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O43768 (ENSA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-endosulfine
Alternative name(s):
ARPP-19e
Gene names
Name:ENSA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length121 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

Interacts (when phosphorylated at Ser-67) with PPP2R2D By similarity. Interacts with ABCC8. Interacts with SNCA; interaction is disrupted when phosphorylated at Ser-109. Ref.13 Ref.14

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Widely expressed with high levels in skeletal muscle and brain and lower levels in the pancreas. Ref.1 Ref.3

Post-translational modification

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. Ref.1 Ref.14

Sequence similarities

Belongs to the endosulfine family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionProtein phosphatase inhibitor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of catalytic activity

Inferred from sequence or structural similarity. Source: GOC

regulation of catalytic activity

Inferred from sequence or structural similarity. Source: GOC

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Traceable author statement Ref.1. Source: ProtInc

transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionion channel inhibitor activity

Traceable author statement Ref.1. Source: ProtInc

phosphatase inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphatase 2A binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphatase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein phosphatase type 2A regulator activity

Inferred from sequence or structural similarity. Source: UniProtKB

receptor binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MCM3P252051EBI-714511,EBI-355153

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43768-1)

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.
Isoform 2 (identifier: O43768-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     118-121: Missing.
Isoform 3 (identifier: O43768-3)

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: G → GDYKSLHWSVLLCADEM
Isoform 4 (identifier: O43768-4)

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: G → GVWGIASYPLSLGLKEVLRMKSVE
     118-121: Missing.
Isoform 5 (identifier: O43768-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: Missing.
     5-19: QEEENPAEETGEEKQ → MAGGLGCDVCYWFVE
Isoform 6 (identifier: O43768-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: Missing.
     5-19: QEEENPAEETGEEKQ → MAGGLGCDVCYWFVE
     118-121: Missing.
Isoform 7 (identifier: O43768-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: Missing.
     5-19: QEEENPAEETGEEKQ → MAGGLGCDVCYWFVE
     61-61: G → GDYKSLHWSVLLCADEM
Isoform 8 (identifier: O43768-8)

The sequence of this isoform differs from the canonical sequence as follows:
     62-121: QKYFDSGDYN...TSKLAGGQVE → VWGIVSYPLS...LNRSRGEFEI
Isoform 9 (identifier: O43768-9)

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: G → GDYKSLHWSVLLCADEM
     118-121: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 121120Alpha-endosulfine
PRO_0000146758

Amino acid modifications

Modified residue21N-acetylserine Ref.15 Ref.17
Modified residue21Phosphoserine Ref.12 Ref.15 Ref.17
Modified residue671Phosphoserine; by GWL Probable
Modified residue1091Phosphoserine; by PKA Ref.14 Ref.15 Ref.17

Natural variations

Alternative sequence1 – 44Missing in isoform 5, isoform 6 and isoform 7.
VSP_037063
Alternative sequence5 – 1915QEEEN…GEEKQ → MAGGLGCDVCYWFVE in isoform 5, isoform 6 and isoform 7.
VSP_037064
Alternative sequence611G → GDYKSLHWSVLLCADEM in isoform 3, isoform 7 and isoform 9.
VSP_037065
Alternative sequence611G → GVWGIASYPLSLGLKEVLRM KSVE in isoform 4.
VSP_037066
Alternative sequence62 – 12160QKYFD…GGQVE → VWGIVSYPLSLELKEVLRMK SVEVLLDPFLEVLLLNRSRG EFEI in isoform 8.
VSP_037067
Alternative sequence118 – 1214Missing in isoform 2, isoform 4, isoform 6 and isoform 9.
VSP_001443

Experimental info

Mutagenesis1091S → E: Mimicks a phosphorylated state and impairs interaction with SNCA. Ref.14
Sequence conflict51Q → R in CAG38815. Ref.8
Sequence conflict211T → M in BAF82753. Ref.6
Sequence conflict221Q → L in AAH68544. Ref.11
Sequence conflict1141K → Q in CAG33411. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 7C76315AA17E7542

FASTA12113,389
        10         20         30         40         50         60 
MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK 

        70         80         90        100        110        120 
GQKYFDSGDY NMAKAKMKNK QLPSAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV 


E 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: D17E754219767472
Show »

FASTA11712,976
Isoform 3 [UniParc].

Checksum: E9CF169C48A1FC1B
Show »

FASTA13715,281
Isoform 4 [UniParc].

Checksum: 2AB6570AFD91E54D
Show »

FASTA14015,534
Isoform 5 [UniParc].

Checksum: EEE3B2739FD70FC2
Show »

FASTA11712,818
Isoform 6 [UniParc].

Checksum: CFD70FC2E5FE760C
Show »

FASTA11312,404
Isoform 7 [UniParc].

Checksum: 852736F0B466D4AB
Show »

FASTA13314,710
Isoform 8 [UniParc].

Checksum: E6306F60528ECCA4
Show »

FASTA10511,990
Isoform 9 [UniParc].

Checksum: 28A1FC1BE09A3895
Show »

FASTA13314,868

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99906 mRNA. Translation: CAA68180.1.
AJ010966 Genomic DNA. Translation: CAB65125.1.
AY326403 expand/collapse EMBL AC list , AY326400, AY326401, AY326402 Genomic DNA. Translation: AAQ73827.1.
AY326403 expand/collapse EMBL AC list , AY326400, AY326401, AY326402 Genomic DNA. Translation: AAQ73828.1.
AY326402, AY326400, AY326401 Genomic DNA. Translation: AAQ73829.1.
AY326401, AY326400 Genomic DNA. Translation: AAQ73830.1.
AY326403 expand/collapse EMBL AC list , AY326400, AY326401, AY326402 Genomic DNA. Translation: AAQ73831.1.
AY326403 expand/collapse EMBL AC list , 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.
RefSeqNP_004427.1. NM_004436.2.
NP_996925.1. NM_207042.1.
NP_996926.1. NM_207043.1.
NP_996927.1. NM_207044.1.
NP_996928.1. NM_207045.1.
NP_996929.1. NM_207046.1.
NP_996930.1. NM_207047.1.
NP_997051.1. NM_207168.1.
UniGeneHs.632456.

3D structure databases

ProteinModelPortalO43768.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108343. 10 interactions.
IntActO43768. 5 interactions.
MINTMINT-1431607.

PTM databases

PhosphoSiteO43768.

Proteomic databases

PaxDbO43768.
PRIDEO43768.

Protocols and materials databases

DNASU2029.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000271690; 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]
GeneID2029.
KEGGhsa:2029.
UCSCuc001evb.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

CTD2029.
GeneCardsGC01M150577.
HGNCHGNC:3360. ENSA.
HPAHPA051294.
MIM603061. gene.
neXtProtNX_O43768.
PharmGKBPA27796.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG312450.
HOVERGENHBG000297.
PhylomeDBO43768.
TreeFamTF314718.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressO43768.
BgeeO43768.
CleanExHS_ENSA.
GenevestigatorO43768.

Family and domain databases

InterProIPR006760. Endosulphine.
[Graphical view]
PfamPF04667. Endosulfine. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSENSA. human.
GeneWikiENSA_(gene).
GenomeRNAi2029.
NextBio8217.
PROO43768.
SOURCESearch...

Entry information

Entry nameENSA_HUMAN
AccessionPrimary (citable) accession number: O43768
Secondary accession number(s): A8K1Z9 expand/collapse secondary AC list , E9PB69, Q5T5H2, Q68D48, Q6FHW0, Q6IAM4, Q6NUL2, Q6VUC6, Q6VUC7, Q6VUC8, Q6VUC9, Q6VUD0, Q6VUD1, Q9NRZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM