Q9ULQ1 (TPC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Two pore calcium channel protein 1

Alternative name(s):
Voltage-dependent calcium channel protein TPC1

Gene names

Name:	TPCN1
Synonyms:	KIAA1169, TPC1

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	816 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Nicotinic acid adenine dinucleotide phosphate (NAADP) receptor that may function as one of the major voltage-gated Ca2+ channels (VDCC) across the lysosomal and endosomal membrane. Ref.7
Subunit structure	Dimer Potential.
Subcellular location	Lysosome membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein Ref.7.
Tissue specificity	Highest expression found in the heart and kidney, and lowest expression found in the spleen. Ref.2
Domain	Each of the two internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position By similarity.
Sequence similarities	Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. Two pore calcium channel subfamily. [View classification]
Sequence caution	The sequence AK057414 differs from that shown. Reason: Frameshift at position 273. The sequence BAA86483.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Endosome Lysosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Calcium channel Ion channel Voltage-gated channel
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	calcium ion transport Inferred from Biological aspect of Ancestor. Source: RefGenome ion transmembrane transport Inferred from Biological aspect of Ancestor. Source: RefGenome membrane depolarization during action potential Inferred from Biological aspect of Ancestor. Source: RefGenome transmembrane transport Traceable author statement. Source: Reactome
Cellular_component	endosome membrane Inferred from direct assay Ref.7. Source: UniProtKB integral component of membrane Inferred from electronic annotation. Source: UniProtKB-KW lysosomal membrane Inferred from direct assay Ref.7. Source: UniProtKB plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	NAADP-sensitive calcium-release channel activity Inferred from direct assay Ref.7. Source: UniProtKB identical protein binding Inferred from physical interaction PubMed 21903581. Source: IntAct protein binding Inferred from physical interaction PubMed 21903581PubMed 24188827. Source: IntAct voltage-gated calcium channel activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-5239895,EBI-5239895
HAX1	O00165	2	EBI-5239895,EBI-357001
TPCN2	Q8NHX9	9	EBI-5239895,EBI-5239949

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9ULQ1-1)

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: Q9ULQ1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-366: Missing.
     569-618: SLGLTLLIFY...WRNHTVGNRT → RYCQPPPWPA...PDGAPRSLES
     619-816: Missing.

Isoform 3 (identifier: Q9ULQ1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MESCYIAQAGLELLGSSSSPTLTSQSAEITEDASNGGVSEQHPWPSGFERELKPETISSPGYHILRATGEENM

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 816	816	Two pore calcium channel protein 1		PRO_0000276853
Regions
	Topological domain	1 – 112	112	Cytoplasmic Potential
	Transmembrane	113 – 133	21	Helical; Name=S1 of repeat I; Potential
	Topological domain	134	1	Extracellular Potential
	Transmembrane	135 – 155	21	Helical; Name=S2 of repeat I; Potential
	Topological domain	156 – 177	22	Cytoplasmic Potential
	Transmembrane	178 – 198	21	Helical; Name=S3 of repeat I; Potential
	Topological domain	199 – 200	2	Extracellular Potential
	Transmembrane	201 – 220	20	Helical; Name=S4 of repeat I; Potential
	Topological domain	221 – 234	14	Cytoplasmic Potential
	Transmembrane	235 – 255	21	Helical; Name=S5 of repeat I; Potential
	Topological domain	256 – 262	7	Extracellular Potential
	Intramembrane	263 – 286	24	Helical; Pore-forming; Potential
	Topological domain	287 – 294	8	Extracellular Potential
	Transmembrane	295 – 315	21	Helical; Name=S6 of repeat I; Potential
	Topological domain	316 – 444	129	Cytoplasmic Potential
	Transmembrane	445 – 465	21	Helical; Name=S1 of repeat II; Potential
	Topological domain	466 – 479	14	Extracellular Potential
	Transmembrane	480 – 500	21	Helical; Name=S2 of repeat II; Potential
	Topological domain	501 – 503	3	Cytoplasmic Potential
	Transmembrane	504 – 526	23	Helical; Name=S3 of repeat II; Potential
	Topological domain	527 – 534	8	Extracellular Potential
	Transmembrane	535 – 549	15	Helical; Name=S4 of repeat II; Potential
	Topological domain	550 – 573	24	Cytoplasmic Potential
	Transmembrane	574 – 594	21	Helical; Name=S5 of repeat II; Potential
	Topological domain	595 – 629	35	Extracellular Potential
	Intramembrane	630 – 653	24	Helical; Pore-forming; Potential
	Topological domain	654 – 670	17	Extracellular Potential
	Transmembrane	671 – 691	21	Helical; Name=S6 of repeat II; Potential
	Topological domain	692 – 816	125	Cytoplasmic Potential
	Coiled coil	769 – 796	28	Potential
Amino acid modifications
	Glycosylation	599	1	N-linked (GlcNAc...) Potential
	Glycosylation	611	1	N-linked (GlcNAc...) Potential
	Glycosylation	616	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 366	366	Missing in isoform 2.		VSP_023003
	Alternative sequence	1	1	M → MESCYIAQAGLELLGSSSSP TLTSQSAEITEDASNGGVSE QHPWPSGFERELKPETISSP GYHILRATGEENM in isoform 3.		VSP_041346
	Alternative sequence	569 – 618	50	SLGLT…VGNRT → RYCQPPPWPAGPGAVWQCPV GAGAEWQSGERSSTKDCNRG PDGAPRSLES in isoform 2.		VSP_023004
	Alternative sequence	619 – 816	198	Missing in isoform 2.		VSP_023005
Experimental info
	Mutagenesis	273	1	L → P: Loss of NAADP-mediated cytoplasmic calcium release. Ref.7
	Sequence conflict	621	1	E → G in AK057414. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 6, 2007. Version 3. Checksum: D6D26BFAF33E1463	FASTA	816	94,147
	10 20 30 40 50 60 MAVSLDDDVP LILTLDEGGS APLAPSNGLG QEELPSKNGG SYAIHDSQAP SLSSGGESSP 70 80 90 100 110 120 SSPAHNWEMN YQEAAIYLQE GENNDKFFTH PKDAKALAAY LFAHNHLFYL MELATALLLL 130 140 150 160 170 180 LLSLCEAPAV PALRLGIYVH ATLELFALMV VVFELCMKLR WLGLHTFIRH KRTMVKTSVL 190 200 210 220 230 240 VVQFVEAIVV LVRQMSHVRV TRALRCIFLV DCRYCGGVRR NLRQIFQSLP PFMDILLLLL 250 260 270 280 290 300 FFMIIFAILG FYLFSPNPSD PYFSTLENSI VSLFVLLTTA NFPDVMMPSY SRNPWSCVFF 310 320 330 340 350 360 IVYLSIELYF IMNLLLAVVF DTFNDIEKRK FKSLLLHKRT AIQHAYRLLI SQRRPAGISY 370 380 390 400 410 420 RQFEGLMRFY KPRMSARERY LTFKALNQNN TPLLSLKDFY DIYEVAALKW KAKKNREHWF 430 440 450 460 470 480 DELPRTALLI FKGINILVKS KAFQYFMYLV VAVNGVWILV ETFMLKGGNF FSKHVPWSYL 490 500 510 520 530 540 VFLTIYGVEL FLKVAGLGPV EYLSSGWNLF DFSVTVFAFL GLLALALNME PFYFIVVLRP 550 560 570 580 590 600 LQLLRLFKLK ERYRNVLDTM FELLPRMASL GLTLLIFYYS FAIVGMEFFC GIVFPNCCNT 610 620 630 640 650 660 STVADAYRWR NHTVGNRTVV EEGYYYLNNF DNILNSFVTL FELTVVNNWY IIMEGVTSQT 670 680 690 700 710 720 SHWSRLYFMT FYIVTMVVMT IIVAFILEAF VFRMNYSRKN QDSEVDGGIT LEKEISKEEL 730 740 750 760 770 780 VAVLELYREA RGASSDVTRL LETLSQMERY QQHSMVFLGR RSRTKSDLSL KMYQEEIQEW 790 800 810 YEEHAREQEQ QRQLSSSAAP AAQQPPGSRQ RSQTVT
	Isoform 2 [UniParc]. Checksum: BDD06287A468FA93	FASTA	252	29,136
	10 20 30 40 50 60 MRFYKPRMSA RERYLTFKAL NQNNTPLLSL KDFYDIYEVA ALKWKAKKNR EHWFDELPRT 70 80 90 100 110 120 ALLIFKGINI LVKSKAFQYF MYLVVAVNGV WILVETFMLK GGNFFSKHVP WSYLVFLTIY 130 140 150 160 170 180 GVELFLKVAG LGPVEYLSSG WNLFDFSVTV FAFLGLLALA LNMEPFYFIV VLRPLQLLRL 190 200 210 220 230 240 FKLKERYRNV LDTMFELLPR MARYCQPPPW PAGPGAVWQC PVGAGAEWQS GERSSTKDCN 250 RGPDGAPRSL ES
	Isoform 3 [UniParc]. Checksum: D3267C511D4C6BC4	FASTA	888	101,796
	10 20 30 40 50 60 MESCYIAQAG LELLGSSSSP TLTSQSAEIT EDASNGGVSE QHPWPSGFER ELKPETISSP 70 80 90 100 110 120 GYHILRATGE ENMAVSLDDD VPLILTLDEG GSAPLAPSNG LGQEELPSKN GGSYAIHDSQ 130 140 150 160 170 180 APSLSSGGES SPSSPAHNWE MNYQEAAIYL QEGENNDKFF THPKDAKALA AYLFAHNHLF 190 200 210 220 230 240 YLMELATALL LLLLSLCEAP AVPALRLGIY VHATLELFAL MVVVFELCMK LRWLGLHTFI 250 260 270 280 290 300 RHKRTMVKTS VLVVQFVEAI VVLVRQMSHV RVTRALRCIF LVDCRYCGGV RRNLRQIFQS 310 320 330 340 350 360 LPPFMDILLL LLFFMIIFAI LGFYLFSPNP SDPYFSTLEN SIVSLFVLLT TANFPDVMMP 370 380 390 400 410 420 SYSRNPWSCV FFIVYLSIEL YFIMNLLLAV VFDTFNDIEK RKFKSLLLHK RTAIQHAYRL 430 440 450 460 470 480 LISQRRPAGI SYRQFEGLMR FYKPRMSARE RYLTFKALNQ NNTPLLSLKD FYDIYEVAAL 490 500 510 520 530 540 KWKAKKNREH WFDELPRTAL LIFKGINILV KSKAFQYFMY LVVAVNGVWI LVETFMLKGG 550 560 570 580 590 600 NFFSKHVPWS YLVFLTIYGV ELFLKVAGLG PVEYLSSGWN LFDFSVTVFA FLGLLALALN 610 620 630 640 650 660 MEPFYFIVVL RPLQLLRLFK LKERYRNVLD TMFELLPRMA SLGLTLLIFY YSFAIVGMEF 670 680 690 700 710 720 FCGIVFPNCC NTSTVADAYR WRNHTVGNRT VVEEGYYYLN NFDNILNSFV TLFELTVVNN 730 740 750 760 770 780 WYIIMEGVTS QTSHWSRLYF MTFYIVTMVV MTIIVAFILE AFVFRMNYSR KNQDSEVDGG 790 800 810 820 830 840 ITLEKEISKE ELVAVLELYR EARGASSDVT RLLETLSQME RYQQHSMVFL GRRSRTKSDL 850 860 870 880 SLKMYQEEIQ EWYEEHAREQ EQQRQLSSSA APAAQQPPGS RQRSQTVT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"NAADP mobilizes calcium from acidic organelles through two-pore channels." Calcraft P.J., Ruas M., Pan Z., Cheng X., Arredouani A., Hao X., Tang J., Rietdorf K., Teboul L., Chuang K.T., Lin P., Xiao R., Wang C., Zhu Y., Lin Y., Wyatt C.N., Parrington J., Ma J. , Evans A.M., Galione A., Zhu M.X. Nature 459:596-600(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain." Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O. DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Brain.
[3]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Placenta.
[5]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[7]	"Essential requirement for two-pore channel 1 in NAADP-mediated calcium signaling." Brailoiu E., Churamani D., Cai X., Schrlau M.G., Brailoiu G.C., Gao X., Hooper R., Boulware M.J., Dun N.J., Marchant J.S., Patel S. J. Cell Biol. 186:201-209(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LEU-273, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY083666 mRNA. Translation: AAM01199.1. AB032995 mRNA. Translation: BAA86483.2. Different initiation. AK057414 mRNA. No translation available. AK075071 mRNA. Translation: BAC11385.1. AC010178 Genomic DNA. No translation available. AC089999 Genomic DNA. No translation available. AC127004 Genomic DNA. No translation available. BC136795 mRNA. Translation: AAI36796.1. BC136796 mRNA. Translation: AAI36797.1. BC150203 mRNA. Translation: AAI50204.1. BC152423 mRNA. Translation: AAI52424.1.
CCDS	CCDS31908.1. [Q9ULQ1-1] CCDS44985.1. [Q9ULQ1-3]
RefSeq	NP_001137291.1. NM_001143819.1. [Q9ULQ1-3] NP_060371.2. NM_017901.4. [Q9ULQ1-1]
UniGene	Hs.524763.
3D structure databases
ProteinModelPortal	Q9ULQ1.
SMR	Q9ULQ1. Positions 198-321, 434-689.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
IntAct	Q9ULQ1. 3 interactions.
STRING	9606.ENSP00000376350.
PTM databases
PhosphoSite	Q9ULQ1.
Polymorphism databases
DMDM	125991219.
Proteomic databases
MaxQB	Q9ULQ1.
PaxDb	Q9ULQ1.
PRIDE	Q9ULQ1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000335509; ENSP00000335300; ENSG00000186815. [Q9ULQ1-1] ENST00000541517; ENSP00000438125; ENSG00000186815. [Q9ULQ1-3] ENST00000550785; ENSP00000448083; ENSG00000186815. [Q9ULQ1-3]
GeneID	53373.
KEGG	hsa:53373.
UCSC	uc001tuw.3. human. [Q9ULQ1-1] uc001tux.3. human. [Q9ULQ1-3]
Organism-specific databases
CTD	53373.
GeneCards	GC12P113660.
HGNC	HGNC:18182. TPCN1.
HPA	HPA039757.
MIM	609666. gene.
neXtProt	NX_Q9ULQ1.
PharmGKB	PA134922711.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG280094.
HOGENOM	HOG000006773.
HOVERGEN	HBG080605.
InParanoid	Q9ULQ1.
KO	K16896.
OMA	WLGFHTF.
OrthoDB	EOG7W41B7.
PhylomeDB	Q9ULQ1.
TreeFam	TF328550.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	Q9ULQ1.
Bgee	Q9ULQ1.
CleanEx	HS_TPCN1.
Genevestigator	Q9ULQ1.
Family and domain databases
Gene3D	1.20.120.350. 1 hit.
InterPro	IPR027359. Channel_four-helix_dom. IPR005821. Ion_trans_dom. IPR028801. TPC1. [Graphical view]
PANTHER	PTHR10037:SF201. PTHR10037:SF201. 1 hit.
Pfam	PF00520. Ion_trans. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TPCN1. human.
GeneWiki	TPCN1.
GenomeRNAi	53373.
NextBio	56034.
PRO	Q9ULQ1.
SOURCE	Search...

Entry information

Entry name

TPC1_HUMAN

Accession

Primary (citable) accession number: Q9ULQ1
Secondary accession number(s): A7E258, Q86XS9, Q8NC20

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 6, 2007
Last sequence update:	February 6, 2007
Last modified:	July 9, 2014
This is version 103 of the entry and version 3 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.