wanglab/gogpt-training-data huggingface dataset:
Protein: Post-transcriptional regulator MKT1 (Inactive endonuclease MKT1) (P40850)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in 3'-UTR mediated RNA regulation. Binds to RNA-binding and RNA regulatory proteins. Complexes with PAB1-binding protein to promote mRNA interactions with poly(A)-binding protein. Promotes mating-type switching in mother cells by positively regulating HO expression.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15082763}. Note=Localizes to polysomes in a PBP1-dependent manner. {ECO:0000269|PubMed:15082763}.
Interaction partners:
- PAB1-binding protein 1
- Cell morphogenesis protein PAG1
- GTP-binding protein RHO2
- Protein LSM12
- Inhibitory regulator protein IRA2
- Antagonist of mitotic exit network protein 1
- Zinc finger protein RME1
- mRNA-binding protein PUF3
- Polyadenylate-binding protein, cytoplasmic and nuclear
- J domain-containing protein APJ1
Sequence:
MAIKSLESFLFERGLVGSYAIEALNNCTLDIDVNHYVSRLLTNKREQYLDAIGGFPTSLKMYLESDLKIFKDFNITPIFVFNGGLTYNQLEASGHFTAASASASISSTTTSSSGTNATTRSNTESVLLQRSRGWTQWNNLISSNQNSYIDQPIQPQEPFRHNTTIDSKAYQNDLIAYFIEHGYMYQVAPYSSWFQLAYLLNSAYIDAIYGPTDCLMLDCVDRFILGMEFPNKEFRFIDRSRVMKDLGCTHEEFIDIAMAVGNDLQPTTLPPLQIYPVPQLFDIALEMVLNTGTNFYAYQLSTTLQNDSKENIQNYQRGISALRYMPVLKDTGKVELFVQEIVVSEEDSEKNNKDGKKSNLSSPSSASSSASPATTVTKNASEKLTYEKSSTKEVRKPRDIPNDVHDFIGQMLPHEYYFYRSIGLVTGKLFDAIVTGVYPEEPPLGGGSSTSYKKLVSKSVEIFKNKEINLLTQPINRYYQIKQIKQVKWYAANEPTTLTNRMSPSMFETINHLIVKTETSDEKEFSISEFITTINGSSNMAKDFISEKVIFPNSVPIESKLNSPFNLLSTNFLRLLVLLEFFTFDFKEKLLEPTRWGEVFLKLNELNIDSKYHESVIIFLVFLKCDVLKLDEEVQPPAPSALSQATLRSYPEESLYVLLITRVLTLFQVDQKPSNYHGPIDKKTLIFRDHLSFIKENLNELFEAVLISSLTSGEFNRLSLDNFGWARKIVRYLPFKLDSPNTIMAMMWEFFLQKYLHNGNAKNDALSLVATEFNTYKSTPNLDEQFVESHRFLLEISKVMQELNAAKLIDENVFKLFTKAVEFTTTALSS
Protein: Potassium channel B446_29190 (S5VBU1)
Organism: Streptomyces collinus (strain DSM 40733 / Tue 365)
Function: Potassium channel.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MNESGRVEAFSDGVFAIAITLLILDIKVPKADGPGGLWHALGAQWPSYAAYVVSFLVIGIMWVNHHQVFSYVARVDRALMFLNLLVLMVVAAVPWPTAMLAEYLREDRASHVAAAVYSLVMVAMALAFQALWWHLTRTGHLFDPRVDAPAARATRIRFALGSLGYPLTVGLAFVSAPLTLAAHGLLALYYGFNQVPVPTREAAAPS
Protein: Zinc finger E-box-binding homeobox 1 (Transcription factor 8) (Q9DEH7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MADGPRCKRRKQANPRRTNVSNYSHVLEGQSDSDDEDKLHIVEEEGSLLDGADCDSVAPDDDPNGTADPDGRWDDVKEECVSDEDERSRDALVEEMLQQGDTAVIFPEAPDDEPRQGTPETSGHDENGTPDSFSQLLTCPYCSRGYKRYTSLKEHIKYRHEKSEDNFSCSLCSYTFAYRTQLDRHMTAHKAGREQRHVTQSGGGGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECSNCKKRFSHSGSYSSHISSKKCIGLISVNGRPRPSPATGAAKTPQCSSPYLPTSSPTARVQVRDKLDNSKPLQEQLPLTQIKSEPLDYEYKPVVVAPSARGVNGMFQGGAAAPLQGAVQAVVLPTVGLVSPISINLGDLQNVLKVAVDGNVIRQVLESTQAKGQQAGTGIVGAGGIAQATQQVIQAISLPILDQDGNAKIFINYSLDPSQAQAVLQSPKKEPLGSNTEVCKGQKLPEDLTVKTNRDKTTLTVDEKSMLHNDILLKHCGKDEHRINGKNLEEKMDLEGLCPGQPPLKNLLSLLKAYFALNNEPTKEELAKISESVSLPAEVVKKWFEKMQLGQISMDPSSPQHEEEQTTPVDLDGTKGASPKPDLDEQMNSEKQEERECCSPAEGIAASVNGIESVPASPSPLNLSADGPVPARTLEEGEGPLDLSLPKSATTASVASGHANTVYSAQEEPLNLTCTKKELLSNASTNAAIYASQPSANPINIMTTQLPTLVAITDQGQAQCLRALTTTKQTILIPQLTYSYTTTSSSPAGTDTPQKNILHVNGIKEEKQEMGSEATSILEEQTDSDSGPTKKKMKRTESGLYACDLCDKIFQKSSSLLRHKYEHTGKRPHECGICSKAFKHKHHLIEHLRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKKEAQGQGLGQGVEEEDNPGEEQPQTGSTATSPPSHLDSDERGSSTRDDESEEEDEMGSGSLVDEDEIQVVKIGEEGDEDDQGADEDQERMEEDGDEEGEGETLKVVVMQDECEEDENEEDEQTSEDAMDTSDHTEEMTERKTPGDNKNIGEHEGNTAAMNGDVK
Protein: Sensor histidine kinase BtsS (EC 2.7.13.3) (P0AD14)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system BtsS/BtsR, which is part of a nutrient-sensing regulatory network composed of BtsS/BtsR, the low-affinity pyruvate signaling system YpdA/YpdB and their respective target proteins, BtsT and YhjX. Responds to depletion of nutrients, specifically serine, and the concomitant presence of extracellular pyruvate. BtsS is a high-affinity receptor for extracellular pyruvate that activates BtsR by phosphorylation. Activation of the BtsS/BtsR signaling cascade also suppresses YpdA/YpdB-mediated yhjX induction.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transcriptional regulatory protein BtsR
- Transcriptional regulatory protein YpdB
- Pyruvate/proton symporter BtsT
- Uncharacterized MFS-type transporter YhjX
- Uncharacterized protein YehS
- Peptide transporter CstA
Sequence:
MYDFNLVLLLLQQMCVFLVIAWLMSKTPLFIPLMQVTVRLPHKFLCYIVFSIFCIMGTWFGLHIDDSIANTRAIGAVMGGLLGGPVVGGLVGLTGGLHRYSMGGMTALSCMISTIVEGLLGGLVHSILIRRGRTDKVFNPITAGAVTFVAEMVQMLIILAIARPYEDAVRLVSNIAAPMMVTNTVGAALFMRILLDKRAMFEKYTSAFSATALKVAASTEGILRQGFNEVNSMKVAQVLYQELDIGAVAITDREKLLAFTGIGDDHHLPGKPISSTYTLKAIETGEVVYADGNEVPYRCSLHPQCKLGSTLVIPLRGENQRVMGTIKLYEAKNRLFSSINRTLGEGIAQLLSAQILAGQYERQKAMLTQSEIKLLHAQVNPHFLFNALNTIKAVIRRDSEQASQLVQYLSTFFRKNLKRPSEFVTLADEIEHVNAYLQIEKARFQSRLQVNIAIPQELSQQQLPAFTLQPIVENAIKHGTSQLLDTGRVAISARREGQHLMLEIEDNAGLYQPVTNASGLGMNLVDKRLRERFGDDYGISVACEPDSYTRITLRLPWRDEA
Protein: C-C chemokine receptor type 9 (C-C CKR-9) (CC-CKR-9) (CCR-9) (Chemokine C-C receptor 10) (CD antigen CDw199) (Q9WUT7)
Organism: Mus musculus (Mouse)
Function: Receptor for chemokine SCYA25/TECK. Subsequently transduces a signal by increasing the intracellular calcium ions level.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P51686}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51686}.
Interaction partners:
- C-C motif chemokine 25
- Mucosal addressin cell adhesion molecule 1
- C-C motif chemokine 19
- Stromal cell-derived factor 1
- Atypical chemokine receptor 4
- C-C motif chemokine 3
- Guanine nucleotide-binding protein G
- C-C motif chemokine 5
- C-C motif chemokine 27
- C-C motif chemokine 1
Sequence:
MMPTELTSLIPGMFDDFSYDSTASTDDYMNLNFSSFFCKKNNVRQFASHFLPPLYWLVFIVGTLGNSLVILVYWYCTRVKTMTDMFLLNLAIADLLFLATLPFWAIAAAGQWMFQTFMCKVVNSMYKMNFYSCVLLIMCISVDRYIAIVQAMKAQVWRQKRLLYSKMVCITIWVMAAVLCTPEILYSQVSGESGIATCTMVYPKDKNAKLKSAVLILKVTLGFFLPFMVMAFCYTIIIHTLVQAKKSSKHKALKVTITVLTVFIMSQFPYNSILVVQAVDAYAMFISNCTISTNIDICFQVTQTIAFFHSCLNPVLYVFVGERFRRDLVKTLKNLGCISQAQWVSFTRREGSLKLSSMLLETTSGALSL
Protein: Twin of eyeless, isoform C (L0MPR7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MMLTTEHIMHGHPHSSVGQSTLFGCSTAGHSGINQLGGVYVNGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIKPRAIGGSKPRVATTPVVQKIADYKRECPSIFAWEIRDRLLSEQVCNSDNIPSVSSINRVLRNLASQKEQQAQQQNESVYEKLRMFNGQTGGWAWYPSNTTTAHLTLPPAASVVTSPANLSGQADRDDVQKRELQFSVEVSHTNSHDSTSDGNSEHNSSGDEDSQMRLRLKRKLQRNRTSFSNEQIDSLEKEFERTHYPDVFARERLADKIGLPEVWFSNRRAKWRREEKMRTQRRSADTVDGSGRTSTANNPSGTTASSSVATSNNSTPGIVNSAINVAERTSSALVLGGEANTTHTSSESPPLQPAAPRLPLNSGFNTMYSSIPQPIATMAENYNSSLGSMTPSCLQQRDAYPYMFHDPLSLGSPYVSAHHRNTACNPSAAHQQPPQHGVYTNSSPMPSSNTGVISAGVSVPVQISTQNVSDLTGSNYWPRLQ
Protein: Amino acid transporter AVT6A (AtAvt6A) (Q9LI61)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable ethanolamine kinase
- Cysteine-rich receptor-like protein kinase 42
- At2g32150/F22D22.10 superfamily protein)
- Probable choline kinase 2
- Probable choline kinase 3
- Probable choline kinase 1
- Nudix hydrolase 8
- Probable galacturonosyltransferase-like 9
- CDP-diacylglycerol--serine O-phosphatidyltransferase 1
- Putative xyloglucan endotransglucosylase/hydrolase protein 13
Sequence:
MTVVGDVAPIPRRNSSTCSNDIAAPLLPECHGDEVAHDEFNGASFSGAVFNLATTIIGAGIMALPATMKILGLGLGITMIVVMAFLTDASIEFLLRFSKAGKNRSYGGLMGGSFGNPGRILLQVAVLVNNIGVLIVYMIIIGDVLAGKTEDGIHHFGVLEGWFGHHWWNGRAAILLITTLGVFAPLACFKRIDSLKFTSALSVALAVVFLIITAGISIMKLISGGVAMPRLLPDVTDLTSFWNLFTVVPVLVTAFICHYNVHSIQNELEDPSQIRPVVRSALMLCSSVYIMTSIFGFLLFGDDTLDDVLANFDTDLGIPFGSILNDAVRVSYALHLMLVFPIVFYPLRINIDGLLFPSARSLSTSNVRFGCLTAGLISVIFLGANFIPSIWDAFQFTGATAAVCLGFIFPASIILKDRHDKATNRDTTLAIFMIVLAVLSNAIAIYSDAYALFKKNAPRE
Protein: Strigolactone esterase D14 (EC 3.1.-.-) (Protein DWARF 14) (Protein DWARF 88) (Protein HIGH-TILLERING DWARF 2) (Q10QA5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in strigolactone (SL) signaling pathway. May function downstream of SL synthesis, as a component of hormone signaling or as an enzyme that participates in the conversion of SL to the bioactive form. Strigolactones are hormones that inhibit tillering and shoot branching through the MAX-dependent pathway, contribute to the regulation of shoot architectural response to phosphate-limiting conditions and function as rhizosphere signal that stimulates hyphal branching of arbuscular mycorrhizal fungi and trigger seed germination of root parasitic weeds. Strigolactone-dependent association of D14 with D3 and D53 (a repressor of SL signaling) triggers D53 ubiquitination and degradation. Hydrolyzes the butenolide ring of SLs. A reaction product D-OH is trapped in the cavity of D14, inducing the interaction with SLR1, and probably with other proteins such as D3 and D53. Contributes to the negative regulation of gibberellin signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24131983}. Nucleus {ECO:0000269|PubMed:24131983, ECO:0000269|PubMed:24616269}. Note=The interaction between D14 and SLR1 takes place in the nucleus (PubMed:24131983). The interaction between D14 and D3 takes place in the nucleus (PubMed:24616269). {ECO:0000269|PubMed:24131983, ECO:0000269|PubMed:24616269}.
Interaction partners:
- Beta-carotene isomerase D27, chloroplastic
- 4-coumarate--CoA ligase
- Carotenoid cleavage dioxygenase 7, chloroplastic
- Os02g0276400 protein
- Os02g0276200 protein
Sequence:
MLRSTHPPPSSPSSSSSGGGGGGGSSASSSSEKTMVGGGGGGGGGSGSAAPSGAKLLQILNVRVVGSGERVVVLSHGFGTDQSAWSRVLPYLTRDHRVVLYDLVCAGSVNPDHFDFRRYDNLDAYVDDLLAILDALRIPRCAFVGHSVSAMIGILASIRRPDLFAKLVLIGASPRFLNDSDYHGGFELEEIQQVFDAMGANYSAWATGYAPLAVGADVPAAVQEFSRTLFNMRPDISLHVCQTVFKTDLRGVLGMVRAPCVVVQTTRDVSVPASVAAYLKAHLGGRTTVEFLQTEGHLPHLSAPSLLAQVLRRALARY
Protein: Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Palmitoyltransferase GLUL) (EC 2.3.1.225) (P15104)
Organism: Homo sapiens (Human)
Function: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine. Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia (By similarity). Essential for proliferation of fetal skin fibroblasts. Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ. Plays a role in ribosomal 40S subunit biogenesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:30158707, ECO:0000269|PubMed:36289327}. Microsome {ECO:0000250|UniProtKB:P09606}. Mitochondrion {ECO:0000250|UniProtKB:P09606}. Cell membrane {ECO:0000269|PubMed:30158707}; Lipid-anchor {ECO:0000269|PubMed:30158707}. Note=Mainly localizes in the cytosol, with a fraction associated with the cell membrane. {ECO:0000269|PubMed:30158707}.
Interaction partners:
- Glutamate dehydrogenase 1, mitochondrial
- Glutaminase liver isoform, mitochondrial
- Glutaminase kidney isoform, mitochondrial
- Glutamate dehydrogenase 2, mitochondrial
- Receptor-interacting serine/threonine-protein kinase 3
- Amidophosphoribosyltransferase
- Carbamoyl-phosphate synthase, mitochondrial
- Multifunctional protein CAD
- Glutamine--fructose-6-phosphate aminotransferase 1
- Glutamine--fructose-6-phosphate aminotransferase 2
Sequence:
MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCLLNETGDEPFQYKN
Protein: Protein FAM229B (Q4G0N7)
Organism: Homo sapiens (Human)
Interaction partners:
- Leucine-rich colipase-like protein 1
Sequence:
MPFQFGTQPRRFPVEGGDSSIELEPGLSSSAACNGKEMSPTRQLRRCPGSHCLTITDVPVTVYATTRKPPAQSSKEMHPK
Protein: Transcription factor CP2 (F8VWL0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU01313}.
Interaction partners:
Sequence:
MLDNRKLGELPEINGKLVKSIFRVVFHDRRLQYTEHQQLEGWRWNRPGDRILDIDIPMSVGIIDPRANPTQLNTVEFLWDPAKRTSVFIQVHCISTEFTMRKHGGEKGVPFRVQIDTFKENENGEYTEHLHSASCQIKVFKPKGADRKQKTDREKMEKRTPHEKEKYQPSYETTILTECSPWPEITYVNNSPSPGFNSSHSSFSLGEGNGSPNHQPEPPPPVTDNLLPTTTPQEAQQWLHRNRFSTFTRLFTNFSGADLLKLTRDDVIQICGPADGIRLFNALKGRMVRPRLTIYVCQESLQLREQQQQQQQQQQKHEDGDSNGTFFVYHAIYLEELTAVELTEKIAQLFSISPCQISQIYKQGPTGIHVLISDEMIQNFQ
Protein: Cytosolic purine 5'-nucleotidase (EC 3.1.3.5) (EC 3.1.3.99) (Cytosolic nucleoside phosphotransferase 5'N) (EC 2.7.1.77) (Q3V1L4)
Organism: Mus musculus (Mouse)
Function: Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside, preferably inosine, deoxyinosine and guanosine. Has the highest activities for IMP and GMP followed by dIMP, dGMP and XMP. Could also catalyze the transfer of phosphates from pyrimidine monophosphates but with lower efficiency. Through these activities regulates the purine nucleoside/nucleotide pools within the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49902}.
Interaction partners:
- 5'
- Cytosolic 5'-nucleotidase 1A
- Deoxycytidine kinase
- Cytosolic 5'-nucleotidase 3A
- Deoxycytidylate deaminase
- Cytosolic 5'-nucleotidase 1B
- 7-methylguanosine phosphate-specific 5'-nucleotidase
- 5'
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
Sequence:
MTTSWSDRLQNAADVPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCDTGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLAPQEITHCHDEDDDEEEEEEE
Protein: Sporulation-specific protein 22 (P40511)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in chromosome segregation during sporulation.
Interaction partners:
- Sporulation-specific protein 16
- Protein ZIP2
- ATP-dependent DNA helicase MER3
- MutS protein homolog 4
- Chromosome stability protein 9
- MutS protein homolog 5
- Synaptonemal complex protein ZIP1
- Meiosis-specific protein HOP1
- Meiotic recombination 1 protein
- Protein ECM11
Sequence:
MSDHNVNSTFRKTLVELCETATWITSQVYAAKNLEKNDLITVDNKISALYPIAEKYDRSFRTTTVILDEELILKLENAASSLWNSLTIAMKAEKASDKYFNEVFCKCKIFATKLLSIHEALFRTNTNLLRNFKCYISSFKSASEYRFDDLITNTQQHSEKYLQIINENVESFSNEEKTEFKKLTFEFYLVNFQLYLSENDLDTANIYTAKVNITDNSKYMDADLLIELCRMIYNSTVMLKEINNPETQLVDVNIISFLKDVEKYLELPVENLKSHTDYSNLKYSVLIFMANCLVEGHPQASELEQCDHYLSLLQNEYPNKVDPFILAINLTKRRNIVNPAETIEEILMRMIMSVDVISNFQAVIASINDLSKMNTKFSIVCLDYLLINKLNSKNDSKFLGKAICSRFLITTQSKTMNDSEIAESLENFSTQMERIVSEPLTKHAISCIITLLWNTGKKLEKMEKYVVSIRFYKLALKDIISQNYSDRGKIQRALQVVYNKIEDYSNTVRVYQDMDEVDRQSPLCQLLMLQSFLADDKTEEALTCLQKIKSSEDEKSTDALILAVAECKRKTDLSVQGLLMIFDKLQSKSNSQTISSTSSSQTLSILRYTLQMIVKVSEEEPLETFINYLPTVQKLLQKAVEFLKTVKLLNQLPPDVEKEAIYQQSVAVNEIEWFASFSYNVAVKCLVDQSCESISEFPQYCIQFIDLIPVQDFTFPKMYHFTYWRFKATILQLIIAKEKAKQDQHQKDWDIYEKSEELVNSINVMKKSSEFKDGSSLEDRNTLHECFLEALTIHLESALMMPDQTRILDILKKTELYQDSRVDALLIDISSNMEDLPKGVLIEILETVLKRNMGPEVKERELCSWLRILLENAINLNHEVELRILDRVLKILNINQSSLQDTDGVLQTELETIATYCWNIGVNYIIKDNKSNGIVWCKHSMGFANMVNEGLQEQLYSLWESLASSANIDINSIAK
Protein: Cytochrome b (Complex III subunit 3) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Ubiquinol-cytochrome-c reductase complex cytochrome b subunit) (P00157)
Organism: Bos taurus (Bovine)
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:1225597, ECO:0000305|PubMed:1327781, ECO:0000305|PubMed:189810}; Multi-pass membrane protein {ECO:0000269|PubMed:12269811, ECO:0000269|PubMed:15312779, ECO:0000269|PubMed:16024040, ECO:0000269|PubMed:16924113, ECO:0000269|PubMed:9204897, ECO:0000269|PubMed:9651245}.
Interaction partners:
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6A2, mitochondrial
- NADH-ubiquinone oxidoreductase chain 5
- NADH-ubiquinone oxidoreductase chain 1
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit 8
- NADH-ubiquinone oxidoreductase chain 4
Sequence:
MTNIRKSHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTFLETWNIGVILLLTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIIMAIAMVHLLFLHETGSNNPTGISSDVDKIPFHPYYTIKDILGALLLILALMLLVLFAPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAFSILILALIPLLHTSKQRSMMFRPLSQCLFWALVADLLTLTWIGGQPVEHPYITIGQLASVLYFLLILVLMPTAGTIENKLLKW
Protein: Photosystem I reaction center subunit XI (PSI subunit V) (PSI-L) (P37277)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Subcellular location: Cellular thylakoid membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I reaction center subunit IX
- Photosystem I reaction center subunit XII
- Photosystem I iron-sulfur center
- Iron stress-induced chlorophyll-binding protein
- Photosystem I reaction center subunit PsaK 1
- Photosystem I reaction center subunit PsaK 2
- Photosystem I reaction center subunit IV
- Photosystem I reaction center subunit VIII
- Photosystem I reaction center subunit III
Sequence:
MAESNQVVQAYNGDPFVGHLSTPISDSAFTRTFIGNLPAYRKGLSPILRGLEVGMAHGYFLIGPWTLLGPLRDSEYQYIGGLIGALALILVATAALSSYGLVTFQGEQGSGDTLQTADGWSQFAAGFFVGGMGGAFVAYFLLENLSVVDGIFRGLFN
Protein: CENP-C-like protein HCP-4 (HoloCentric chromosome binding Protein) (G5EDA3)
Organism: Caenorhabditis elegans
Interaction partners:
- Histone H3-like centromeric protein hcp-3
- Kinetochore protein ndc-80
- HoloCentric chromosome binding Protein
- Kinetochore null protein 2
- HoloCentric chromosome binding Protein
Sequence:
MNRKPRTRSTIVPGRKMITEIVALREAGLDDTRPSYLEEPTVIVDESMMNDSANLEEREWRKQGLSEKQMFAILEKRKQTQLNNARKRLEKEMYGAKTFKELIACREYSECESDSENTVNQNVRSASVFAIPALPKHISEKSMMGSPIANSRGSGKAGLSCSTPKSSSDTSMRSLRSLDISHVVNTDRLDAERVTVHTKSVVIPTILEERESTLQKTLTIEKNHSSQLQKTFTVAEDAPEELQKTVTIEKNQSSEMQRTFTVAKDASKEQSQLQRTVTIEKNQSSQLQGNFTVAKDAPEELQKTVTIEKNQSSEMQGTVTVAKDAEHSSLQKTFTKPTEKDESSLQRTFNVANRDENNDSTLQKTFIIEERDAYEQGTTSVGVKPPVLAQNTMEGGEKRRTSKVTSDERERRNASISNPLHNSMLEKEEIQSPGANFFKHPRKKIRPVVQTPPRIKATSRLSTESNKERTIEMESVAEERTMEADSIGSSYISPTFNASRVSPVPEVPEKVEPMHVSKAATPKSIRHTDNSIRNIGPTNNVECARAALLSTPTRMDIVDSVNRVTPARRYEQPTFASLVKRMNMKDANRLLEETSRKNTPAKTTATTSSAAVRMVLEDDEEDQATEVIEKRSENGGVIVDGEDEAADSSNRSLNIELNALTVNEEPAHDISAIDFPEDDTNEMRSSSDEEEMEARPDPRKKSSRRLGLLSDSIALGLASSSRRRPNDTFVDETWYPEPNSKGNRRPRTHRGMKLKEHQLMKPEDAPDGVRRSTRVRVKPVRSWLGEQPVYVNSPISGCKRLTGVTAVVIKDPRLCYYRTADVRTATERELKDKANKRALAQEKKQQRQNARSGRRHDSDDDEEDDM
Protein: Nitrile hydratase b-subunit homolog (P96453)
Organism: Rhodococcus rhodochrous
Interaction partners:
Sequence:
MPRLNEQPHPGLEANLGDLVQNLPFNERIPRRSGEVAFDQAWEIRAFSIATALHGQGRFEWDEFQSRLIESIKQWEAEHATTEQWSYYERWMLALEELLHDKGFVAGEELAHRTEQVLATPAGAHHQHAVRDPIAVHAIGTRTTDSDG
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3 (Transducin beta chain 3) (P16520)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MGEMEQLRQEAEQLKKQIADARKACADVTLAELVSGLEVVGRVQMRTRRTLRGHLAKIYAMHWATDSKLLVSASQDGKLIVWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNMCSIYNLKSREGNVKVSRELSAHTGYLSCCRFLDDNNIVTSSGDTTCALWDIETGQQKTVFVGHTGDCMSLAVSPDFNLFISGACDASAKLWDVREGTCRQTFTGHESDINAICFFPNGEAICTGSDDASCRLFDLRADQELICFSHESIICGITSVAFSLSGRLLFAGYDDFNCNVWDSMKSERVGILSGHDNRVSCLGVTADGMAVATGSWDSFLKIWN
Protein: 5-aminovalerate aminotransferase DavT (EC 2.6.1.48) (5-aminovalerate transaminase) (Delta-aminovalerate aminotransferase) (Q9I6M4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the conversion of 5-aminovalerate to 5-oxopentanoate.
Interaction partners:
- Glutarate-semialdehyde dehydrogenase
- Probable aldehyde dehydrogenase
- Guanidinobutyrase
- Probable aldehyde dehydrogenase
- aldehyde dehydrogenase
- Putrescine--pyruvate aminotransferase
- Probable glutamine synthetase
- FAD dependent oxidoreductase domain-containing protein
- Probable glutamine synthetase
Sequence:
MSKTNESLLKRRQAAVPRGVGQIHPVVAERAENSTVWDVEGREYIDFAGGIAVLNTGHLHPKVIAAVQEQLGKLSHTCFQVLAYEPYIELAEEIAKRVPGDFPKKTLLVTSGSEAVENAVKIARAATGRAGVIAFTGAYHGRTMMTLGLTGKVVPYSAGMGLMPGGIFRALAPCELHGVSEDDSIASIERIFKNDAQPQDIAAIIIEPVQGEGGFYVNSKSFMQRLRALCDQHGILLIADEVQTGAGRTGTFFATEQLGIVPDLTTFAKSVGGGFPISGVAGKAEIMDAIAPGGLGGTYAGSPIACAAALAVLKVFEEEKLLERSQAVGERLKAGLREIQAKHKVIGDVRGLGSMVAIELFEGGDTHKPAAELVSKIVVRAREKGLILLSCGTYYNVIRFLMPVTIPDAQLEKGLAILAECFDELA
Protein: Derlin-2 (Degradation in endoplasmic reticulum protein 2) (DERtrin-2) (Der1-like protein 2) (F-LAN-1) (F-LANa) (Q9GZP9)
Organism: Homo sapiens (Human)
Function: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins. May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:16449189}; Multi-pass membrane protein {ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:16449189}.
Interaction partners:
- Protein sel-1 homolog 1
- Protein OS-9
- E3 ubiquitin-protein ligase synoviolin
- FAS-associated factor 2
- E3 ubiquitin-protein ligase AMFR
- Transitional endoplasmic reticulum ATPase
- Lipid droplet-regulating VLDL assembly factor AUP1
- Endoplasmic reticulum lectin 1
- Derlin-1
- Selenoprotein S
Sequence:
MAYQSLRLEYLQIPPVSRAYTTACVLTTAAVQLELITPFQLYFNPELIFKHFQIWRLITNFLFFGPVGFNFLFNMIFLYRYCRMLEEGSFRGRTADFVFMFLFGGFLMTLFGLFVSLVFLGQAFTIMLVYVWSRRNPYVRMNFFGLLNFQAPFLPWVLMGFSLLLGNSIIVDLLGIAVGHIYFFLEDVFPNQPGGIRILKTPSILKAIFDTPDEDPNYNPLPEERPGGFAWGEGQRLGG