wanglab/gogpt-training-data huggingface dataset:
Protein: Inner membrane protein CreD (P08369)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Sensor protein CreC
- Transcriptional regulatory protein CreB
- Protein CreA
- Protein CbrA
Sequence:
MLKSPLFWKMTSLFGAVLLLLIPIMLIRQVIVERADYRSDVEDAIRQSTSGPQKLVGPLIAIPVTELYTVQEEDKTVERKRSFIHFWLPESLMVDGNQNVEERKIGIYTGQVWHSDLTLKADFDVSRLSELNAPNITLGKPFIVISVGDARGIGVVKAPEVNGTALTIEPGTGLEQGGQGVHIPLPEGDWRKQNLKLNMALNLSGTGDLSVVPGGRNSEMTLTSNWPHPSFLGDFLPAKREVSESGFQAHWQSSWFANNLGERFASGNDTGWENFPAFSVAVTTPADQYQLTDRATKYAILLIALTFMAFFVFETLTAQRLHPMQYLLVGLSLVMFYLLLLALSEHTGFTVAWIIASLIGAIMNGIYLQAVLKGWCNSMLFTLALLLLDGVMWGLLNSADSALLLGTSVLVVALAGMMFVTRNIDWYAFSLPKMKASKEVTTDDELRIWK
Protein: Receptor-like cytosolic serine/threonine-protein kinase RBK2 (EC 2.7.11.1) (Protein ROP BINDING PROTEIN KINASES 2) (Q8RXC8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Rac-like GTP-binding protein ARAC5
- peptidylprolyl isomerase
- Probable boron transporter 6
- Probable boron transporter 7
- Uncharacterized protein At4g00950
- Probable boron transporter 2
- Probable boron transporter 3
- Putative boron transporter 5
- Boron transporter 1
Sequence:
MNSASAHDLRLLEVDKEKQDPKSPRGALEACLTRCSISSASSSSDDPPPNREAIDNADADTDVQCKNHRASSNWGKFFKLWKRRSMKRLSSFPPLSGAAPPIIKQNKSADPNMNGMVLHDIYDFQSSLQNFSISDIEIATDNFSPENIIGRGGYADVYQGILPEGKLIAVKRLTKGTPDEQTAEFLSELGIIAHVDHPNTAKFIGCCIEGGMHLVFRLSPLGSLGSLLHGPSKYKLTWSRRYNVALGTADGLVYLHEGCQRRIIHRDIKADNILLTEDFQPQICDFGLAKWLPKQLTHHNVSKFEGTFGYFAPEYFMHGIVDEKTDVFAFGVLLLELITGHPALDESQQSLVLWAKPLLERKAIKELVDPSLGDEYNREELIRLTSTASLCIDQSSLLRPRMSQVVELLLGHEDVVMTPREAKIKMMQRTYSEELLDSVEYNSTKYLGDLDRIREVALAS
Protein: Bifunctional NMN adenylyltransferase/Nudix hydrolase [Includes: Nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1) (NAD(+) diphosphorylase) (NAD(+) pyrophosphorylase) (NMN adenylyltransferase); ADP compounds hydrolase (EC 3.6.1.-)] (Q55928)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: The Nudix hydrolase domain is active on ADP-ribose, (2')-phospho-ADP-ribose, IDP-ribose and NADPH.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Nicotinamide phosphoribosyltransferase
- Glutamine-dependent NAD
- Probable nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Probable nicotinate-nucleotide adenylyltransferase
- CinA-like protein
- NAD kinase 2
- NAD kinase 1
- Slr1134 protein
- 5'-nucleotidase SurE
- NAD
Sequence:
MQTKYQYGIYIGRFQPFHLGHLRTLNLALEKAEQVIIILGSHRVAADTRNPWRSPERMAMIEACLSPQILKRVHFLTVRDWLYSDNLWLAAVQQQVLKITGGSNSVVVLGHRKDASSYYLNLFPQWDYLETGHYPDFSSTAIRGAYFEGKEGDYLDKVPPAIADYLQTFQKSERYIALCDEYQFLQAYKQAWATAPYAPTFITTDAVVVQAGHVLMVRRQAKPGLGLIALPGGFIKQNETLVEGMLRELKEETRLKVPLPVLRGSIVDSHVFDAPGRSLRGRTITHAYFIQLPGGELPAVKGGDDAQKAWWMSLADLYAQEEQIYEDHFQIIQHFVSKV
Protein: Junctophilin-3 (JP-3) (Junctophilin type 3) (Trinucleotide repeat-containing gene 22 protein) (Q8WXH2)
Organism: Homo sapiens (Human)
Function: Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH3 is brain-specific and appears to have an active role in certain neurons involved in motor coordination and memory.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Localized predominantly on the plasma membrane. The transmembrane domain is anchored in endoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane (By similarity). {ECO:0000250}.
Interaction partners:
- Triadin
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Intermembrane lipid transfer protein VPS13A
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Ryanodine receptor 1
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Synaptophysin-like protein 2
- Junctophilin-4
- Aspartyl/asparaginyl beta-hydroxylase
Sequence:
MSSGGRFNFDDGGSYCGGWEDGKAHGHGVCTGPKGQGEYTGSWSHGFEVLGVYTWPSGNTYQGTWAQGKRHGIGLESKGKWVYKGEWTHGFKGRYGVRECAGNGAKYEGTWSNGLQDGYGTETYSDGGTYQGQWVGGMRQGYGVRQSVPYGMAAVIRSPLRTSINSLRSEHTNGTALHPDASPAVAGSPAVSRGGFVLVAHSDSEILKSKKKGLFRRSLLSGLKLRKSESKSSLASQRSKQSSFRSEAGMSTVSSTASDIHSTISLGEAEAELAVIEDDIDATTTETYVGEWKNDKRSGFGVSQRSDGLKYEGEWASNRRHGYGCMTFPDGTKEEGKYKQNILVGGKRKNLIPLRASKIREKVDRAVEAAERAATIAKQKAEIAASRTSHSRAKAEAALTAAQKAQEEARIARITAKEFSPSFQHRENGLEYQRPKRQTSCDDIEVLSTGTPLQQESPELYRKGTTPSDLTPDDSPLQSFPTSPAATPPPAPAARNKVAHFSRQVSVDEERGGDIQMLLEGRAGDCARSSWGEEQAGGSRGVRSGALRGGLLVDDFRTRGSGRKQPGNPKPRERRTESPPVFTWTSHHRASNHSPGGSRLLELQEEKLSNYRMEMKPLLRMETHPQKRRYSKGGACRGLGDDHRPEDRGFGVQRLRSKAQNKENFRPASSAEPAVQKLASLRLGGAEPRLLRWDLTFSPPQKSLPVALESDEENGDELKSSTGSAPILVVMVILLNIGVAILFINFFI
Protein: Pyruvate decarboxylase isozyme 3 (EC 4.1.1.-) (EC 4.1.1.43) (EC 4.1.1.72) (EC 4.1.1.74) (Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase) (2ODC) (P26263)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Minor of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate), valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate), isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins. The expression level of this protein in the presence of fermentable carbon sources is so low that it cannot compensate for the other two pyruvate decarboxylases to sustain fermentation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pyruvate decarboxylase isozyme 2
- Pyruvate decarboxylase isozyme 1
- Alcohol dehydrogenase 4
- Pyruvate kinase 1
- Pyruvate kinase 2
- NADP-dependent alcohol dehydrogenase 6
- Transketolase 2
- Transketolase 1
- Alcohol dehydrogenase 2
- Alcohol dehydrogenase 1
Sequence:
MSEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGLSVLVTTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTSMITDIATAPSEIDRLIRTTFITQRPSYLGLPANLVDLKVPGSLLEKPIDLSLKPNDPEAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGVYVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVEFHSDYVKVKNATFLGVQMKFALQNLLKVIPDVVKGYKSVPVPTKTPANKGVPASTPLKQEWLWNELSKFLQEGDVIISETGTSAFGINQTIFPKDAYGISQVLWGSIGFTTGATLGAAFAAEEIDPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPHAEYNEIQTWDHLALLPAFGAKKYENHKIATTGEWDALTTDSEFQKNSVIRLIELKLPVFDAPESLIKQAQLTAATNAKQ
Protein: Zinc protease PQQL-like (EC 3.4.24.-) (Q9FJT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDLIAGESSKVLRKQGFRSLKLMSVDMEQELGNELEPFGADYGRLDNGLIYYVRRNSKPRMRAALALAVKVGSVLEEEDQRGVAHIVEHLAFSATTRYTNHDIVKFLESIGAEFGPCQNAMTTADETIYELFVPVDKPELLSQAISILAEFSSEIRVSKEDLEKERGAVMEEYRGNRNATGRMQDSHWQLMMEGSKYAERLPIGLEKVIRSVPAATVKQFYQKWYHLCNMAVVAVGDFPDTKTVVDLIKTHFEDKRSSSEPPQIPVFPVPSHEETRFSCFVESEAAGSAVMISYKMPVSDLKTVKDYRDMLAESMFLHALNQRLFKISRRKDPPFFACSVAADVLVARVRLHGFSEREISVVRALMMSEIESAYLERDQVQSTSLRDEYIQHFLHKEPVIGIEYEAQLQKTLLPQISASDVSRYSEKLRTSCGCVIKSMEPKSAATIDHMRNVVSKVNSLEEEKMIAPWDEENIPEEIVSEKPTPGDITHQLEYPEVGVTELTLSNGMQVCYKSTDFLDDQVLFTGFSYGGLSELPESDYISCSMGSTIAGEIGMFGYKPSVLMDMLADLETALQLVYQLFTTNVMPQEEEVGIVMQMAEESVRARERDPYTVFANRVKELNYGNSYFFRPIRISELRKVDPLKACEYFNSCFRDPSTFTVVIVGNLDPTIALPLILQYLGGIPKPPQPVLNFNRDDLKGLPFTFPTKITKEFVRSPMVEAQCSVQLCFPVQLTNGTMIEEIHCIGFLGKLLETKIIQFLRFEHGQIYSAEVSVFLGGNKPSRTADLRGDISVNFSCDPEISSKLVDLALEEIVRLQKEGPSQEDISAILEIEQRAHENGMQENYYWLDRIIRGYQSRVYAGDLGASCKILEEGRLRMRESLAPQTAQAALQRILPHPCKKQYTAVILMPQRSRFGFLSSIFSSRSEGPYIRDTKILAGIAGLGVVVFGIWRYSRK
Protein: Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP) (Q9QWY8)
Organism: Mus musculus (Mouse)
Function: May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Plays a role in ciliogenesis (By similarity). Posseses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2.
Subcellular location: Cytoplasm. Membrane. Golgi apparatus {ECO:0000250|UniProtKB:Q9ULH1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9ULH1}. Note=Predominantly cytoplasmic. Partially membrane-associated.
Interaction partners:
- ADP-ribosylation factor 6
- Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3
- ADP-ribosylation factor 4
- Src substrate cortactin
- Rab11 family-interacting protein 3
- Ras-related protein Rab-11A
- Rhodopsin
- Adenomatous polyposis coli protein
- Focal adhesion kinase 1
- ADP-ribosylation factor 1
Sequence:
MRSSASRLSSFSSRDSLWNRMPDQISVSEFIAETTEDYNSPTTSSFTTRLHNCRNTVTLLEEALDQDRTALQKVKKSVKAIYNSGQDHVQNEENYAQVLDKFGSNFLSRDNPDLGTAFVKFSTLTKELSTLLKNLLQGLSHNVIFTLDSLLKGDLKGVKGDLKKPFDKAWKDYETKFTKIEKEKREHAKQHGMIRTEITGAEIAEEMEKERRLFQLQMCEYLIKVNEIKTKKGVDLLQNLIKYYHAQCNFFQDGLKTADKLKQYIEKLAADLYNIKQTQDEEKKQLTALRDLIKSSLQLDPKEVGGLYVASRANSSRRDSQSRQGGYSMHQLQGNKEYGSEKKGFLLKKSDGIRKVWQRRKCAVKNGILTISHATSNRQPAKLNLLTCQVKPNAEDKKSFDLISHNRTYHFQAEDEQDYIAWISVLTNSKEEALTMAFRGEQSTGENSLEDLTKAIIEDVQRLPGNDICCDCGSSEPTWLSTNLGILTCIECSGIHREMGVHISRIQSLELDKLGTSELLLAKNVGNNSFNDIMEANLPSPSPKPTPSSDMTVRKEYITAKYVDHRFSRKTCASSSAKLNELLEAIKSRDLLALIQVYAEGVELMEPLLEPGQELGETALHLAVRTADQTSLHLVDFLVQNCGNLDKQTSVGNTVLHYCSMYGKPECLKLLLRSKPTVDIVNQNGETALDIAKRLKATQCEDLLSQAKSGKFNPHVHVEYEWNLRQDEMDESDDDLDDKPSPIKKERSPRPQSFCHSSSISPQDKLALPGFSTPRDKQRLSYGAFTNQIFASTSTDLPTSPTSEAPPLPPRNAGKGPTGPPSTLPLGTQTSSGSSTLSKKRPPPPPPGHKRTLSDPPSPLPHGPPNKGAIPWGNDVGPLSSSKTANKFEGLSQQASTSSAKTALGPRVLPKLPQKVALRKTETSHHLSLDRTNIPPETFQKSSQLTELPQKPPLGELPPKPVELAPKPQVGELPPKPGELPPKPQLGDLPPKPQLSDLPPKPQMKDLPPKPQLGDLLAKSQAGDVSAKVQPPSEVTQRSHTGDLSPNVQSRDAIQKQASEDSNDLTPTLPETPVPLPRKINTGKNKVRRVKTIYDCQADNDDELTFIEGEVIIVTGEEDQEWWIGHIEGQPERKGVFPVSFVHILSD
Protein: Serpentine receptor class gamma (G5EEF5)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- SRBC-64)
- Serpentine Receptor, class BC
- G-protein coupled receptor daf-37
- G-protein coupled receptor daf-38
- Serpentine receptor class X-43
- 7TM GPCR serpentine receptor class x
- Guanine nucleotide-binding protein alpha-3 subunit
- Guanine nucleotide-binding protein alpha-2 subunit
- Serpentine receptor class gamma-47
Sequence:
MTLASLLRFIITSVYGAALLVLYTYVVIIIIAHKKSESSFRSSFYKLFIVGFFMNMMTYFNSLISLRLPQSNGINETLSNFFLTHNEHNMEVIFPVKVFHFLHYYFAYAQYIYNFFISLNRFSLITNPIKSELFWRKRFWWFVFAIFAIPWAFAVPILVGRSYYVYHSHGDYFFLDTTIKRSLIYTILAPTLSVITAMNSFLNFMSVRKVIILKLSGGRVPEKNLLQMSFVIFFIDIFLVILTLIKAIIIACGLSFKSESTDEILSWIVILIPFASDALTLTQPLLLLFFSKTVRRCCIWPFPCLKSLRSHRLIARNSVLVVRPFGAPTITG
Protein: Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) (SR Ca(2+)-ATPase 2) (EC 7.2.2.10) (Calcium pump 2) (Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) (P16615)
Organism: Homo sapiens (Human)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation. Also modulates ER contacts with lipid droplets, mitochondria and endosomes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:12804600}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER contact junction. {ECO:0000250|UniProtKB:O55143}.
Interaction partners:
- Phospholamban
- Sarcolipin
- Sarcoplasmic reticulum histidine-rich calcium-binding protein
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Histone acetyltransferase KAT5
- Nuclear receptor ROR-alpha
- Ryanodine receptor 2
- Sodium/potassium-transporting ATPase subunit beta-1
Sequence:
MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDRVEGDTCSLNEFTITGSTYAPIGEVHKDDKPVNCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTSGVKQKIMSVIREWGSGSDTLRCLALATHDNPLRREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELNPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFEGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNVTQWLMVLKISLPVILMDETLKFVARNYLEPGKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS
Protein: cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A (EC 3.1.4.17) (Cyclic GMP-inhibited phosphodiesterase A) (CGI-PDE A) (cGMP-inhibited cAMP phosphodiesterase) (cGI-PDE) (Q14432)
Organism: Homo sapiens (Human)
Function: Cyclic nucleotide phosphodiesterase with specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has also activity toward cUMP. Independently of its catalytic activity it is part of an E2/17beta-estradiol-induced pro-apoptotic signaling pathway. E2 stabilizes the PDE3A/SLFN12 complex in the cytosol, promoting the dephosphorylation of SLFN12 and activating its pro-apoptotic ribosomal RNA/rRNA ribonuclease activity. This apoptotic pathway might be relevant in tissues with high concentration of E2 and be for instance involved in placenta remodeling.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9Z0X4}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:35104454}.
Interaction partners:
- Ribonuclease SLFN12
- cAMP-dependent protein kinase catalytic subunit alpha
- Adenosine kinase
- cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- GMP reductase 1
- GTP:AMP phosphotransferase AK3, mitochondrial
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Adenine phosphoribosyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MAVPGDAARVRDKPVHSGVSQAPTAGRDCHHRADPASPRDSGCRGCWGDLVLQPLRSSRKLSSALCAGSLSFLLALLVRLVRGEVGCDLEQCKEAAAAEEEEAAPGAEGGVFPGPRGGAPGGGARLSPWLQPSALLFSLLCAFFWMGLYLLRAGVRLPLAVALLAACCGGEALVQIGLGVGEDHLLSLPAAGVVLSCLAAATWLVLRLRLGVLMIALTSAVRTVSLISLERFKVAWRPYLAYLAGVLGILLARYVEQILPQSAEAAPREHLGSQLIAGTKEDIPVFKRRRRSSSVVSAEMSGCSSKSHRRTSLPCIPREQLMGHSEWDHKRGPRGSQSSGTSITVDIAVMGEAHGLITDLLADPSLPPNVCTSLRAVSNLLSTQLTFQAIHKPRVNPVTSLSENYTCSDSEESSEKDKLAIPKRLRRSLPPGLLRRVSSTWTTTTSATGLPTLEPAPVRRDRSTSIKLQEAPSSSPDSWNNPVMMTLTKSRSFTSSYAISAANHVKAKKQSRPGALAKISPLSSPCSSPLQGTPASSLVSKISAVQFPESADTTAKQSLGSHRALTYTQSAPDLSPQILTPPVICSSCGRPYSQGNPADEPLERSGVATRTPSRTDDTAQVTSDYETNNNSDSSDIVQNEDETECLREPLRKASACSTYAPETMMFLDKPILAPEPLVMDNLDSIMEQLNTWNFPIFDLVENIGRKCGRILSQVSYRLFEDMGLFEAFKIPIREFMNYFHALEIGYRDIPYHNRIHATDVLHAVWYLTTQPIPGLSTVINDHGSTSDSDSDSGFTHGHMGYVFSKTYNVTDDKYGCLSGNIPALELMALYVAAAMHDYDHPGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLFMSRPEYNFLINLDHVEFKHFRFLVIEAILATDLKKHFDFVAKFNGKVNDDVGIDWTNENDRLLVCQMCIKLADINGPAKCKELHLQWTDGIVNEFYEQGDEEASLGLPISPFMDRSAPQLANLQESFISHIVGPLCNSYDSAGLMPGKWVEDSDESGDTDDPEEEEEEAPAPNEEETCENNESPKKKTFKRRKIYCQITQHLLQNHKMWKKVIEEEQRLAGIENQSLDQTPQSHSSEQIQAIKEEEEEKGKPRGEEIPTQKPDQ
Protein: Protein TRIGALACTOSYLDIACYLGLYCEROL 2, chloroplastic (ABC transporter I family member 15) (ABC transporter ABCI.15) (AtABCI15) (Q9LTR2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of a phosphatidic acid/lipid transport complex in the chloroplast envelope. Specifically binds phosphatidic acid (PA). Involved in lipid transfer from the endoplasmic reticulum (ER) to plastids, and necessary for thylakoids formation.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:16818883}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein TRIGALACTOSYLDIACYLGLYCEROL 1, chloroplastic
- Protein TRIGALACTOSYLDIACYLGLYCEROL 3, chloroplastic
- Protein TRIGALACTOSYLDIACYLGLYCEROL 4, chloroplastic
- Protein TRIGALACTOSYLDIACYLGLYCEROL 5
- Protein ABCI7, chloroplastic
- Protein PTST homolog 2, chloroplastic
- Iron-sulfur cluster assembly SufBD family protein ABCI8, chloroplastic
- ABC transporter I family member 6, chloroplastic
- ABC transporter I family member 1
- Cytochrome C assembly protein
Sequence:
MIGNPVIQVPSSLMPSSSMIACPRVSPNGVPYLPPKPRTRHLVVRAASNSDAAHGQPSSDGGKNPLTVVLDVPRNIWRQTLKPLSDFGFGKRSIWEGGVGLFIVSGATLLALSWAWLRGFQMRSKFRKYQTVFELSHASGICTGTPVRIRGVTVGTIIRVNPSLKNIEAVAEIEDDKIIIPRNSLVEVNQSGLLMETMIDIMPRNPIPEPSVGPLHPECGKEGLIVCDRQTIKGVQGVSLDELVGIFTRIGREVEAIGVANTYSLAERAASVIEEARPLLKKIQAMAEDAQPLLSEFRDSGLLKEVECLTRSLTQASDDLRKVNSSIMTPENTELIQKSIYTLVYTLKNVESISSDILGFTGDEATRKNLKLLIKSLSRLL
Protein: Octanoyltransferase (EC 2.3.1.181) (Lipoate-protein ligase B) (Lipoyl/octanoyl transferase) (Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase) (P9WK83)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}.
Interaction partners:
- Lipoyl synthase
- Glycine cleavage system H protein
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Epimerase family protein Rv2216
- Probable fatty acid synthase Fas
- Uncharacterized protein Rv2219
- Diglucosylglycerate octanoyltransferase
- Pyridoxal 5'-phosphate synthase subunit PdxS
- Nucleoside triphosphate pyrophosphatase
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks1
Sequence:
MTGSIRSKLSAIDVRQLGTVDYRTAWQLQRELADARVAGGADTLLLLEHPAVYTAGRRTETHERPIDGTPVVDTDRGGKITWHGPGQLVGYPIIGLAEPLDVVNYVRRLEESLIQVCADLGLHAGRVDGRSGVWLPGRPARKVAAIGVRVSRATTLHGFALNCDCDLAAFTAIVPCGISDAAVTSLSAELGRTVTVDEVRATVAAAVCAALDGVLPVGDRVPSHAVPSPL
Protein: Exosome complex component rrp46 (Ribosomal RNA-processing protein 46) (O42894)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. ski6 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Exosome complex exonuclease dis3
- Exosome complex component rrp42
- Exosome complex component rrp4
- Exosome complex component rrp43
- Exosome complex protein C1739.07
- Exosome complex component rrp40
- Exosome complex component ski6
- Exosome complex component csl4
- Exosome complex component mtr3
- Exosome complex component rrp45
Sequence:
MNRIGILSRSDGSSEWKQGSARVICGVNGPIDVKIRDERLNKATVEVLVQPVSGVAETLEKMISSRIVGILEDAIFLNTYPRTLIQVSIQIIEEDGTDTLAAVINGAVLALLDAGISLKYIPCAINCHWKNKITQDEPDVDGTINKLESIITICYSISSEPAKLIFLETAGPIPEEDFFRVLETAPLHAEEVSKKMKELLFETYNESDGHENEKNPKEDVEMDVVA
Protein: TSC complex subunit 2 (A0A2R8YDR3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XPTSKDSGLKEKFKILLGLGTPRPNPRSAEGKQTEFIITAEILRELSMECGLNNRIRMIGQICEVAKTKKFEEHAVEALWKAVADLLQPERPLEARHAVLALLKAIVQGQGERLGVLRALFFKVIKDYPSNEDLHERLEVFKALTDNGRHITYLEEELADFVLQWMDVGLSSEFLLVLVNLVKFNSCYLDEYIARMVQMICLLCVRTASSVDIEVSLQVLDAVVCYNCLPAESLPLFIVTLCRTINVKELCEPCWKLMRNLLGTHLGHSAIYNMCHLMEDRAYMEDAPLLRGAVFFVGMALWGAHRLYSLRNSPTSVLPSFYQAMACPNEVVSYEIVLSITRLIKKYRKELQVVAWDILLNIIERLLQQLQTLDSPELRTIVHDLLTTVEELCDQNEFHGSQERYFELVERCADQRPESSLLNLISYRAQSIHPAKDGWIQNLQALMERFFRSESRGAVRIKVLDVLSFVLLINRQFYEEELINSVVISQLSHIPEDKDHQVRKLATQLLVDLAEGCHTHHFNSLLDIIEKVMARSLSPPPELEERDVAAYSASLEDVKTAVLGLLVILQTKLYTLPASHATRVYEMLVSHIQLHYKHSYTLPIASSIRLQAFDFLLLLRADSLHRLGLPNKDGVVRFSPYCVCDYMEPERGSEKKTSGPLSPPTGPPGPAPAGPAVRLGSVPYSLLFRVLLQCLKQESDWKVLKLVLGRLPESLRYKVLIFTSPCSVDQLCSALCSMLSGPKTLERLRGAPEGFSRTDLHLAVVPVLTALISYHNYLDKTKQREMVYCLEQGLIHRCASQCVVALSICSVEMPDIIIKALPVLVVKLTHISATASMAVPLLEFLSTLARLPHLYRNFAAEQYASVFAISLPYTNPSKFNQYIVCLAHHVIAMWFIRCRLPFRKDFVPFITKGLRSNVLLSFDDTPEKDSFRARSTSLNERPKSLRIARPPKQGLNNSPPVKEFKESSAAEAFRCRSISVSEHVVRRIQTSLTSASLGSADENSVAQADDSLKNLHLELTETCLDMMARYVFSNFTAVPKRSPVGEFLLAGGRTKTWLVGNKLVTVTTSVGTGTRSLLGLDSGELQSGPESSSSPGVHVRQTKEAPAKLESQAGQQVSRGARDRVRSMSGGHGLRVGALDVPASQFLGSATSPGPRTAPAAKPEKASAGTRVPVQEKTNLAAYVPLLTQGWAEILVRRPTGNTSWLMSLENPLSPFSSDINNMPLQELSNALMAAERFKEHRDTALYKSLSVPAASTAKPPPLPRSNTDSAVVMEEGSPGEVPVLVEPPGLEDVEAALGMDRRTDAYSRSSSVSSQEEKSLHAEELVGRGIPIERVVSSEGGRPSVDLSFQPSQPLSKSSSSPELQTLQDILGDPGDKADVGRLSPEVKARSQSGTLDGESAAWSASGEDSRGQPEGPLPSSSPRSPSGLRPRGYTISDSAPSRRGKRVERDALKSRATASNAEKVPGINPSFVFLQLYHSPFFGDESNKPILLPNESQSFERSVQLLDQIPSYDTHKIAVLYVGEGQSNSELAILSNEHGSYRYTEFLTGLGRLIELKDCQPDKVYLGGLDVCGEDGQFTYCWHDDIMQAVFHIATLMPTKDVDKHRCDKKRHLGNDFVSIVYNDSGEDFKLGTIKGQFNFVHVIVTPLDYECNLVSLQCRKDMEGLVDTSVAKIVSDRNLPFVARQMALHANMASQVHHSRSNPTDIYPSKWIARLRHIKRLRQRICEEAAYSNPSLPLVHPPSHSKAPAQTPAEPTPGYEVGQRKRLISSVEDFTEFV