wanglab/gogpt-training-data huggingface dataset:
Protein: Long-chain fatty acid transport protein 5 (FATP-5) (Fatty acid transport protein 5) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Bile acyl-CoA synthetase) (BACS) (EC 6.2.1.7) (Cholate--CoA ligase) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR) (EC 6.2.1.-) (Q9ES38)
Organism: Rattus norvegicus (Rat)
Function: Mediates the import of long-chain fatty acids (LCFA) by facilitating their transport across cell membranes (By similarity). Also catalyzes the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (By similarity). Mainly functions as a bile acyl-CoA synthetase catalyzing the activation of bile acids via formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine. In particular, catalyzes the activation of the primary bile acid, chenodeoxycholic acid. Primary bile acid cholic acid and secondary bile acids (deoxycholic acid and lithocholic acid) are principal substrates too (By similarity). In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate ((25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate or THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol (By similarity). Plays an important role in hepatic fatty acid uptake and bile acid reconjugation and recycling but not in de novo synthesis of bile acids (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y2P5}; Multi-pass membrane protein {ECO:0000255}. Microsome {ECO:0000269|PubMed:12951368}. Cell membrane {ECO:0000250|UniProtKB:Q4LDG0}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Bile acid-CoA:amino acid N-acyltransferase
- Acyl-coenzyme A amino acid N-acyltransferase 1
- Sterol 26-hydroxylase, mitochondrial
- Acyl-coenzyme A amino acid N-acyltransferase 2
- Acyl-coenzyme A thioesterase 8
- Bile salt export pump
- Hepatic sodium/bile acid cotransporter
- Peroxisomal acyl-coenzyme A oxidase 2
- Solute carrier organic anion transporter family member 1B2
- Histidine-rich glycoprotein
Sequence:
MGVWKKLTFLLLSLLLLVGLGQPLWPAATALALRWFLGDPTCFVLLGLAFLGRPWISSWIPHWLSLAAAALTLSLLPPRPPPELRWLHKDVAFAFKLLFYGLNLRRRLNRHPPELFVDALEQQAQARPDQVALVCTGSEGCSITNRELNAKACQAAWALKAKLKEATIQEDKGATAILVLPSKSISALSVFLGLAKLGCPVAWINPHSRGMPLLHSVQSSGASVLIVDPDLQENLEEVLPKLLAENIRCFYLGHSSPTPGVEALGAALDAAPSDPVPAKLRANIKWKSPAIFIYTSGTTGLPKPAILSHERVIQMSNVLSFCGRTADDVVYNVLPLYHSMGLVLGVLGCLQLGATCVLAPKFSASRYWAECRQYSVTVVLYVGEVLRYLCNVPGQPEDKKHTVRFALGNGLRADVWENFQQRFGPIQIWELYGSTEGNVGLMNYVGHCGAVGKTSCFIRMLTPLELVQFDIETAEPVRDKQGFCIPVETGKPGLLLTKIRKNQPFLGYRGSQDETKRKLVANVRQVGDLYYNTGDVLALDQEGFFYFRDRLGDTFRWKGENVSTREVEGVLSILDFLEEVNVYGVTVPGCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSQLAREGFDVGVIADPLYILDNKAETFRSLMPDVYQAVCEGTWKL
Protein: PHD finger protein ALFIN-LIKE 6 (Protein AL6) (Q8S8M9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:19154204}.
Interaction partners:
- PHD finger family protein / SWIB complex BAF60b domain-containing protein / GYF domain-containing protein
- Histone H3.3
- Histone H3-like 1
- Histone H3-like centromeric protein CENH3
- Histone H3-like 4
- Histone H3.1
- Putative E3 ubiquitin-protein ligase RING1a
- Histone H3-like 2
- Histone H3-like 5
- Histone H3-like 3
Sequence:
MEGITHPIPRTVEEVFSDFRGRRAGLIKALTNDMVKFYQTCDPEKENLCLYGLPNETWEVNLPVEEVPPELPEPALGINFARDGMQEKDWVSLVAVHSDSWLLSVAFYFGARFGFGKNERKRLFQMINELPTIFEVVSGNAKQSKDLSVNNNNSKSKPSGVKSRQSESLSKVAKMSSPPPKEEEEEEDESEDESEDDEQGAVCGACGDNYGTDEFWICCDACEKWFHGKCVKITPAKAEHIKHYKCPTCSNKRARP
Protein: ACT domain-containing protein ACR11 (Protein ACT DOMAIN REPEATS 11) (Q9FZ47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in feedback regulation of amino acid metabolism. May be involved in the regulation of glutamine metabolism.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21861936}.
Interaction partners:
- ACT domain-containing protein ACR10
- ACT domain-containing protein ACR9
- ACT domain-containing protein ACR8
- Uncharacterized protein At4g15545
- ACT domain-containing protein ACR7
- Aspartokinase 2, chloroplastic
- Small ribosomal subunit protein mS29
- Phosphoglycerate mutase-like protein 1
- Aspartokinase 1, chloroplastic
- Aspartokinase 3, chloroplastic
Sequence:
MAMASASGSALCFTDASSSLALRRDCGALCLPPRTVTFGFVDKPLVNLERLRLSTLKIRASNATAVENGKQEGSAADSDKVPTPVVIIDQDSDPDATVLEVTFGDRLGALLDTMNALKNLGLNVVKANVYLDSSGKHNKFAITRADSGRKVEDPELLEAIRLTVINNLLEFHPESSSQLAMGAAFGVLPPTEPIDVDIATHITIEDDGPDRSLLFIESADRPGLLVELVKIISDISVAVESGEFDTEGLLAKVKFHVSYRNKALIKPLQQVLANSLRYFLRRPSTDESSF
Protein: Cyclin dependent kinase 14 (C9IYJ9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSTRNCQGMDSVIKPLDTIPEDKKVRVQRTQSTFDPFEKPANQVKRVHSENNACINFKTSSTGKESPKVRRHSSPSSPTSPKFGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEG
Protein: Uncharacterized protein (Q38C69)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWRCSTLLHKGSLTALLRDVIRCTQPCGIPLGDVEIKAKEHFLSLSNGEQEEFPLALKKALLEANDAHYIDGAKLYPCNWERVVQSIAVEMPCEGLTEKGLVDRILEFEPRFNMESASLGEPLSEWMARRFPHIILVSRSASTGVPVYRPVRGKLPEEVECIANALQLLGREKLPVYTDFALIAPLLPATVCPTRGNWVAFLERGSVQCHFDLDVDVHIRLSPNSIPSTVCVDGTTVELARVNEVLAANGLSDSTCSLKVFRRAEDPVWSQDDIVLPSFLEPEHAIGAAIASLGARSCMRIYILCGDSAVERYKTGLLDLLRSAETDVRIFTPCNAGFTDGAISSGVDRREKTVGKS
Protein: Transcriptional regulator CRZ1 (Calcineurin-responsive zinc finger protein 1) (Q5A4H5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor involved in the regulation of calcium ion homeostasis and required for the maintenance of membrane integrity. Binds to the calcineurin-dependent response element. Plays a role in azole tolerance.
Subcellular location: Cytoplasm. Nucleus. Note=Localizes in the nucleus in a calcium- and calcineurin-dependent manner.
Interaction partners:
- Calcineurin subunit B
- Calmodulin
- Calcium-transporting ATPase
- Mlc2p
- Calcium-channel protein CCH1
- pH-response transcription factor pacC/RIM101
- Mitogen-activated protein kinase MKC1
- Heat shock protein 90 homolog
- Rlm1p
- Vacuolar calcium ion transporter
Sequence:
MSNNPHPQDDGSQLYDNFEISPPSIVIRKADTDQSLNKIMLNQESQDINNYYTENVKNDNNPNNSYQDYTFSGNSSNQQHQQQQQQHLYEDLPTQFHYSNNSFFEPPPAPTVELTDDPLPNFNYPPSNIYINDNASDISLNTKDLPQFTTNEFLSPTSQLSTPFSPGHYSQSSQDFLQVNHTNGSGNNNNNNNNNNLLNPRSPSQYSSHSLYSDNSSQPASPFLDAASHVSNNSFIPPVIPTALSDVGSQNLDPSHNLGLSANQHFDSVNEFLSTGEIQLGQSVSSTNLPSMEEDSIKWGGGNGQEAYTSLAMMEQRASADNSGMRLATHQFSETQIKQEDQQTNMNHQYTFSNPQMNFDFDITVTPPPQQLEVKPFGNDKDMNNSSGTTNNNNNNSQFDIVSTAATNNSNQLLTENNLSNYNQLQRTEQGNDNDSLQIHRDATGIIISINQAPEEIAAKTPSLFSNSSANSSIHNSPRSDIDNKSGQYYNNGGDGNSLVPNSQLLPSSPNSNNDNYGGGGSSNDENNLLNPEEFQSVKRGRRKSHASRTSTNPNSLSPRSRSRSRSSAKSSNDAVISDNDESDDVLQSREKMLELALPSSSSKRTQKHPSLYACHLCDKRFTRPYNLKSHIRTHTQEKPFICSKCGKSFARSHDKKRHELLHQGIKNFKCEGYLQDGTRWGCGKSFARADALRRHFQTEAGKQCVKRLLLEEQANSSGKPLATSSGVEIT
Protein: IME2-dependent-signaling protein (P46958)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Seems to act indirectly to modify IME2 activity, thus permitting IME2 to carry out later meiotic functions.
Interaction partners:
- Inactive deaminase YJL070C
Sequence:
MDNQQESISEDITGDLAAAVRKSWSESQDNPLLLNFNNSPIGTPTDRYSPEPATMMEGNAMNLSSLARGSTQQQQRLYGSSQTREKSDQQQQDYQLFKHHYSLGQETRESVSDILNDLTLGSPEPSERASPIRQPSVDVPPLTTRRSSIQDVQWIRHLLNPRSSFSGASSNEPTNSPGDFLNQSRAWITILHDSSAESLQAVIVLAESLKNVNSQYNLWVLHSSEVNAFQLAQVGIKTLIIDEYINLFMNFGTGSGFSASSQSTETKGELNFKWCKLFLFFSLIDRFELICYLSPTCLVLQNIDELLESTEVSDEIDNETCVLLSNKVNYINEDLVSVNQDQSSAENYDDDPQIIILKPNRAVAMCIKEYFTIYGNDFEGESKRSMFHQMNDLQIMKALFGDKWSYIDSVGYCAVPIASVPANRLNYKIIEFKILKPWERQNYIAAGQHRESIMNKWLDLWRDFLNQAN
Protein: Immunoglobulin heavy constant alpha 1 (Ig alpha-1 chain C region) (Ig alpha-1 chain C region BUR) (Ig alpha-1 chain C region TRO) (P01876)
Organism: Homo sapiens (Human)
Function: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen. Ig alpha is the major immunoglobulin class in body secretions.
Subcellular location: [Isoform 1]: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
ASPTSPKVFPLSLCSTQPDGNVVIACLVQGFFPQEPLSVTWSESGQGVTARNFPPSQDASGDLYTTSSQLTLPATQCLAGKSVTCHVKHYTNPSQDVTVPCPVPSTPPTPSPSTPPTPSPSCCHPRLSLHRPALEDLLLGSEANLTCTLTGLRDASGVTFTWTPSSGKSAVQGPPERDLCGCYSVSSVLPGCAEPWNHGKTFTCTAAYPESKTPLTATLSKSGNTFRPEVHLLPPPSEELALNELVTLTCLARGFSPKDVLVRWLQGSQELPREKYLTWASRQEPSQGTTTFAVTSILRVAAEDWKKGDTFSCMVGHEALPLAFTQKTIDRLADWQMPPPYVVLDLPQETLEEETPGANLWPTTITFLTLFLLSLFYSTALTVTSVRGPSGNREGPQY
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8T0Q5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCTVIGSGTFSTVLLGTLQRERGLVETQRRRFAIKHHNPTNHPERILRELECMYRIGGVENVIGINCCIRYNDNVAFIMPYMTHDRFHDIYRSLNFPEIRDYLRNLLIALRHVHKFNVIHRDVKPSNILYNRRTGKFLLCDFGLAQRIADDGSVVQSSDLSSREVFSILRDLENGRSVTLTDGNSAQAEAEDYMARRRMRALGGGGSVERAVTGPPSIQKLREQAGGHLTKKDVANQRADTMRLLNRLRLVSPNADPNNYVVSTNTSKKEMHASRAGTPGYRPPEVLLRYPKQSTAVDVWAAGVIMLSLLSGLHPFFKAPHDCGALAEIINLFGDMPVRKTAFLLDRLILLAQKVNTLDLRRVCMRFRHADFFLAPEIQRKYQRPDGTTEMCRSCEQPTFNCLCSNSGHNLERYDGLDIFPAVAYDLLSRLLEVNPQKRITAEEALKHPFFSDQHRITPGIPLHQQQLIMHQQQHIMQHQQHLQRSRETLPSSAARTLKAFVCYPMEITSTASQAAGNI
Protein: HAUS augmin-like complex subunit 3 (Q68CZ6)
Organism: Homo sapiens (Human)
Function: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:19427217}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
Interaction partners:
- HAUS augmin-like complex subunit 4
- HAUS augmin-like complex subunit 1
- HAUS augmin-like complex subunit 5
- HAUS augmin-like complex subunit 6
- HAUS augmin-like complex subunit 8
- HAUS augmin-like complex subunit 2
- HAUS augmin-like complex subunit 7
- Protein NEDD1
- Tubulin gamma-1 chain
- Nuclear mitotic apparatus protein 1
Sequence:
MSCGNEFVETLKKIGYPKADNLNGEDFDWLFEGVEDESFLKWFCGNVNEQNVLSERELEAFSILQKSGKPILEGAALDEALKTCKTSDLKTPRLDDKELEKLEDEVQTLLKLKNLKIQRRNKCQLMASVTSHKSLRLNAKEEEATKKLKQSQGILNAMITKISNELQALTDEVTQLMMFFRHSNLGQGTNPLVFLSQFSLEKYLSQEEQSTAALTLYTKKQFFQGIHEVVESSNEDNFQLLDIQTPSICDNQEILEERRLEMARLQLAYICAQHQLIHLKASNSSMKSSIKWAEESLHSLTSKAVDKENLDAKISSLTSEIMKLEKEVTQIKDRSLPAVVRENAQLLNMPVVKGDFDLQIAKQDYYTARQELVLNQLIKQKASFELLQLSYEIELRKHRDIYRQLENLVQELSQSNMMLYKQLEMLTDPSVSQQINPRNTIDTKDYSTHRLYQVLEGENKKKELFLTHGNLEEVAEKLKQNISLVQDQLAVSAQEHSFFLSKRNKDVDMLCDTLYQGGNQLLLSDQELTEQFHKVESQLNKLNHLLTDILADVKTKRKTLANNKLHQMEREFYVYFLKDEDYLKDIVENLETQSKIKAVSLED
Protein: Large ribosomal subunit protein P1A (60S acidic ribosomal protein P1-A) (CaRP1A) (Q9HFQ7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Plays an important role in the elongation step of protein synthesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P05318}.
Interaction partners:
- Large ribosomal subunit protein uL15
- 60S acidic ribosomal protein P0
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein uS2
Sequence:
MSTESALSYAALILADAEVEITSEKLLALVTKANVEVEGIWADLFAKALEGKDLKEFFFNFSAAPAAAAAGGAAGGGAAAEEAAEEEKEEEAKEESDDDMGFGLFD
Protein: Tryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (TrpRS) (Q09692)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Tryptophan--tRNA ligase, mitochondrial
- Serine--tRNA ligase, cytoplasmic
- Probable arginine--tRNA ligase, cytoplasmic
- Putative leucine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, mitochondrial
- Probable methionine--tRNA ligase, cytoplasmic
- Putative leucine--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, cytoplasmic
- Probable cysteine--tRNA ligase
- Lysine--tRNA ligase, cytoplasmic
Sequence:
MSVEEQIVTPWDVKGSIVDGEEKGIDYERLIVQFGTRKITPEQLERFEKLTGKKPHLLLRRGAFFSHRDFDMILDRYEQKKPFYLYTGRGPSSDSMHLGHMIPFMFCKWLQDVFQVPLVIQLTDDEKFLFKQGVSLEDCQRFARENAKDIIAVGFDPKKTFIFMNSTYVGGAFYQNVVRIAKCITANQSKACFGFTDSDSIGKIHFASIQAAPSFSSSFPHIFNGAKDIPCLIPCAIDQDPYFRLTRDVSGRLKFKKPALLHSRFFPALQGPQSKMSASKDSSAIFMTDTPNKIKNKINRHAFSGGGATIEIHREKGGNPDVDVAYQYLSFFLDDDEKLKQLYNTYKAGTLSTGEMKGECIKLLQQFVSDFQAARSKVDEATLDMFMDGSRKLEW
Protein: Alport syndrome mental retardation midface hypoplasia and elliptocytosis chromosomal region protein 1 isoform 1 (A0A0S2Z4V0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAGCCGVKKQKLSSSPPSGSGGGGGASSSSHCSGESQCRAGELGLGGAGTRLNGLGGLTGGGSGSGCTLSPPQGCGGGGGGIALSPPPSCGVGTLLSTPAAATSSSPSSSSAASSSSPGSRKMVVSAEMCCFCFDVLYCHLYGYQQPRTPRFTNEPYALKDSRFPPMTRDELPRLFCSVSLLTNFEDVCDYLDWEVGVHGIRIEFINEKGSKRTATYLPEVAKEQGWDHIQTIDSLLRKGGYKAPITNEFRKTIKLTRYRSEKMTLSYAEYLAHRQHHHFQNGIGHPLPPYNHYS
Protein: Deoxyribose-phosphate aldolase (DERA) (EC 4.1.2.4) (2-deoxy-D-ribose 5-phosphate aldolase) (Phosphodeoxyriboaldolase) (Deoxyriboaldolase) (Q9Y315)
Organism: Homo sapiens (Human)
Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. Participates in stress granule (SG) assembly. May allow ATP production from extracellular deoxyinosine in conditions of energy deprivation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25229427}. Cytoplasmic granule {ECO:0000269|PubMed:25229427}. Nucleus {ECO:0000269|PubMed:25229427}. Note=Recruited to stress granules but not to processing bodies upon arsenite or clotrimazole treatment or energy deprivation. {ECO:0000269|PubMed:25229427}.
Interaction partners:
- Phosphopentomutase
- Ribokinase
- Thymidine phosphorylase
- Aldehyde dehydrogenase family 16 member A1
- Transketolase
- Transketolase-like protein 2
- Transaldolase
- Transketolase-like protein 1
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase A
Sequence:
MSAHNRGTELDLSWISKIQVNHPAVLRRAEQIQARRTVKKEWQAAWLLKAVTFIDLTTLSGDDTSSNIQRLCYKAKYPIREDLLKALNMHDKGITTAAVCVYPARVCDAVKALKAAGCNIPVASVAAGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEIRQFRKACGEAHLKTILATGELGTLTNVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIRDFFWKTGNKIGFKPAGGIRSAKDSLAWLSLVKEELGDEWLKPELFRIGASTLLSDIERQIYHHVTGRYAAYHDLPMS
Protein: Bcl-2-like protein 10 (Bcl2-L-10) (Anti-apoptotic protein Boo) (Apoptosis regulator Bcl-B) (Q99M66)
Organism: Rattus norvegicus (Rat)
Function: Promotes cell survival by suppressing apoptosis induced by BAX but not BAK (By similarity). Increases binding of AHCYL1/IRBIT to ITPR1 (By similarity). Reduces ITPR1-mediated calcium release from the endoplasmic reticulum cooperatively with AHCYL1/IRBIT under normal cellular conditions (By similarity). Under apoptotic stress conditions, dissociates from ITPR1 and is displaced from mitochondria-associated endoplasmic reticulum membranes, leading to increased Ca(2+) transfer to mitochondria which promotes apoptosis (By similarity). Required for the correct formation of the microtubule organizing center during oocyte cell division, potentially via regulation of protein abundance and localization of other microtubule organizing center components such as AURKA and TPX2 (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9HD36}. Nucleus membrane {ECO:0000250|UniProtKB:Q9HD36}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9HD36}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9Z0F3}. Note=Localizes to mitochondria-associated endoplasmic reticulum membranes (MAMs) (By similarity). Localization to MAMs is greatly reduced under apoptotic stress conditions (By similarity). {ECO:0000250|UniProtKB:Q9HD36}.
Interaction partners:
- Bcl-2-like protein 11
- Bcl2-interacting killer, isoform CRA_a.
- Bcl2-associated agonist of cell death
Sequence:
MGDPLQDRTRRLLTDYILFCARAPNTPEPLPTSVEAALLRSVTSQIQQEHQDLFNSFRDYQGNRLELVTQMADELLSNDQEFNWGRLVMLLAFVGTLMNQDRTVKRRRDQRNRLLLERDCYLIVSLLYNRLTGRHRSWLEAHGGWDGFCQFFKNPLPPGFWRRLLIRAILSCFFATAIFYIWKCL
Protein: Low-density lipoprotein receptor-related protein (A1Z9D7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Frizzled
- Axin
- Segment polarity protein dishevelled
- Frizzled-3
- Protein wingless
- Frizzled-2
- Wnt inhibitor of Dorsal protein
- Protein Wnt-5
- Frizzled-4
- Protein Wnt
Sequence:
MALEPYTKSAEIEPQLCQVIDNNEDVTTKATKCTKSNSGVGWRQMLIGFLLICFGISNSWQYKNVHMPSSSSLIASPPASAFVNTPATLLFTTRHDIQVANITRPTGGPQIDVIVRDLAEAMAIDFYYAKNLVCWTDSGREIIECAQTNSSALQPLLRAPKQTVISTGLDKPEGLAMDWYTDKIYWTDGEKNRIEVATLDGRYQKVLFWTDLDQPRAVAVVPARKLLIWTDWGEYPKIERASMDGDPLSRMTLVKEHVFWPNGLAVDLKNELIYWTDGKHHFIDVMRLDGSSRRTIVNNLKYPFSLTFYDDRLYWTDWQRGSLNALDLQTRELKELIDTPKAPNSVRAWDPSLQPYEDNPCAHNNGNCSHLCLLATNSQGFSCACPTGVKLISANTCANGSQEMMFIVQRTQISKISLDSPDYTIFPLPLGKVKYAIAIDYDPVEEHIYWSDVETYTIKRAHADGTGVTDFVTSEVRHPDGLALDWLARNLYWTDTVTDRIEVCRLDGTARKVLIYEHLEEPRAIAVAPSLGWMFWSDWNERKPKVERASLDGSERVVLVSENLGWPNGIALDIEAKAIYWCDGKTDKIEVANMDGSGRRVVISDNLKHLFGLSILDDYLYWTDWQRRSIDRAHKITGNNRIVVVDQYPDLMGLKVTRLREVRGQNACAVRNGGCSHLCLNRPRDYVCRCAIDYELANDKRTCVVPAAFLLFSRQEHIGRISIEYNEGNHNDERIPFKDVRDAHALDVSVAERRIYWTDQKSKCIFRAFLNGSYVQRIVDSGLIGPDGIAVDWLANNIYWSDAEARRIEVARLDGSSRRVLLWKGVEEPRSLVLEPRRGYMYWTESPTDSIRRAAMDGSDLQTIVAGANHAAGLTFDQETRRLYWATQSRPAKIESADWDGKKRQILVGSDMDEPYAVSLYQDYVYWSDWNTGDIERVHKTTGQNRSLVHSGMTYITSLLVFNDKRQTGVNPCKVNNGGCSHLCLAQPGRRGMTCACPTHYQLAKDGVSCIPPRNYIIFSQRNCFGRLLPNTTDCPNIPLPVSGKNIRAVDYDPITHHIYWIEGRSHSIKRSLANGTKVSLLANSGQPFDLAIDIIGRLLFWTCSQSNSINVTSFLGESVGVIDTGDSEKPRNIAVHAMKRLLFWTDVGSHQAIIRARVDGNERVELAYKLEGVTALALDQQSDMIYYAHGKRIDAIDINGKNKKTLVSMHISQVINIAALGGFVYWLDDKTGVERITVNGERRSAELQRLPQITDIRAVWTPDPKVLRNHTCMHSRTKCSHICIASGEGIARTRDVCSCPKHLMLLEDKENCGAFPACGPDHFTCAAPVSGISDVNKDCIPASWRCDGQKDCPDKSDEVGCPTCRADQFSCQSGECIDKSLVCDGTTNCANGHDEADCCKRPGEFQCPINKLCISAALLCDGWENCADGADESSDICLQRRMAPATDKRAFMILIGATMITIFSIVYLLQFCRTRIGKSRTEPKDDQATDPLSPSTLSKSQRVSKIASVADAVRMSTLNSRNSMNSYDRNHITGASSSTTNGSSMVAYPINPPPSPATRSRRPYRHYKIINQPPPPTPCSTDICDESDSNYTSKSNSNNSNGGATKHSSSSAAACLQYGYDSEPYPPPPTPRSHYHSDVRIVPESSCPPSPSSRSSTYFSPLPPPPSPVQSPSRGFT
Protein: Transcription factor 4 (Q91YV0)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYCAYTIPGMGGNSLMYYYNGKAVYAPSASTADYNRDSPGYPSSKPAASTFPSSFFMQDGHHSSDPWSSSSGMNQPGYGGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGTGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAVPGGHGDMHGIMGPSHNGAMGSLGSGYGTSLLSANRHSLMVGAHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVSSGSSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDAANHMGQM
Protein: Psoralen synthase (EC 1.14.14.141) (Cytochrome P450 CYP71AJ1) (Q6QNI4)
Organism: Ammi majus (Bishop's weed)
Function: Involved in linear furanocumarin (psoralen) biosynthesis. Converts marmesin to psoralen.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKMLEQNPQYLYFFSLFLVTIFLYKWLTLKKTPLKNLPPSPPQYPIIGNLHQIGPDPQASLRDLAQKYGPLMFLKFGTVPVLVVSSADAAREALKTHDLVFADRPYSSVANKIFYNGKDMVFARYTEYWRQVKSICVTQLLSNKRVNSFHYVREEEVDLLVQNLENSHSKVANLTELLIEVTGNVVCRVSVGSGDKVDSYKILILEIMDMLGYSRSIEDFFPLLGWVDWLTGLRGKVAEAAKGVDTFLEGVLKEHLSTTGSKYNDFVSILLEIQEADAGSSMDNECIKSLIWDMLGAGTETISTALEWTLAALIKNPDAMFKLQNEVREIGKGKSKISEADLVKMNYLQAVMKESMRLYFTAPLLVPREARQDIKFMGYDISSGTQVLINAWAIARDPLLWDKPEEFRPERFLNSPIDYKGFHYEFLPFGAGRRGCPGIQFAMCINELVVANLVHKFNFELPDGKRLEDLDMTAASGITLRKKSPLLVVARPHV
Protein: Aldehyde oxidase (EC 1.2.3.1) (Aldehyde oxidase 1) (Azaheterocycle hydroxylase) (EC 1.17.3.-) (Q06278)
Organism: Homo sapiens (Human)
Function: Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18671973, ECO:0000269|PubMed:20444863, ECO:0000269|PubMed:23857892}.
Interaction partners:
- Molybdenum cofactor sulfurase
- Amine oxidase [flavin-containing] B
- Sulfite oxidase, mitochondrial
- Cytochrome P450 2C9
- Cytochrome P450 2B6
- Molybdenum cofactor biosynthesis protein 1
- Nicotinamide N-methyltransferase
- Cytochrome P450 3A4)
- Cytochrome P450 2A6
- All-trans-retinol dehydrogenase [NAD
Sequence:
MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPGMVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCCLDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHAYNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRKWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKLIGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPVHYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYCDDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAEKFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPERKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKYIQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGEDMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKFPNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEIDQTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGSRAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETVPNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVGYFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAIDIGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSNTLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWNVPI