O43768 (ENSA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-endosulfine

Alternative name(s):
ARPP-19e

Gene names

Name:

ENSA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	121 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Protein phosphatase inhibitor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from sequence or structural similarity. Source: UniProtKB response to glucose stimulus Inferred from electronic annotation. Source: Compara response to nutrient Traceable author statement Ref.1. Source: ProtInc transport Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ion 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
MCM3	P25205	1	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.15
	Chain	2 – 121	120	Alpha-endosulfine		PRO_0000146758
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.15 Ref.17
	Modified residue	2	1	Phosphoserine Ref.12 Ref.15 Ref.17
	Modified residue	67	1	Phosphoserine; by GWL Probable
	Modified residue	109	1	Phosphoserine; by PKA Ref.14 Ref.15 Ref.17
Natural variations
	Alternative sequence	1 – 4	4	Missing in isoform 5, isoform 6 and isoform 7.		VSP_037063
	Alternative sequence	5 – 19	15	QEEEN…GEEKQ → MAGGLGCDVCYWFVE in isoform 5, isoform 6 and isoform 7.		VSP_037064
	Alternative sequence	61	1	G → GDYKSLHWSVLLCADEM in isoform 3, isoform 7 and isoform 9.		VSP_037065
	Alternative sequence	61	1	G → GVWGIASYPLSLGLKEVLRM KSVE in isoform 4.		VSP_037066
	Alternative sequence	62 – 121	60	QKYFD…GGQVE → VWGIVSYPLSLELKEVLRMK SVEVLLDPFLEVLLLNRSRG EFEI in isoform 8.		VSP_037067
	Alternative sequence	118 – 121	4	Missing in isoform 2, isoform 4, isoform 6 and isoform 9.		VSP_001443
Experimental info
	Mutagenesis	109	1	S → E: Mimicks a phosphorylated state and impairs interaction with SNCA. Ref.14
	Sequence conflict	5	1	Q → R in CAG38815. Ref.8
	Sequence conflict	21	1	T → M in BAF82753. Ref.6
	Sequence conflict	22	1	Q → L in AAH68544. Ref.11
	Sequence conflict	114	1	K → Q in CAG33411. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 7C76315AA17E7542	FASTA	121	13,389
	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
	Isoform 2 (Beta) [UniParc]. Checksum: D17E754219767472	FASTA	117	12,976
	10 20 30 40 50 60 MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK 70 80 90 100 110 GQKYFDSGDY NMAKAKMKNK QLPSAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAG
	Isoform 3 [UniParc]. Checksum: E9CF169C48A1FC1B	FASTA	137	15,281
	10 20 30 40 50 60 MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK 70 80 90 100 110 120 GDYKSLHWSV LLCADEMQKY FDSGDYNMAK AKMKNKQLPS AGPDKNLVTG DHIPTPQDLP 130 QRKSSLVTSK LAGGQVE
	Isoform 4 [UniParc]. Checksum: 2AB6570AFD91E54D	FASTA	140	15,534
	10 20 30 40 50 60 MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK 70 80 90 100 110 120 GVWGIASYPL SLGLKEVLRM KSVEQKYFDS GDYNMAKAKM KNKQLPSAGP DKNLVTGDHI 130 140 PTPQDLPQRK SSLVTSKLAG
	Isoform 5 [UniParc]. Checksum: EEE3B2739FD70FC2	FASTA	117	12,818
	10 20 30 40 50 60 MAGGLGCDVC YWFVEDTQEK EGILPERAEE AKLKAKYPSL GQKPGGSDFL MKRLQKGQKY 70 80 90 100 110 FDSGDYNMAK AKMKNKQLPS AGPDKNLVTG DHIPTPQDLP QRKSSLVTSK LAGGQVE
	Isoform 6 [UniParc]. Checksum: CFD70FC2E5FE760C	FASTA	113	12,404
	10 20 30 40 50 60 MAGGLGCDVC YWFVEDTQEK EGILPERAEE AKLKAKYPSL GQKPGGSDFL MKRLQKGQKY 70 80 90 100 110 FDSGDYNMAK AKMKNKQLPS AGPDKNLVTG DHIPTPQDLP QRKSSLVTSK LAG
	Isoform 7 [UniParc]. Checksum: 852736F0B466D4AB	FASTA	133	14,710
	10 20 30 40 50 60 MAGGLGCDVC YWFVEDTQEK EGILPERAEE AKLKAKYPSL GQKPGGSDFL MKRLQKGDYK 70 80 90 100 110 120 SLHWSVLLCA DEMQKYFDSG DYNMAKAKMK NKQLPSAGPD KNLVTGDHIP TPQDLPQRKS 130 SLVTSKLAGG QVE
	Isoform 8 [UniParc]. Checksum: E6306F60528ECCA4	FASTA	105	11,990
	10 20 30 40 50 60 MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK 70 80 90 100 GVWGIVSYPL SLELKEVLRM KSVEVLLDPF LEVLLLNRSR GEFEI
	Isoform 9 [UniParc]. Checksum: 28A1FC1BE09A3895	FASTA	133	14,868
	10 20 30 40 50 60 MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK 70 80 90 100 110 120 GDYKSLHWSV LLCADEMQKY FDSGDYNMAK AKMKNKQLPS AGPDKNLVTG DHIPTPQDLP 130 QRKSSLVTSK LAG

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. 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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00220797. IPI00383552. IPI00410178. IPI00410179. IPI00410180. IPI00410181. IPI00410387. IPI00644717. IPI00929648.
RefSeq	NP_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.
UniGene	Hs.632456.
3D structure databases
ProteinModelPortal	O43768.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43768. 5 interactions.
MINT	MINT-1431607.
PTM databases
PhosphoSite	O43768.
Proteomic databases
PaxDb	O43768.
PRIDE	O43768.
Protocols and materials databases
DNASU	2029.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000271690; ENSP00000271690; ENSG00000143420. ENST00000339643; ENSP00000341743; ENSG00000143420. ENST00000361532; ENSP00000354835; ENSG00000143420. ENST00000361631; ENSP00000355239; ENSG00000143420. ENST00000362052; ENSP00000355220; ENSG00000143420. ENST00000369014; ENSP00000358010; ENSG00000143420. ENST00000503241; ENSP00000424242; ENSG00000143420. ENST00000503345; ENSP00000421458; ENSG00000143420. ENST00000509582; ENSP00000426110; ENSG00000143420. ENST00000513281; ENSP00000422343; ENSG00000143420.
GeneID	2029.
KEGG	hsa:2029.
UCSC	uc001evb.3. human. uc001evc.3. human. uc001evd.3. human. uc001eve.3. human. uc001evf.3. human. uc001evi.3. human.
Organism-specific databases
CTD	2029.
GeneCards	GC01M150574.
HGNC	HGNC:3360. ENSA.
HPA	HPA051294.
MIM	603061. gene.
neXtProt	NX_O43768.
PharmGKB	PA27796.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG312450.
HOVERGEN	HBG000297.
OrthoDB	EOG4KSPM7.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	O43768.
Bgee	O43768.
CleanEx	HS_ENSA.
Genevestigator	O43768.
GermOnline	ENSG00000143420. Homo sapiens.
Family and domain databases
InterPro	IPR006760. Endosulphine. [Graphical view]
Pfam	PF04667. Endosulfine. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ENSA. human.
GenomeRNAi	2029.
NextBio	8217.
SOURCE	Search...

Entry information

Entry name

ENSA_HUMAN

Accession

Primary (citable) accession number: O43768
Secondary accession number(s): A8K1Z9 , 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 3, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.