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O43768

- ENSA_HUMAN

UniProt

O43768 - ENSA_HUMAN

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Protein

Alpha-endosulfine

Gene

ENSA

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

Functioni

Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase (By similarity). Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents.By similarity1 Publication

GO - Molecular functioni

  1. ion channel inhibitor activity Source: ProtInc
  2. phosphatase inhibitor activity Source: UniProtKB
  3. potassium channel inhibitor activity Source: MGI
  4. protein phosphatase 2A binding Source: UniProtKB
  5. protein phosphatase inhibitor activity Source: UniProtKB-KW
  6. protein phosphatase type 2A regulator activity Source: UniProtKB
  7. receptor binding Source: MGI

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: UniProtKB
  2. mitotic cell cycle Source: Reactome
  3. mitotic nuclear division Source: UniProtKB
  4. negative regulation of catalytic activity Source: GOC
  5. regulation of catalytic activity Source: GOC
  6. regulation of insulin secretion Source: MGI
  7. response to glucose Source: Ensembl
  8. response to nutrient Source: ProtInc
  9. transport Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Protein phosphatase inhibitor

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150182. MASTL Facilitates Mitotic Progression.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-endosulfine
Alternative name(s):
ARPP-19e
Gene namesi
Name:ENSA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3360. ENSA.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091S → E: Mimicks a phosphorylated state and impairs interaction with SNCA. 1 Publication

Organism-specific databases

PharmGKBiPA27796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 121120Alpha-endosulfinePRO_0000146758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei2 – 21Phosphoserine3 Publications
Modified residuei67 – 671Phosphoserine; by GWL1 Publication
Modified residuei109 – 1091Phosphoserine; by PKA3 Publications

Post-translational modificationi

Phosphorylation at Ser-67 by GWL during mitosis is essential for interaction with PPP2R2D (PR55-delta) and subsequent inactivation of PP2A (By similarity). Phosphorylated by PKA.By similarity5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO43768.
PaxDbiO43768.
PRIDEiO43768.

PTM databases

PhosphoSiteiO43768.

Expressioni

Tissue specificityi

Widely expressed with high levels in skeletal muscle and brain and lower levels in the pancreas.2 Publications

Gene expression databases

BgeeiO43768.
CleanExiHS_ENSA.
ExpressionAtlasiO43768. baseline and differential.
GenevestigatoriO43768.

Organism-specific databases

HPAiHPA051294.

Interactioni

Subunit structurei

Interacts (when phosphorylated at Ser-67) with PPP2R2D (By similarity). Interacts with ABCC8. Interacts with SNCA; interaction is disrupted when phosphorylated at Ser-109.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MCM3P252051EBI-714511,EBI-355153

Protein-protein interaction databases

BioGridi108343. 10 interactions.
IntActiO43768. 5 interactions.
MINTiMINT-1431607.

Structurei

3D structure databases

ProteinModelPortaliO43768.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the endosulfine family.Curated

Phylogenomic databases

eggNOGiNOG312450.
GeneTreeiENSGT00390000010139.
HOVERGENiHBG000297.
InParanoidiO43768.
PhylomeDBiO43768.
TreeFamiTF314718.

Family and domain databases

InterProiIPR006760. Endosulphine.
[Graphical view]
PfamiPF04667. Endosulfine. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

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

This entry describes 9 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43768-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha

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
MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG
60 70 80 90 100
SDFLMKRLQK GQKYFDSGDY NMAKAKMKNK QLPSAGPDKN LVTGDHIPTP
110 120
QDLPQRKSSL VTSKLAGGQV E
Length:121
Mass (Da):13,389
Last modified:June 1, 1998 - v1
Checksum:i7C76315AA17E7542
GO
Isoform 2 (identifier: O43768-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     118-121: Missing.

Show »
Length:117
Mass (Da):12,976
Checksum:iD17E754219767472
GO
Isoform 3 (identifier: O43768-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: G → GDYKSLHWSVLLCADEM

Show »
Length:137
Mass (Da):15,281
Checksum:iE9CF169C48A1FC1B
GO
Isoform 4 (identifier: O43768-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: G → GVWGIASYPLSLGLKEVLRMKSVE
     118-121: Missing.

Show »
Length:140
Mass (Da):15,534
Checksum:i2AB6570AFD91E54D
GO
Isoform 5 (identifier: O43768-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: Missing.
     5-19: QEEENPAEETGEEKQ → MAGGLGCDVCYWFVE

Show »
Length:117
Mass (Da):12,818
Checksum:iEEE3B2739FD70FC2
GO
Isoform 6 (identifier: O43768-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: Missing.
     5-19: QEEENPAEETGEEKQ → MAGGLGCDVCYWFVE
     118-121: Missing.

Show »
Length:113
Mass (Da):12,404
Checksum:iCFD70FC2E5FE760C
GO
Isoform 7 (identifier: O43768-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: Missing.
     5-19: QEEENPAEETGEEKQ → MAGGLGCDVCYWFVE
     61-61: G → GDYKSLHWSVLLCADEM

Show »
Length:133
Mass (Da):14,710
Checksum:i852736F0B466D4AB
GO
Isoform 8 (identifier: O43768-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     62-121: QKYFDSGDYN...TSKLAGGQVE → VWGIVSYPLS...LNRSRGEFEI

Show »
Length:105
Mass (Da):11,990
Checksum:iE6306F60528ECCA4
GO
Isoform 9 (identifier: O43768-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: G → GDYKSLHWSVLLCADEM
     118-121: Missing.

Note: No experimental confirmation available.

Show »
Length:133
Mass (Da):14,868
Checksum:i28A1FC1BE09A3895
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51Q → R in CAG38815. 1 PublicationCurated
Sequence conflicti21 – 211T → M in BAF82753. (PubMed:14702039)Curated
Sequence conflicti22 – 221Q → L in AAH68544. (PubMed:15489334)Curated
Sequence conflicti114 – 1141K → Q in CAG33411. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 44Missing in isoform 5, isoform 6 and isoform 7. 1 PublicationVSP_037063
Alternative sequencei5 – 1915QEEEN…GEEKQ → MAGGLGCDVCYWFVE in isoform 5, isoform 6 and isoform 7. 1 PublicationVSP_037064Add
BLAST
Alternative sequencei61 – 611G → GDYKSLHWSVLLCADEM in isoform 3, isoform 7 and isoform 9. 1 PublicationVSP_037065
Alternative sequencei61 – 611G → GVWGIASYPLSLGLKEVLRM KSVE in isoform 4. 1 PublicationVSP_037066
Alternative sequencei62 – 12160QKYFD…GGQVE → VWGIVSYPLSLELKEVLRMK SVEVLLDPFLEVLLLNRSRG EFEI in isoform 8. CuratedVSP_037067Add
BLAST
Alternative sequencei118 – 1214Missing in isoform 2, isoform 4, isoform 6 and isoform 9. 5 PublicationsVSP_001443

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99906 mRNA. Translation: CAA68180.1.
AJ010966 Genomic DNA. Translation: CAB65125.1.
AY326403
, AY326400, AY326401, AY326402 Genomic DNA. Translation: AAQ73827.1.
AY326403
, AY326400, AY326401, AY326402 Genomic DNA. Translation: AAQ73828.1.
AY326402, AY326400, AY326401 Genomic DNA. Translation: AAQ73829.1.
AY326401, AY326400 Genomic DNA. Translation: AAQ73830.1.
AY326403
, AY326400, AY326401, AY326402 Genomic DNA. Translation: AAQ73831.1.
AY326403
, AY326400, AY326401, AY326402 Genomic DNA. Translation: AAQ73832.1.
AF067170 mRNA. Translation: AAD32454.1.
AF157509 mRNA. Translation: AAF80340.1.
AF157510 mRNA. Translation: AAF80341.1.
AK001981 mRNA. Translation: BAG50998.1.
AK290064 mRNA. Translation: BAF82753.1.
DA888224 mRNA. No translation available.
CR749580 mRNA. Translation: CAH18372.1.
CR457130 mRNA. Translation: CAG33411.1.
CR536578 mRNA. Translation: CAG38815.1.
AL356356 Genomic DNA. Translation: CAI15505.1.
AL356356 Genomic DNA. Translation: CAI15506.1.
AL356356 Genomic DNA. Translation: CAI15507.1.
AL356356 Genomic DNA. Translation: CAI15509.1.
AL356356 Genomic DNA. Translation: CAI15510.1.
AL356356 Genomic DNA. Translation: CAI15511.1.
AL356356 Genomic DNA. Translation: CAI15512.1.
CH471121 Genomic DNA. Translation: EAW53528.1.
CH471121 Genomic DNA. Translation: EAW53529.1.
CH471121 Genomic DNA. Translation: EAW53530.1.
CH471121 Genomic DNA. Translation: EAW53532.1.
CH471121 Genomic DNA. Translation: EAW53533.1.
BC000436 mRNA. Translation: AAH00436.1.
BC004461 mRNA. Translation: AAH04461.1.
BC068544 mRNA. Translation: AAH68544.1.
BC069208 mRNA. Translation: AAH69208.1.
CCDSiCCDS958.1. [O43768-1]
CCDS959.1. [O43768-3]
CCDS960.1. [O43768-7]
CCDS961.1. [O43768-5]
CCDS962.1. [O43768-9]
CCDS963.1. [O43768-2]
CCDS964.1. [O43768-6]
CCDS965.1. [O43768-8]
RefSeqiNP_004427.1. NM_004436.2. [O43768-1]
NP_996925.1. NM_207042.1. [O43768-3]
NP_996926.1. NM_207043.1. [O43768-9]
NP_996927.1. NM_207044.1. [O43768-2]
NP_996928.1. NM_207045.1. [O43768-7]
NP_996929.1. NM_207046.1. [O43768-5]
NP_996930.1. NM_207047.1. [O43768-6]
NP_997051.1. NM_207168.1. [O43768-8]
UniGeneiHs.632456.

Genome annotation databases

EnsembliENST00000271690; ENSP00000271690; ENSG00000143420. [O43768-2]
ENST00000339643; ENSP00000341743; ENSG00000143420. [O43768-3]
ENST00000361532; ENSP00000354835; ENSG00000143420. [O43768-5]
ENST00000361631; ENSP00000355239; ENSG00000143420. [O43768-7]
ENST00000362052; ENSP00000355220; ENSG00000143420. [O43768-8]
ENST00000369014; ENSP00000358010; ENSG00000143420. [O43768-1]
ENST00000503241; ENSP00000424242; ENSG00000143420. [O43768-9]
ENST00000503345; ENSP00000421458; ENSG00000143420. [O43768-8]
ENST00000509582; ENSP00000426110; ENSG00000143420. [O43768-8]
ENST00000513281; ENSP00000422343; ENSG00000143420. [O43768-6]
GeneIDi2029.
KEGGihsa:2029.
UCSCiuc001evb.3. human. [O43768-7]
uc001evc.3. human. [O43768-5]
uc001evd.3. human. [O43768-3]
uc001eve.3. human. [O43768-1]
uc001evf.3. human. [O43768-6]
uc001evi.3. human. [O43768-8]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99906 mRNA. Translation: CAA68180.1 .
AJ010966 Genomic DNA. Translation: CAB65125.1 .
AY326403
, AY326400 , AY326401 , AY326402 Genomic DNA. Translation: AAQ73827.1 .
AY326403
, AY326400 , AY326401 , AY326402 Genomic DNA. Translation: AAQ73828.1 .
AY326402 , AY326400 , AY326401 Genomic DNA. Translation: AAQ73829.1 .
AY326401 , AY326400 Genomic DNA. Translation: AAQ73830.1 .
AY326403
, AY326400 , AY326401 , AY326402 Genomic DNA. Translation: AAQ73831.1 .
AY326403
, AY326400 , AY326401 , AY326402 Genomic DNA. Translation: AAQ73832.1 .
AF067170 mRNA. Translation: AAD32454.1 .
AF157509 mRNA. Translation: AAF80340.1 .
AF157510 mRNA. Translation: AAF80341.1 .
AK001981 mRNA. Translation: BAG50998.1 .
AK290064 mRNA. Translation: BAF82753.1 .
DA888224 mRNA. No translation available.
CR749580 mRNA. Translation: CAH18372.1 .
CR457130 mRNA. Translation: CAG33411.1 .
CR536578 mRNA. Translation: CAG38815.1 .
AL356356 Genomic DNA. Translation: CAI15505.1 .
AL356356 Genomic DNA. Translation: CAI15506.1 .
AL356356 Genomic DNA. Translation: CAI15507.1 .
AL356356 Genomic DNA. Translation: CAI15509.1 .
AL356356 Genomic DNA. Translation: CAI15510.1 .
AL356356 Genomic DNA. Translation: CAI15511.1 .
AL356356 Genomic DNA. Translation: CAI15512.1 .
CH471121 Genomic DNA. Translation: EAW53528.1 .
CH471121 Genomic DNA. Translation: EAW53529.1 .
CH471121 Genomic DNA. Translation: EAW53530.1 .
CH471121 Genomic DNA. Translation: EAW53532.1 .
CH471121 Genomic DNA. Translation: EAW53533.1 .
BC000436 mRNA. Translation: AAH00436.1 .
BC004461 mRNA. Translation: AAH04461.1 .
BC068544 mRNA. Translation: AAH68544.1 .
BC069208 mRNA. Translation: AAH69208.1 .
CCDSi CCDS958.1. [O43768-1 ]
CCDS959.1. [O43768-3 ]
CCDS960.1. [O43768-7 ]
CCDS961.1. [O43768-5 ]
CCDS962.1. [O43768-9 ]
CCDS963.1. [O43768-2 ]
CCDS964.1. [O43768-6 ]
CCDS965.1. [O43768-8 ]
RefSeqi NP_004427.1. NM_004436.2. [O43768-1 ]
NP_996925.1. NM_207042.1. [O43768-3 ]
NP_996926.1. NM_207043.1. [O43768-9 ]
NP_996927.1. NM_207044.1. [O43768-2 ]
NP_996928.1. NM_207045.1. [O43768-7 ]
NP_996929.1. NM_207046.1. [O43768-5 ]
NP_996930.1. NM_207047.1. [O43768-6 ]
NP_997051.1. NM_207168.1. [O43768-8 ]
UniGenei Hs.632456.

3D structure databases

ProteinModelPortali O43768.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108343. 10 interactions.
IntActi O43768. 5 interactions.
MINTi MINT-1431607.

PTM databases

PhosphoSitei O43768.

Proteomic databases

MaxQBi O43768.
PaxDbi O43768.
PRIDEi O43768.

Protocols and materials databases

DNASUi 2029.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000271690 ; ENSP00000271690 ; ENSG00000143420 . [O43768-2 ]
ENST00000339643 ; ENSP00000341743 ; ENSG00000143420 . [O43768-3 ]
ENST00000361532 ; ENSP00000354835 ; ENSG00000143420 . [O43768-5 ]
ENST00000361631 ; ENSP00000355239 ; ENSG00000143420 . [O43768-7 ]
ENST00000362052 ; ENSP00000355220 ; ENSG00000143420 . [O43768-8 ]
ENST00000369014 ; ENSP00000358010 ; ENSG00000143420 . [O43768-1 ]
ENST00000503241 ; ENSP00000424242 ; ENSG00000143420 . [O43768-9 ]
ENST00000503345 ; ENSP00000421458 ; ENSG00000143420 . [O43768-8 ]
ENST00000509582 ; ENSP00000426110 ; ENSG00000143420 . [O43768-8 ]
ENST00000513281 ; ENSP00000422343 ; ENSG00000143420 . [O43768-6 ]
GeneIDi 2029.
KEGGi hsa:2029.
UCSCi uc001evb.3. human. [O43768-7 ]
uc001evc.3. human. [O43768-5 ]
uc001evd.3. human. [O43768-3 ]
uc001eve.3. human. [O43768-1 ]
uc001evf.3. human. [O43768-6 ]
uc001evi.3. human. [O43768-8 ]

Organism-specific databases

CTDi 2029.
GeneCardsi GC01M150595.
HGNCi HGNC:3360. ENSA.
HPAi HPA051294.
MIMi 603061. gene.
neXtProti NX_O43768.
PharmGKBi PA27796.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG312450.
GeneTreei ENSGT00390000010139.
HOVERGENi HBG000297.
InParanoidi O43768.
PhylomeDBi O43768.
TreeFami TF314718.

Enzyme and pathway databases

Reactomei REACT_150182. MASTL Facilitates Mitotic Progression.

Miscellaneous databases

ChiTaRSi ENSA. human.
GeneWikii ENSA_(gene).
GenomeRNAii 2029.
NextBioi 8217.
PROi O43768.
SOURCEi Search...

Gene expression databases

Bgeei O43768.
CleanExi HS_ENSA.
ExpressionAtlasi O43768. baseline and differential.
Genevestigatori O43768.

Family and domain databases

InterProi IPR006760. Endosulphine.
[Graphical view ]
Pfami PF04667. Endosulfine. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human alpha-endosulfine, a possible regulator of sulfonylurea-sensitive K(ATP) channel: molecular cloning, expression and biological properties."
    Heron L., Virsolvy A., Peyrollier K., Gribble F.M., Le Cam A., Ashcroft F.M., Bataille D.
    Proc. Natl. Acad. Sci. U.S.A. 95:8387-8391(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION.
    Tissue: Brain.
  2. "Isolation, characterization, and chromosomal localization of the human ENSA gene that encodes alpha-endosulfine, a regulator of beta-cell K(ATP) channels."
    Heron L., Virsolvy A., Apiou F., Le Cam A., Bataille D.
    Diabetes 48:1873-1876(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "The transcribed endosulfine alpha gene is located within a type 2 diabetes-linked region on 1q: sequence and expression analysis in Pima Indians."
    Thameem F., Farook V.S., Yang X., Lee Y.-H., Permana P.A., Bogardus C., Prochazka M.
    Mol. Genet. Metab. 81:16-21(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 5; 7 AND 8), TISSUE SPECIFICITY.
  4. "Human alpha endosulfine gene."
    Zhang Q., Fu G., Wu J., Zhou J., Ye M., Shen Y., Kan L., He K., Gu B., Chen S., Mao M., Chen Z.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Cloning and molecular characterization of two isoforms of human endosulfine."
    Scott V.E.S., Roch J.-M., Davis-Taber R.A., Molinari E.J., Whiteaker K.L., Gopalakrishnan M., Idler K., Sullivan J.P.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  6. "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; 6 AND 9).
    Tissue: Placenta and Pulmonary artery.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Liver.
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  9. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: B-cell, Lung and Testis.
  12. "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-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Conformation-specific binding of alpha-synuclein to novel protein partners detected by phage display and NMR spectroscopy."
    Woods W.S., Boettcher J.M., Zhou D.H., Kloepper K.D., Hartman K.L., Ladror D.T., Qi Z., Rienstra C.M., George J.M.
    J. Biol. Chem. 282:34555-34567(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNCA.
  14. "Membrane-induced folding of the cAMP-regulated phosphoprotein endosulfine-alpha."
    Boettcher J.M., Hartman K.L., Ladror D.T., Qi Z., Woods W.S., George J.M., Rienstra C.M.
    Biochemistry 47:12357-12364(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNCA, PHOSPHORYLATION AT SER-109, MUTAGENESIS OF SER-109.
  15. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiENSA_HUMAN
AccessioniPrimary (citable) accession number: O43768
Secondary accession number(s): A8K1Z9
, E9PB69, Q5T5H2, Q68D48, Q6FHW0, Q6IAM4, Q6NUL2, Q6VUC6, Q6VUC7, Q6VUC8, Q6VUC9, Q6VUD0, Q6VUD1, Q9NRZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: June 1, 1998
Last modified: October 29, 2014
This is version 116 of the entry and version 1 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3