wanglab/gogpt-training-data huggingface dataset:
Protein: 5-oxoprolinase (EC 3.5.2.9) (5-oxo-L-prolinase) (5-OPase) (Pyroglutamase) (P28273)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the cleavage of 5-oxo-L-proline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Glutamate--cysteine ligase
- Glutathione hydrolase proenzyme
- Glutathione-specific gamma-glutamylcyclotransferase
- NADP-specific glutamate dehydrogenase 1
- NAD-specific glutamate dehydrogenase
- NADP-specific glutamate dehydrogenase 2
- Glutamine synthetase
- Glutamate synthase
- Glutamate decarboxylase
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
Sequence:
MQKGNIRIAIDKGGTFTDCVGNIGTGKQEHDTVIKLLSVDPKNYPDAPLEGIRRLLEVLEHKTIPRGIPLDISNVRSLRMGTTLATNCALERNGERCAFITTKGFKDSLLIGDQTRPDIFNLNIKKVVPLYDTVVEIDERVTLEDFSEDPYFTKSSPNEQEGILEGNSGEMVRVIKKPDESSVRSILKVLYASGIKSIAIAFLHSYTFPDHERIVGNIAREIGFSHVSLSSEVSPMIKFLPRAHSSVADAYLTPVIKKYLNSISAGLSHAEDTHIQFMQSDGGLVDGGKFSGLKSILSGPAGGVIGYSSTCYDKNNNIPLIGFDMGGTSTDVSRYGDGRLEHVFETVTAGIIIQSPQLDIHTVAAGGSSILSWKNGLFRVGPDSAAADPGPAAYRKGGPLTITDANLFLGRLVPEFFPKIFGPNEDESLDLETTTLKFRELTDVINKDLNSNLTMEEVAYGFIKVANECMARPVRAITEAKGHVVSQHRLVSFGGAGGQHAIAVADSLGIDTVLIHRYSSILSAYGIFLADVIEENQEPCSFILGEPETILKVKKRFLELSKNSIKNLLSQSFSREDIVLERYLNLRYEGTETSLMILQKYDDQWNFREWFSEAHKKEFGFSFDDKRIIIDDIRIRAIGKSGVRKEKTVDEQLIEISHFKKADVSKDASFTQKAYFDNKWVDTAVFKIDDLPAGTIIEGPAILADGTQTNIILPNSQATILNSHIFIKINQKAAKTLSKSGYELDIDPILLSIFSHRFMDIALQMGTQLRKTSVSTNVKERLDFSCALFDSKGNLVANAPHVPVHLGSMSTCISAQAKLWEGKLKPGDVLITNHPDIGGTHLPDITVITPSFSSTGELIFYVASRAHHADIGGILPGSVPPNSKELYEEGTAIYSELVVKEGIFQEELIYKLFVEDPGKYPGCSGSRRFSDNISDLKAQVAANTKGIQLIGSLTKEYDLATILKYMAAIQTNASESIKKMLAKMVEHFGTTKFSGEDRLDDGSLIKLQVIIRPEKEEYIFNFDGTSPQVYGNLNAPEAITNSAILYCLRCLVGEDIPLNQGCLKPLTIKIPAGSLLSPRSGAAVVGGNVLTSQRVTDVILKTFNVMADSQGDCNNFTFGTGGNSGNKTDKQIKGFGYYETICGGSGAGADSWRGSGWNGSDAVHTNMTNTRMTDTEVFERRYPVLLKEFSIRRGSGGKGKYTGGNGVVRDVQFRKAVTASILSERRVIGPHGIKGGQDGSRGENLWVRHSTGALINVGGKNTIYAQPGDRFIIKTPGGGGFGQYKD
Protein: Two-component response regulator-like APRR9 (Pseudo-response regulator 9) (Q8L500)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional repressor of CCA1 and LHY, and positive regulator of LWD1 and LWD2 expression. Controls photoperiodic flowering response and temperature compensation. Involved in the positive and negative feedback loops of the circadian clock. Expression of several members of the ARR-like family is controlled by circadian rhythm. Regulated at the transcriptional level by a corepressor complex consisting of ELF4, ELF3, and LUX. APRR9, APRR7, and APRR5 coordinately act on the upstream region of the target genes to repress their expression from noon until midnight. The particular coordinated sequential expression of APRR9, APRR7, APRR5, APRR3 and APPR1 result to circadian waves that may be at the basis of the endogenous circadian clock.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein LHY
- Protein CCA1
- Transcription factor LUX
- Histone deacetylase 6
- Protein EARLY FLOWERING 4
- Protein EARLY FLOWERING 3
- Protein GIGANTEA
- Protein LNK1
- Adagio protein 1
- Adagio protein 3
Sequence:
MGEIVVLSSDDGMETIKNRVKSSEVVQWEKYLPKTVLRVLLVESDYSTRQIITALLRKCCYKVVAVSDGLAAWEVLKEKSHNIDLILTELDLPSISGFALLALVMEHEACKNIPVIMMSSQDSIKMVLKCMLRGAADYLIKPMRKNELKNLWQHVWRRLTLRDDPTAHAQSLPASQHNLEDTDETCEDSRYHSDQGSGAQAINYNGHNKLMENGKSVDERDEFKETFDVTMDLIGGIDKRPDSIYKDKSRDECVGPELGLSLKRSCSVSFENQDESKHQKLSLSDASAFSRFEESKSAEKAVVALEESTSGEPKTPTESHEKLRKVTSDQGSATTSSNQENIGSSSVSFRNQVLQSTVTNQKQDSPIPVESNREKAASKEVEAGSQSTNEGIAGQSSSTEKPKEEESAKQRWSRSQREAALMKFRLKRKDRCFDKKVRYQSRKKLAEQRPRVKGQFVRTVNSDASTKS
Protein: NPC intracellular cholesterol transporter 1 (A0A8I6GB30)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
CCNCAAQVFSQSCVWYGECGVAFGDKRYNCEYSGPPKPLPKDGYDLVQELCPGLFFGNVSLCCDVQQLQTLKSNLQLPLQFLSRCPSCFYNLMTLFCELTCSPHQSQFLNVTATEDYFDPETRENKTNVKELEYYVGRSFANAMYNACRDVEAPSSNEKALGLLCGRDARACNATNWIEYMFNKDNGQAPFTIIPVFSDLSVLGMEPMRNATKGCNESVDEVTGPCSCQDCSAVCGPKPQPPPPPVPWRILGLDAMYVIMWVAYMAFLVLFFGGLLAVWCHRRRYFVSEYTPIDSNIAFSSNSSDKGEASCCDPLGVAFDDCLRRMFTKWGAFCVRNPTCIIFFSLVFIAACSSGLVFVQVTTNPVELWSAPHSQARLEKEYFDKHFGPFFRTEQLIIQAPNSSVHIYEPYPSGADVPFGPPLNKEILHQVLDLQIAIESITASYNNETVTLQDICVAPLSPYNKNCTIMSVLNYFQNSHAVLDNQVGDDFFVYADYHTHFLYCVRAPASLNDTSLLHGPCLGTFGGPVFPWLVLGGYDDQNYNNATALVITFPVNNYYNDTEKLQRAWAWEKEFINFVKNYKNPNLTISFTAERSIEDELNRESNSDVFTVLISYAVMFLYISLALGHIQSWNRVLVDSKISLGIAGILIVLSSVTCSLGIFSYIGMPLTLIVIEVIPFLVLAVGVDNIFILVQTYQRDERLQEETLDQQLGRILGEVAPTMFLSSFSETSAFFFGALSSMPAVHTFSLFAGMAVLIDFLLQITCFVSFLGLDIKRQEKNRLDILCCVRGPDDGQESQASESYLFRFFKNAFAPFLLTDWLRPVVMAVFVGILSFSIAVVNKVEIGLDQSLSMPNDSYVIDYFKSLGQYLHSGPPVYFVLEEGYNYSSRRGQNMVCGGMGCDNDSLVQQIFNAAELDTYTRVGFAPSSWIDDYFDWVSPQSSCCRLYNVTHQFCNASVIDPTCVRCRPLTPEGKQRPQGKEFMKFLPMFLSDNPNPKCGKGGHAAYSSAVNIMGDDTYIGATYFMTYHTILKTSADYIDALKKARLIASNITETMRSKGSDYRVFPYSVFYVFYEQYLTIIDDAIFNLSVSLGSIFLVTLVALGCELWSAVIMCLTIAMILVNMFGVMWLWGISLNAVSLVNLVMTCGISVEFCSHITRAFTMSTKGSRVSRAEEALAHMGSSVFSGITLTKFGGIVVLAFAKSQIFEIFYFRMYLAMVLLGATHGLIFLPVLLSYIGPSVNKAKRHTTQERYKGTERERLLNF
Protein: DNA polymerase beta (EC 2.7.7.7) (5'-deoxyribose-phosphate lyase) (5'-dRP lyase) (EC 4.2.99.-) (AP lyase) (EC 4.2.99.18) (Q6DRD3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P06746}. Cytoplasm {ECO:0000250|UniProtKB:P06746}. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. {ECO:0000250|UniProtKB:P06746}.
Interaction partners:
- DNA repair protein XRCC1
- Flap endonuclease 1
- Endonuclease 8-like 1 lyase Neil1)
- DNA repair nuclease APEX1
- DNA ligase
- Bifunctional polynucleotide phosphatase/kinase
- Poly [ADP-ribose] polymerase.
- Ubiquitin carboxyl-terminal hydrolase 47
- Poly [ADP-ribose] polymerase 1
- Tyrosyl-DNA phosphodiesterase 1
Sequence:
SKRKAPQESLNEGITDFLVELANYERNVNRAIHKYNAYRKAASVIAKYPQKIKSGTEAKKLDGVGAKIAEKIDEFLTTGKLRKLEKIRNDDTSSSINFLTRVTGIGPAAARKFFDEGVRNLEDLKKIEHKLNHHQQIGLKYFEEFEKRIPRSEMQKMEALILKELDIVDPEYIGTICGSYRRGAESSGDIDILLTHPDFTSQSEKQPKLLHAVVDHLESIGFITDTLSKGDTKFMGVCQLQKEKEEEEEESLHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRTHALEKGFTLNEYTIRPLGVTGVAGEPLLVDSEKDIFEYIQWKYREPKDRSE
Protein: E3 ubiquitin-protein ligase CHIP (EC 2.3.2.27) (RING-type E3 ubiquitin transferase CHIP) (A0A8I5ZPA4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
RGDQMSPHSLSPDLGSQTRNPLVAVYYTNRALCYLKMQQPEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERRIHQESELHSYLTRLIAAERERELEECQRNHEGDEDDGHIRAQQACIEAKHDKYMADMNELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDAFISENGWVEDY
Protein: Fe regulatory protein (Ferric uptake regulator homolog) (Q7BR72)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Catalase-peroxidase
- Zinc uptake regulation protein
- Alkyl hydroperoxide reductase C
Sequence:
MTASRNSRKPATADELRRAGLRVTAARVALLETVRAGDHLDAEALTSGVRRRVGHVSLQAVYDALHALTAARLVRRIEPPGSPARFEGRVGDNHHHVLCRSCGALADVDCAVGDAPCLTASDDRGFVIDEAEVIYRGLCPDCSTPGSSPAP
Protein: Schlafen family member 2 (Schlafen-2) (Q9Z0I6)
Organism: Mus musculus (Mouse)
Function: tRNA-binding protein involved in T-cell mediated immunity. Plays a key role during the metabolic reprograming phase of activated T-cell, when T-cells produce reactive oxygen species (ROS): acts by binding tRNAs and protecting them from cleavage by the oxidative stress-activated ribonuclease angiogenin (ANG). Also required for T-cell quiescence maintenance.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19592487}.
Interaction partners:
Sequence:
MGTRLEATEQSNHRTQRNDIQLENAKAAGKMGISVDLEAKYAKLGLNLGAITFGEKDRKKMKNSHLRKQENANISLAVCALLNSGGGAIKVKIENENYSLTRDGLGLDLEASLCKCLPFVQWHLDFTESEGYIYIYVKSWSQEIFGLPIGTLRTNLYVRSMSSSVQVSAAAALEFLQDLEETGGRPCVRPELPASIAFPEVEGEWHLEDLAAALFNRTEFQYEETFPFTRSRYVEVTLLSAKRLRKRIKELLPQTVSAFANTDGGFLFIGLDGKTQQIIGFEAEKSDLVLLESEIEKHIRQLPVTHFCEEKEKIKYTCKFIEVHKSGAVCAYVCALRVERFCCAVFAAEPESWHVEGGCVKRFTTEEWVKLQMNAPSG
Protein: Inner membrane protein YdgK (P76180)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Ion-translocating oxidoreductase complex subunit A
- OriC-binding nucleoid-associated protein
- Ion-translocating oxidoreductase complex subunit B
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreA
Sequence:
MTTTTPQRIGGWLLGPLAWLLVALLSTTLALLLYTAALSSPQTFQTLGGQALTTQILWGVSFITAIALWYYTLWLTIAFFKRRRCVPKHYIIWLLISVLLAVKAFAFSPVEDGIAVRQLLFTLLATALIVPYFKRSSRVKATFVNP
Protein: SWI/SNF chromatin-remodeling complex subunit snf30 (SWI/SNF complex subunit snf30) (Q9P7S6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- SWI/SNF and RSC complexes subunit arp9
- SWI/SNF chromatin-remodeling complex subunit snf22
- SWI/SNF chromatin-remodeling complex subunit sol1
- SWI/SNF and RSC complexes subunit arp42
- Transcription initiation factor TFIID subunit 14
- SWI/SNF chromatin-remodeling complex subunit snf5
- SWI/SNF and RSC complexes subunit ssr2
- SWI/SNF and RSC complexes subunit ssr3
- SWI/SNF and RSC complexes subunit ssr1
- SWI/SNF and RSC complexes subunit ssr4
Sequence:
MSFVSKSPPIVNSASPTGQVNPMEVEKANKLLEINRLILWKCLELQHIKTAQNSTLEQRALSTELFNSYIQRLKANLAFVVSIASPRQMQVLTPPLSCPESLPQLEPLYKELRQYFQIAQTSTLSYPPSNGDSSSYANGTDLHGNTGTMQQEEKANPSLTRSDSVSSGSYITMQGANSLKAQQDLLNSFTGAPSNNSHNIPDPNLSQTFSATSMGPPNNNYSKFRTDNYLARSSNRSGTPNIQNEQSRFFDSQQAQVQARALMQRYQQGMEFNK
Protein: Aur1p (C7GQH1)
Organism: Saccharomyces cerevisiae (strain JAY291) (Baker's yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MANPFSRWFLSERPPNCHVADLETSLDPHQTLLKVQKYKPALSDWVHYIFLGSIMLFVFITNPAPWIFKILFYCFLGTLFIIPATSQFFFNALPILTWVALYFTSSYFPDDRRPPITVKVLPAVETILYGDNLSDILATSTNSFLDILAWLPYGLFHFGAPFVVAAILFVFGPPTVLQGYAFAFGYMNLFGVIMQNVFPAAPPWYKILYGLQSANYDMHGSPGGLARIDKLLGINMYTTAFSNSSVIFGAFPSLHSGCATMEALFFCYCFPKLKPLFIAYVCWLWWSTMYLTHHYFVDLMAGSVLSYVIFQYTKYTHLPIVDTSLFCRWSYTSIEKYDISKSDPLAADSNDIESVPLSNLELDFDLNMTDEPSVSPSLFDGSTSVSRSSATSITSLGVKRA
Protein: Heat shock transcription factor 1 (A0A8I5Y5J6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
KTKCWSVPRDDQSALGNWWSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTRLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLSDSSSAHSVPKYGRQYSLEHVHGPGPYSAPSPAYSSSSLYSSDAVTSSGPIISDITELAPTSPLASPGRSIDERPLSSSTLVRVKEEPPSPPHSPRVLEASPGRPASMDTPLSPTAFIDSILRESEPTPAASNTAPMDTTGAQAPAPPAPSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQTMLTSHGFSVDTSALLDLFSPSVTMPDMSLPDLDSSLASIQELLSPQEPPRPIEAENSNADSGKQLVHYTAQPLFLLDPDAVDTGSSELPVLFELGESSYFSEGDDYTDDPTISLLTGTEPHKAKDPTVS
Protein: Prodigiosin synthesizing transferase PigC (EC 6.4.-.-) (Prodigiosin synthetase PigC) (Q5W269)
Organism: Serratia sp. (strain ATCC 39006) (Prodigiosinella confusarubida)
Function: Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the transfer of 2-methyl-3-n-amyl-pyrrole (MAP) to 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC) to yield prodigiosin.
Interaction partners:
- Oxidoreductase PigB
- NADP-dependent malic enzyme
- Pyruvate-flavodoxin oxidoreductase
- Pyruvate-flavodoxin oxidoreductase
- D-2-hydroxyglutarate dehydrogenase
- L-prolyl-[peptidyl-carrier protein] dehydrogenase
- NAD-dependent malic enzyme
- Putative phosphoenolpyruvate synthase regulatory protein
- 3-isopropylmalate dehydratase
- Multiphosphoryl transfer protein
Sequence:
MNQPLVVEISGDKALEHHHLGGKGYSLNNLIHAGLPVPSAFCVTAQAYQQFIEEVVPGAELTDGDLIAVRDAILHADIPDSLKQAIGDAYQHLGHDTTIAVRSSALDEDGQRQSFAGQYETYLHVKGSEAVLHKVQACWASLWAERAAQYRHESASHSAIAVILQVMVDADAAGVMFTQDPLSGSTDKVVIDSCWGLGEGVVSGQVTTDSFTLDKATGELCDQQIRHKPNYCQRDEHGLVTLLQTPEAKRDLPSLTPAQLQQLVTLARQAQLIYSTELDIEWAVKDDKVWLLQARPVTTSAKTANVIYANPWESDPAAKEGAFFSRMDTGEIVTGLMTPLGLSFCQFYQKHIHGPAIKTMGLADISHWQIYMGYIQGYVYLNISGSAYMLRQCPPTRNEMKFTTRYATDEIDFKDYKNPYGAGVQGWDYAKSCWYWLKQQVRNMRSAARTVEQMIALRQDETTRFLGLDLTAMTLQQLDQELQRIDRFFLDSCAAYMPFFLQSFALYDALAQACERHIKDGKGLQNRIKASMNNLRTIEVTLGIIKLVATVNQQTELKALFEQHRADELVTLLPVHDISRAFWQGDFEDFLVEFGSRGRQEFDLSIPRWRDDPSYLLQVMKMYLQHPVDLHKKLRETELLRQQDSEALFSAMSWSGRFKLKTLIKLYGMMAERREATRPTFITETWFYRCIMLEVLRRLDAQGIASSADLPYVDFEQFRAYVAGTIPAEQAFSKARLDQNRHQHLFNLHAEEPPMAIVGPYTPKVKAPTQDDKTIRSLTGLAASPGNVVAKARVITDLQVQAGEFQPDEILVARFTDASWTPLFALAAGIVTDIGSTLSHSCIVAREFGIPAVVNLKTATQIINSGDMLILDGDSGTVIIQHQEERNHDG
Protein: At5g38070 (RING/FYVE/PHD zinc finger superfamily protein) (Similarity to unknown protein) (Q9LS14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGDHLVLVVDRLSSDSGLGTVNRADPKADSVNEDGVSESISAGADLCESKFVQCRICHDEDEDTNMDTPCSCSGTLKFAHHNCVQRWCNEKGDTVCEICRQQYKPGYTAPRQLFHYTGISMNFGSDWGIEGLDLRNPYFLTWGDADDDHDLYSFHSPTSLICCRLIALLFVLLLFLRHSLPVLLGGVDDFSITLLMLPLVRTLGILLIAYVFFKSFIVIQRCRQERDTRLSGFSSDEETAPPRILMALPERPELHVPVN
Protein: Cyclic GMP-AMP synthase-like receptor (cGLR) (EC 2.7.7.-) (P0DV12)
Organism: Lucilia cuprina (Green bottle fly) (Australian sheep blowfly)
Function: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (3',2'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Synthesizes 3',2'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG (By similarity). Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',2'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the antiviral immune response via activation of the NF-kappa-B transcription factor Rel (Relish) (By similarity).
Interaction partners:
Sequence:
MELQANLENVLQKVNNFINIDAKRQIYAAHFDNLKNTIFNELRKNEVLAYLFNGFQLGGSYGDNVKVTVPNEYDLVFNIKFPEQPLIIVTADHELPGNVFLDFTRVIHKIAKEKQHEKILQHLKQWLDDENYLKVEKFQWFLRSCFIDVLTKMNFKITFKGRTSSLRYSREGPAHTIKVTESLNFDYSVDFVPGILLNANQCVTSNIVGQWEAIPKPTPTNNHLYKSFRASFYRQEQKIIKNQQQLKNVYRMMKKFRDSKTNMLKMKSYFIKTLFLWKSSRENVSYWSKPLTEIIIDMFKDMEKSLREEKLPFYWDRKLNLYDNYQPRLMREMLNCVESARETLEKAAKELTLPLQKRVFCIFCKLKI
Protein: Asparaginyl-tRNA synthetase (AsnRS) (NARS2) (EC 6.1.1.22) (Asparagine--tRNA ligase, mitochondrial) (Q96I59)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000250}. Mitochondrion {ECO:0000269|PubMed:25807530, ECO:0000269|PubMed:35558980}.
Interaction partners:
- Glutamyl-tRNA
- Glutamyl-tRNA
- Glutamyl-tRNA
- Tyrosine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Tyrosine--tRNA ligase, mitochondrial
- Asparagine--tRNA ligase, cytoplasmic
- Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial
- Probable proline--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
Sequence:
MLGVRCLLRSVRFCSSAPFPKHKPSAKLSVRDALGAQNASGERIKIQGWIRSVRSQKEVLFLHVNDGSSLESLQVVADSGLDSRELNFGSSVEVQGQLIKSPSKRQNVELKAEKIKVIGNCDAKDFPIKYKERHPLEYLRQYPHFRCRTNVLGSILRIRSEATAAIHSFFKDSGFVHIHTPIITSNDSEGAGELFQLEPSGKLKVPEENFFNVPAFLTVSGQLHLEVMSGAFTQVFTFGPTFRAENSQSRRHLAEFYMIEAEISFVDSLQDLMQVIEELFKATTMMVLSKCPEDVELCHKFIAPGQKDRLEHMLKNNFLIISYTEAVEILKQASQNFTFTPEWGADLRTEHEKYLVKHCGNIPVFVINYPLTLKPFYMRDNEDGPQHTVAAVDLLVPGVGELFGGGLREERYHFLEERLARSGLTEVYQWYLDLRRFGSVPHGGFGMGFERYLQCILGVDNIKDVIPFPRFPHSCLL
Protein: Uncharacterized protein YGR168C (P53293)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized membrane protein YIL089W
- Peroxisomal targeting signal receptor 9
- Uncharacterized protein YBL039W-B
- Peroxisomal membrane protein PEX25
- Peroxisomal adenine nucleotide transporter 1
- Peroxisomal membrane protein PEX27
- Peroxisomal membrane protein PEX34
Sequence:
MKHNRPNGTGKAVSGFKQIIRRLLLLLNKKRRKQLVIILKRITQVYGINLVFYVKKWKLKKLQGENIQINDIMPWLRESTILVLLNILYPTLMKFPFLKNHYIHWSSIVGISLMLTKGEVPSWIIAHFLVEAIASKLKIAKLTQWLKKKNFSQGTLIKFQQILVCLAIIVLFAKLDRSSLPFRVLFDHRPFLIDFFTINAIFTVLAVYHRTLKFFFTSGTKSNKNVGGHEVRNFSQYLGVKNHNDWPISSSNLKHVMDRLNEIHEVTIDDNYANINEKIINSYFTKGFFPSLKWTILRQCIEYLFVTKRRRLMGNKLRCIVMLLTFTFVDPTSKMKISPFFAKFFAKSLVNVYLKKYWHCNFGKYILFFLFQLSIM
Protein: Carboxypeptidase sxa2 (EC 3.4.16.-) (P32825)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in degradation or processing of the mating pheromones. Its loss causes a persistent response to the pheromones. It may be required for stabilization of enzymes that are essential for zygote formation. May degrade the mating pheromone P-factor.
Subcellular location: Secreted.
Interaction partners:
- Pro-P-factor
- Pheromone P-factor receptor
- Aspartic proteinase sxa1
- Mating factor M secretion protein mam1
- M-factor
- Pheromone M-factor receptor
- Transcriptional activator protein rec16
- M-factor
- Adenylate cyclase
Sequence:
MLSLFLKSLFAIIIIELTIIHALPTYTVHWKCSIQQANTSSASSNQTVQPRQHAAPSSDRIKSLPEFKGSLPELYSGYLEANSDKSLFYTYAPAVVDSETFIVWLQGGPGCAGTLGFFSENGPIEISQSSPSPSLNPESWTNFANMLWLDQPFGTGYSQGQAAYTTTIEEASSDFVNALKSFYQKFPHLMKKKLYLVGESYGSIWSANFAEALLSEPSLNINFMGVGIVSGLTADYETQEQITASIWVEHISKLGYYFNNTSSTISEEFKKRNKECQYDSVLNRLTFPTEQYPIWRPEYNFSTSTSLRKREALDGEDIGNVFNSISGCDLYSLSNFLLYLENSCVITYDVSLDCSFNEYNDPLITYLNREDVRSSLHATKASTALTSGEGVFADGCNFDLYKKIVSNNVESVLVEIIPRLTEKYKVSFLAGALDLQILWTGTLLALQNTTWNGWQGFTQSPGSLETTNGFTLDERNLAFTLSNSVGHMAPSKDPQMVREWLENTLLY
Protein: Pentalenene oxygenase (EC 1.14.15.32) (Q82IY3)
Organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Function: Catalyzes the conversion of pentalenene to pentalen-13-al by stepwise oxidation via pentalen-13-ol, a precursor of neopentalenolactone antibiotic.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSQHTFVAGTAPGAVPVVGHAWQMMRRPLHFMSSLSAHGDLVKIRIGPTSAYVPCHPELLRQVLTNDRVFDKGGVFYDRARDIAGNGLVTCPYRDHRRQRRLMQSAFQRTQLERYSTAMRAEIDATAARWHDGTVIDAFPELYGMALRTVARTLYSTPVTEELAQRVEQAFDTVLNGLFRQMFLPHSLRRLPTPANLRYRNNLRFLHDTVQDLITEYRRDDTQRDDLLSALLASRDEDGGRLGDTEIHDQVITVMAAGTETVAGTLTWIFHLLSRHPEIEARLYEEIDTVLDGKPPHWDDLPSLSLTDRIITEALRMYPPAWIFTRLTASDVDLAGVRLPEGTTIVFSPSSVQRHSEAYDDASRFDPDRWLPDRTSAVARQAFTAFGTGARKCIGDLFARTEATLALATMLSQWRVTVEPDADVRPVALATVYHPRRLRLRLTARTPGQ
Protein: Membrane-associated phosphatidylinositol transfer protein 1 (Drosophila retinal degeneration B homolog) (Phosphatidylinositol transfer protein, membrane-associated 1) (PITPnm 1) (Pyk2 N-terminal domain-interacting receptor 2) (NIR-2) (O00562)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of phosphatidylinositol (PI) between membranes. Binds PI, phosphatidylcholine (PC) and phosphatidic acid (PA) with the binding affinity order of PI > PA > PC. Regulates RHOA activity, and plays a role in cytoskeleton remodeling. Necessary for normal completion of cytokinesis. Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi. Binds calcium ions.
Subcellular location: Cytoplasm. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:12225667}; Peripheral membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12225667}; Peripheral membrane protein. Lipid droplet {ECO:0000269|PubMed:12225667}. Cleavage furrow {ECO:0000269|PubMed:15125835}. Midbody {ECO:0000269|PubMed:15125835}. Note=Peripheral membrane protein associated with Golgi stacks in interphase cells. A minor proportion is associated with the endoplasmic reticulum. Associated with lipid droplets (PubMed:12225667). Dissociates from the Golgi early on in mitosis and localizes to the cleavage furrow and midbody during cytokinesis (PubMed:15125835). {ECO:0000269|PubMed:12225667, ECO:0000269|PubMed:15125835}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein B/C
- Protein-tyrosine kinase 2-beta
- Vesicle-associated membrane protein-associated protein A
- Oncomodulin-2
- Oncomodulin-1
- Prestin
- Transforming protein RhoA
- Oxysterol-binding protein 1
Sequence:
MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPRLYHSVKTGRGPLSDDWARTAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWTELSMADIRALEEETARMLAQRMAKCNTGSEGSEAQPPGKPSTEARSAASNTGTPDGPEAPPGPDASPDASFGKQWSSSSRSSYSSQHGGAVSPQSLSEWRMQNIARDSENSSEEEFFDAHEGFSDSEEVFPKEMTKWNSNDFIDAFASPVEAEGTPEPGAEAAKGIEDGAQAPRDSEGLDGAGELGAEACAVHALFLILHSGNILDSGPGDANSKQADVQTLSSAFEAVTRIHFPEALGHVALRLVPCPPICAAAYALVSNLSPYSHDGDSLSRSQDHIPLAALPLLATSSSRYQGAVATVIARTNQAYSAFLRSPEGAGFCGQVALIGDGVGGILGFDALCHSANAGTGSRGSSRRGSMNNELLSPEFGPVRDPLADGVEGLGRGSPEPSALPPQRIPSDMASPEPEGSQNSLQAAPATTSSWEPRRASTAFCPPAASSEAPDGPSSTARLDFKVSGFFLFGSPLGLVLALRKTVMPALEAAQMRPACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLTVPRYQKFPLGDGSSLLLADTLQTHSSLFLEELEMLVPSTPTSTSGAFWKGSELATDPPAQPAAPSTTSEVVKILERWWGTKRIDYSLYCPEALTAFPTVTLPHLFHASYWESADVVAFILRQVIEKERPQLAECEEPSIYSPAFPREKWQRKRTQVKIRNVTSNHRASDTVVCEGRPQVLSGRFMYGPLDVVTLTGEKVDVYIMTQPLSGKWIHFGTEVTNSSGRLTFPVPPERALGIGVYPVRMVVRGDHTYAECCLTVVARGTEAVVFSIDGSFTASVSIMGSDPKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWLSQHNFPHGVVSFCDGLTHDPLRQKAMFLQSLVQEVELNIVAGYGSPKDVAVYAALGLSPSQTYIVGRAVRKLQAQCQFLSDGYVAHLGQLEAGSHSHASSGPPRAALGKSSYGVAAPVDFLRKQSQLLRSRGPSQAEREGPGTPPTTLARGKARSISLKLDSEE
Protein: Rifin (Q9NFB5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYINILLFELPLNILIYNQRNHKSTTPHTPNHTQTTRLLCECELYSPANNDNDAEMKRVMQQFEDRTTQRFHEYDERMKTTRQKCKEQCDKEIQKIILKDKLEKELMDKFATLQTDIQSDSIPTCICEKSLEDKVEKGCLRCAGVLGGGIAPGWSLVSGLGYAVWTNYVTQTALQKGIEAGVKAGIEGLRDFSGLGKLIPISVIQNLINHTNYDIAKTYITFVKSVNSTKCAVKEHSFCFSTYISNENALSKRAAGIAEYAADMAKITERGVLDAATPGLTTYSNAITASVVAIVVIVLVMIIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: RNA helicase (EC 3.6.4.13) (Q8IKF0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Small ribosomal subunit protein eS30
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit B
- Polyadenylate-binding protein-interacting protein 1, putative
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit E
- Small ribosomal subunit protein eS1
Sequence:
MSTKEETFNNENDIEGNTEEIVDTFDALGLNEKLLRGIYSYGFEKPSAIQQRGIKPILNGYDTIGQAQSGTGKTATFVISSLQLINYDYVACQALILAPTRELAQQIQKVVLALGDYLKVKCHACVGGTVVREDIDKLKQGVHMVVGTPGRVYDMIDKRHLGVDRLKLFILDEADEMLSRGFKAQIYEVFKKLVPDIQVALFSATMPQEILELTTRFMRDPKTILVKKDELTLEGIRQFYVAVEKEEWKLDTLCDLYETLTITQSIIYCNTRKKVDILTQEMHNRLFTVSCMHGDMDQKDRDLIMREFRSGSTRVLVTTDLLARGIDVQQVSLVINYDLPASPDTYIHRIGRSGRFGRKGVAINFVTNDDKEKDKLKKIESYYSTQIEEMPLEVADYL