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Protein

Calcium-transporting ATPase type 2C member 2

Gene

ATP2C2

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

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium.By similarity

Catalytic activityi

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi332 – 3321Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi333 – 3331Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi335 – 3351Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi337 – 3371Calcium 2By similarity
Active sitei379 – 37914-aspartylphosphate intermediateBy similarity
Metal bindingi674 – 6741MagnesiumBy similarity
Metal bindingi678 – 6781MagnesiumBy similarity
Metal bindingi768 – 7681Calcium 2By similarity
Metal bindingi772 – 7721Calcium 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.3.8. 2681.
ReactomeiR-HSA-936837. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.2.9. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-transporting ATPase type 2C member 2 (EC:3.6.3.8)
Short name:
ATPase 2C2
Alternative name(s):
Secretory pathway Ca(2+)-ATPase 2
Gene namesi
Name:ATP2C2
Synonyms:KIAA0703, SPCA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:29103. ATP2C2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 106106CytoplasmicSequence analysisAdd
BLAST
Transmembranei107 – 12721Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini128 – 1292ExtracellularSequence analysis
Transmembranei130 – 15021Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini151 – 23181CytoplasmicSequence analysisAdd
BLAST
Transmembranei232 – 25221Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini253 – 29341ExtracellularSequence analysisAdd
BLAST
Transmembranei294 – 31421Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini315 – 33117CytoplasmicSequence analysisAdd
BLAST
Transmembranei332 – 35221Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini353 – 750398ExtracellularSequence analysisAdd
BLAST
Transmembranei751 – 77121Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini772 – 80433CytoplasmicSequence analysisAdd
BLAST
Transmembranei805 – 82521Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini826 – 83712ExtracellularSequence analysisAdd
BLAST
Transmembranei838 – 85518Helical; Name=8Sequence analysisAdd
BLAST
Topological domaini856 – 87419CytoplasmicSequence analysisAdd
BLAST
Transmembranei875 – 89521Helical; Name=9Sequence analysisAdd
BLAST
Topological domaini896 – 90510ExtracellularSequence analysis
Transmembranei906 – 92621Helical; Name=10Sequence analysisAdd
BLAST
Topological domaini927 – 94620CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162377204.

Polymorphism and mutation databases

BioMutaiATP2C2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 946946Calcium-transporting ATPase type 2C member 2PRO_0000046207Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei264 – 2641PhosphothreonineCombined sources
Modified residuei267 – 2671PhosphoserineCombined sources
Modified residuei268 – 2681PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75185.
PaxDbiO75185.
PRIDEiO75185.

PTM databases

iPTMnetiO75185.
PhosphoSiteiO75185.

Expressioni

Gene expression databases

BgeeiO75185.
CleanExiHS_ATP2C2.
ExpressionAtlasiO75185. baseline and differential.
GenevisibleiO75185. HS.

Organism-specific databases

HPAiHPA052262.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ORAI1Q96D3110EBI-2939806,EBI-2291476

Protein-protein interaction databases

IntActiO75185. 1 interaction.
STRINGi9606.ENSP00000262429.

Structurei

3D structure databases

ProteinModelPortaliO75185.
SMRiO75185. Positions 63-931.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi114 – 1196Poly-Leu

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0202. Eukaryota.
COG0474. LUCA.
HOGENOMiHOG000265621.
HOVERGENiHBG106478.
InParanoidiO75185.
KOiK01537.
OrthoDBiEOG7F7W81.
PhylomeDBiO75185.
TreeFamiTF354251.

Family and domain databases

Gene3Di1.20.1110.10. 3 hits.
InterProiIPR030334. ATP2C2.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006413. P-type_ATPase_IIA_PMR1.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF220. PTHR24093:SF220. 1 hit.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: O75185-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVEGRVSEFL KKLGFSGGGR QYQALEKDEE EALIDEQSEL KAIEKEKKVT
60 70 80 90 100
ALPPKEACKC QKEDLARAFC VDLHTGLSEF SVTQRRLAHG WNEFVADNSE
110 120 130 140 150
PVWKKYLDQF KNPLILLLLG SALVSVLTKE YEDAVSIATA VLVVVTVAFI
160 170 180 190 200
QEYRSEKSLE ELTKMVPPEC NCLREGKLQH LLARELVPGD VVSLSIGDRI
210 220 230 240 250
PADIRLTEVT DLLVDESSFT GEAEPCSKTD SPLTGGGDLT TLSNIVFMGT
260 270 280 290 300
LVQYGRGQGV VIGTGESSQF GEVFKMMQAE ETPKTPLQKS MDRLGKQLTL
310 320 330 340 350
FSFGIIGLIM LIGWSQGKQL LSMFTIGVSL AVAAIPEGLP IVVMVTLVLG
360 370 380 390 400
VLRMAKKRVI VKKLPIVETL GCCSVLCSDK TGTLTANEMT VTQLVTSDGL
410 420 430 440 450
RAEVSGVGYD GQGTVCLLPS KEVIKEFSNV SVGKLVEAGC VANNAVIRKN
460 470 480 490 500
AVMGQPTEGA LMALAMKMDL SDIKNSYIRK KEIPFSSEQK WMAVKCSLKT
510 520 530 540 550
EDQEDIYFMK GALEEVIRYC TMYNNGGIPL PLTPQQRSFC LQEEKRMGSL
560 570 580 590 600
GLRVLALASG PELGRLTFLG LVGIIDPPRV GVKEAVQVLS ESGVSVKMIT
610 620 630 640 650
GDALETALAI GRNIGLCNGK LQAMSGEEVD SVEKGELADR VGKVSVFFRT
660 670 680 690 700
SPKHKLKIIK ALQESGAIVA MTGDGVNDAV ALKSADIGIA MGQTGTDVSK
710 720 730 740 750
EAANMILVDD DFSAIMNAVE EGKGIFYNIK NFVRFQLSTS ISALSLITLS
760 770 780 790 800
TVFNLPSPLN AMQILWINII MDGPPAQSLG VEPVDKDAFR QPPRSVRDTI
810 820 830 840 850
LSRALILKIL MSAAIIISGT LFIFWKEMPE DRASTPRTTT MTFTCFVFFD
860 870 880 890 900
LFNALTCRSQ TKLIFEIGFL RNHMFLYSVL GSILGQLAVI YIPPLQRVFQ
910 920 930 940
TENLGALDLL FLTGLASSVF ILSELLKLCE KYCCSPKRVQ MHPEDV
Length:946
Mass (Da):103,187
Last modified:December 16, 2008 - v2
Checksum:iAEB061210ED09D1C
GO
Isoform 2 (identifier: O75185-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: MVEGRVSEFL...QKEDLARAFC → MLHFHLLKFK...SELVPDLSFQ

Show »
Length:963
Mass (Da):105,041
Checksum:iA82EA87032866F4D
GO
Isoform 3 (identifier: O75185-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     778-778: S → RSSQKTEVCCTAVRLGVEGRGESTWAGRAG

Note: No experimental confirmation available.Curated
Show »
Length:975
Mass (Da):106,235
Checksum:i4AD1288CAC4CD7A5
GO

Sequence cautioni

The sequence BAA31678.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711N → D in CAI46049 (PubMed:17974005).Curated
Sequence conflicti361 – 3611V → A in CAI46049 (PubMed:17974005).Curated
Sequence conflicti880 – 8801L → R in CAI46049 (PubMed:17974005).Curated
Isoform 2 (identifier: O75185-2)
Sequence conflicti12 – 121R → I in BAA31678 (PubMed:9734811).Curated
Isoform 3 (identifier: O75185-3)
Sequence conflicti789 – 7891A → G in CAI46049 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti165 – 1651M → L.2 Publications
Corresponds to variant rs247818 [ dbSNP | Ensembl ].
VAR_059137
Natural varianti411 – 4111G → S.
Corresponds to variant rs2303853 [ dbSNP | Ensembl ].
VAR_047935
Natural varianti466 – 4661M → L.1 Publication
Corresponds to variant rs247897 [ dbSNP | Ensembl ].
VAR_047936
Natural varianti604 – 6041L → Q.1 Publication
Corresponds to variant rs62640926 [ dbSNP | Ensembl ].
VAR_070929
Natural varianti907 – 9071L → P.
Corresponds to variant rs16973859 [ dbSNP | Ensembl ].
VAR_047937

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7070MVEGR…ARAFC → MLHFHLLKFKTRVVFSAVII MVTGLCLFLLSLPHLHGVFE QVPAPWWTSLCPWPIMEAAA FQSGSLYPVASFLAAPMSEL VPDLSFQ in isoform 2. 1 PublicationVSP_035989Add
BLAST
Alternative sequencei778 – 7781S → RSSQKTEVCCTAVRLGVEGR GESTWAGRAG in isoform 3. 1 PublicationVSP_054679

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY791884 mRNA. Translation: AAV54193.1.
AB014603 mRNA. Translation: BAA31678.2. Different initiation.
AK300526 mRNA. Translation: BAG62238.1.
BX648333 mRNA. Translation: CAI46049.1.
CR749829 mRNA. Translation: CAH18686.1.
AC010551 Genomic DNA. No translation available.
AC022165 Genomic DNA. No translation available.
CCDSiCCDS42207.1. [O75185-1]
CCDS67088.1. [O75185-3]
RefSeqiNP_001273456.2. NM_001286527.2.
NP_001278383.1. NM_001291454.1.
NP_055676.3. NM_014861.3.
UniGeneiHs.6168.

Genome annotation databases

EnsembliENST00000262429; ENSP00000262429; ENSG00000064270.
GeneIDi9914.
KEGGihsa:9914.
UCSCiuc002fhx.4. human. [O75185-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY791884 mRNA. Translation: AAV54193.1.
AB014603 mRNA. Translation: BAA31678.2. Different initiation.
AK300526 mRNA. Translation: BAG62238.1.
BX648333 mRNA. Translation: CAI46049.1.
CR749829 mRNA. Translation: CAH18686.1.
AC010551 Genomic DNA. No translation available.
AC022165 Genomic DNA. No translation available.
CCDSiCCDS42207.1. [O75185-1]
CCDS67088.1. [O75185-3]
RefSeqiNP_001273456.2. NM_001286527.2.
NP_001278383.1. NM_001291454.1.
NP_055676.3. NM_014861.3.
UniGeneiHs.6168.

3D structure databases

ProteinModelPortaliO75185.
SMRiO75185. Positions 63-931.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO75185. 1 interaction.
STRINGi9606.ENSP00000262429.

Protein family/group databases

TCDBi3.A.3.2.9. the p-type atpase (p-atpase) superfamily.

PTM databases

iPTMnetiO75185.
PhosphoSiteiO75185.

Polymorphism and mutation databases

BioMutaiATP2C2.

Proteomic databases

MaxQBiO75185.
PaxDbiO75185.
PRIDEiO75185.

Protocols and materials databases

DNASUi9914.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262429; ENSP00000262429; ENSG00000064270.
GeneIDi9914.
KEGGihsa:9914.
UCSCiuc002fhx.4. human. [O75185-1]

Organism-specific databases

CTDi9914.
GeneCardsiATP2C2.
H-InvDBHIX0013295.
HIX0013296.
HGNCiHGNC:29103. ATP2C2.
HPAiHPA052262.
MIMi613082. gene.
neXtProtiNX_O75185.
PharmGKBiPA162377204.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0202. Eukaryota.
COG0474. LUCA.
HOGENOMiHOG000265621.
HOVERGENiHBG106478.
InParanoidiO75185.
KOiK01537.
OrthoDBiEOG7F7W81.
PhylomeDBiO75185.
TreeFamiTF354251.

Enzyme and pathway databases

BRENDAi3.6.3.8. 2681.
ReactomeiR-HSA-936837. Ion transport by P-type ATPases.

Miscellaneous databases

ChiTaRSiATP2C2. human.
GenomeRNAii9914.
NextBioi35500152.
PROiO75185.
SOURCEiSearch...

Gene expression databases

BgeeiO75185.
CleanExiHS_ATP2C2.
ExpressionAtlasiO75185. baseline and differential.
GenevisibleiO75185. HS.

Family and domain databases

Gene3Di1.20.1110.10. 3 hits.
InterProiIPR030334. ATP2C2.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006413. P-type_ATPase_IIA_PMR1.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF220. PTHR24093:SF220. 1 hit.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The secretory pathway Ca2+/Mn2+-ATPase 2 is a Golgi-localized pump with high affinity for Ca2+ ions."
    Vanoevelen J., Dode L., Van Baelen K., Fairclough R.J., Missiaen L., Raeymaekers L., Wuytack F.
    J. Biol. Chem. 280:22800-22808(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "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] (ISOFORM 1), VARIANTS LEU-165 AND LEU-466.
    Tissue: Prostate.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANTS LEU-165 AND GLN-604.
    Tissue: Endometrium and Small intestine.
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-264; SER-267 AND SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiAT2C2_HUMAN
AccessioniPrimary (citable) accession number: O75185
Secondary accession number(s): B4DU76
, E7ES94, Q5HYC3, Q5S053, Q68CQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: December 16, 2008
Last modified: April 13, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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.