AK300208 mRNA. Translation: BAG61978.1.
AL834398 mRNA. Translation: CAD39060.2.
AL117499 mRNA. Translation: CAB55964.1.
AC010614 Genomic DNA. No translation available.
BC016842 mRNA. Translation: AAH16842.1.
CCDSiCCDS12435.1. [Q8ND56-2]
CCDS46040.1. [Q8ND56-1]
PIRiT17274.
RefSeqiNP_001107565.1. NM_001114093.1. [Q8ND56-1]
NP_056393.2. NM_015578.2. [Q8ND56-2]
UniGeneiHs.744009.

3D structure databases

ProteinModelPortaliQ8ND56.
SMRiQ8ND56. Positions 2-83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117527. 20 interactions.
IntActiQ8ND56. 7 interactions.
MINTiMINT-5005437.
STRINGi9606.ENSP00000413964.

PTM databases

iPTMnetiQ8ND56.
PhosphoSiteiQ8ND56.

Polymorphism and mutation databases

BioMutaiLSM14A.

Proteomic databases

EPDiQ8ND56.
MaxQBiQ8ND56.
PaxDbiQ8ND56.
PRIDEiQ8ND56.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000433627; ENSP00000413964; ENSG00000257103. [Q8ND56-1]
ENST00000540746; ENSP00000446451; ENSG00000257103. [Q8ND56-3]
ENST00000544216; ENSP00000446271; ENSG00000257103. [Q8ND56-2]
ENST00000570462; ENSP00000459843; ENSG00000262860. [Q8ND56-1]
ENST00000575811; ENSP00000461225; ENSG00000262860. [Q8ND56-2]
GeneIDi26065.
KEGGihsa:26065.
UCSCiuc002nva.5. human. [Q8ND56-1]

Organism-specific databases

CTDi26065.
GeneCardsiLSM14A.
HGNCiHGNC:24489. LSM14A.
HPAiHPA017961.
MIMi610677. gene.
neXtProtiNX_Q8ND56.
PharmGKBiPA134989467.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1073. Eukaryota.
ENOG41122RA. LUCA.
GeneTreeiENSGT00390000004174.
HOGENOMiHOG000231251.
HOVERGENiHBG054326.
InParanoidiQ8ND56.
KOiK18749.
OMAiPSYAHPM.
PhylomeDBiQ8ND56.
TreeFamiTF313514.

Miscellaneous databases

ChiTaRSiLSM14A. human.
GenomeRNAii26065.
PROiQ8ND56.
SOURCEiSearch...

Gene expression databases

BgeeiQ8ND56.
CleanExiHS_LSM14A.
ExpressionAtlasiQ8ND56. baseline and differential.
GenevisibleiQ8ND56. HS.

Family and domain databases

InterProiIPR025762. DFDF.
IPR019050. FDF_dom.
IPR025761. FFD_box.
IPR025609. Lsm14_N.
IPR010920. LSM_dom.
IPR025768. TFG_box.
[Graphical view]
PfamiPF09532. FDF. 1 hit.
PF12701. LSM14. 1 hit.
[Graphical view]
SMARTiSM01199. FDF. 1 hit.
SM01271. LSM14. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
PROSITEiPS51512. DFDF. 1 hit.
PS51513. FFD. 1 hit.
PS51536. TFG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Possible alpha synuclein binding protein."
    Takeda K., Araki W., Tabira T.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  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] (ISOFORMS 2 AND 3), VARIANT GLN-238.
    Tissue: Mammary gland and Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-238.
    Tissue: Brain and Testis.
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [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 2).
    Tissue: Pancreas.
  6. "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-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "RAP55, a cytoplasmic mRNP component, represses translation in Xenopus oocytes."
    Tanaka K.J., Ogawa K., Takagi M., Imamoto N., Matsumoto K., Tsujimoto M.
    J. Biol. Chem. 281:40096-40106(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "RNA-associated protein 55 (RAP55) localizes to mRNA processing bodies and stress granules."
    Yang W.H., Yu J.H., Gulick T., Bloch K.D., Bloch D.B.
    RNA 12:547-554(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. "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 SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-183; SER-192; THR-194 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "RAP55: insights into an evolutionarily conserved protein family."
    Marnef A., Sommerville J., Ladomery M.R.
    Int. J. Biochem. Cell Biol. 41:977-981(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "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-183; SER-192 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-192 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiLS14A_HUMAN
AccessioniPrimary (citable) accession number: Q8ND56
Secondary accession number(s): B4DTG6
, Q76LX7, Q96AR3, Q96K73, Q96SN5, Q9UFR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2005
Last sequence update: August 2, 2005
Last modified: June 8, 2016
This is version 125 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

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 one 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.