wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase srb10 (EC 2.7.11.22) (EC 2.7.11.23) (Cyclin-dependent kinase 8) (Suppressor of RNA polymerase B srb10) (O13958)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic component of the Cdk8 module/Srb8-11 module which is a regulatory module of the Mediator complex that regulates basal RNA polymerase II transcription. The Cdk8 module may sterically hinder the interaction between Mediator and RNA polymerase II leading to transcriptional repression of a subset of genes regulated by Mediator.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 12
- RNA polymerase II holoenzyme cyclin-like subunit
- Mediator of RNA polymerase II transcription subunit 13
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 21
Sequence:
MKDGYKIIGFISSGTYGKVYKAVSSNSNDKRLFAIKKFKAESKQVSSNAQQTGVSQSAIREMMLCREIQHENIVSLVQVLLKDGTISMVFEYAEHDLLQIIHFHSRSRTRQIPPSILKSILWQIINGVAYLHENWIMHRDLKPANIMITATGKVKIGDLGLGRLIRDPILPFYSSDRVVVTIWYRAPELLLGAHDYTPAIDVWAIGCIYGEMLALSPLFKGDEIKMEDKKVVPFQSTQMLRIMELLGTPTEERWPGLKNYPEYYQLSSFEVRYWNNLLPQWYQTVKNRDPQGLDLLMKMLQYDPKSRITAKQALEHVFFTSDKLWTTSPFLNQPIHYPERRISEDDSEVSSKRVLSTSLRSESKRFKGN
Protein: Regulator of G-protein signaling 1 (RGS1) (B-cell activation protein BL34) (Early response protein 1R20) (Q08116)
Organism: Homo sapiens (Human)
Function: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the N-formylpeptide chemoattractant receptors and leukotriene receptors. Inhibits B cell chemotaxis toward CXCL12 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10480894}; Peripheral membrane protein {ECO:0000269|PubMed:10480894}; Cytoplasmic side {ECO:0000269|PubMed:10480894}. Cytoplasm, cytosol {ECO:0000269|PubMed:10480894}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Early activation antigen CD69
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- T-cell activation Rho GTPase-activating protein
- Guanine nucleotide-binding protein subunit alpha-12
Sequence:
MRAAAISTPKLDKMPGMFFSANPKELKGTTHSLLDDKMQKRRPKTFGMDMKAYLRSMIPHLESGMKSSKSKDVLSAAEVMQWSQSLEKLLANQTGQNVFGSFLKSEFSEENIEFWLACEDYKKTESDLLPCKAEEIYKAFVHSDAAKQINIDFRTRESTAKKIKAPTPTCFDEAQKVIYTLMEKDSYPRFLKSDIYLNLLNDLQANSLK
Protein: T-complex protein 1 subunit gamma (Q8I5C4)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- CCT-beta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit zeta
- Phosducin-like protein 1, putative
- Prefoldin subunit 5, putative
- Serine/threonine-protein phosphatase
Sequence:
MLKNPGTVLVFKPNTKREEGRKTQLSNIQASRAVSDIVKTTLGPMAMLKMMLDPLGGIVITNDGNCILREVDVAHPAAKSLIELSRSQDEEVGDGTTSVVILSGELLSVAETFLRQNIHPTIIVNCYMNALDSSLKFLEEISIDIDVNSESDLLKAIDSCLSTKFVNRYNKIVSKLALEATRCVKMDNLMGRKEIDIKRYAKVEKIPGGDITDSYVLKGVMINKDITHPKMRRYIKNPRILLLDCTLEYKKAESQTNVEILDEKTWNELLLQEEIEVKKMCEYIIDSKCDIVITEKGVSDLAQHFLVKKNISVIRRVRKTDLNRLERISGATIVNRCEEIVEGDIGTKCGLFEIKKIGDDYYSFFVECKDPHACTILLRGSTKDVLNEIERNLHDGMNVAKNILMEGKLLYGGGCTEIRVGQYLIKEAAKFNDSRKSITEAVASALEIIPKILAQNSGVNVVKTMNELRIKHEQEGGQEFGIDGITGDIIKVTTKNIWDLLSVKKQIYKSAIEAASMILRIDDVVSGVGKDEKVQKTIKNEF
Protein: Small ribosomal subunit protein uS2 (40S ribosomal protein SA) (Q55BY1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03015}.
Interaction partners:
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein uL30
- Small ribosomal subunit protein uS5
Sequence:
MTQFPAALNPHQDDILKMLACQTHLGGNNVDVEMESYTWKRKDNGHFIINLAKTWEKIQLAARVIVAIENPADISVISAKPLGQRAVLKFANFIGATAFSGRFTPGTFTNQIQSKFTEPRLLIVADPLLDKQPLMEASYVNIPTIALCDTTSCLDGVDIAIPCNNRGKNSIALMFWLLAREVLYLRGTIPRNTTWSVKVDLFIYRDTDEEPEKEKTAAVAAAPVAAVEAVEFTQQPIAEWSAPDN
Protein: Metallothionein-4 (MT-4) (Metallothionein-IV) (MT-IV) (P47945)
Organism: Mus musculus (Mouse)
Function: Seems to bind zinc and copper. Could play a special role in regulating zinc metabolism during the differentiation of stratified epithelia.
Interaction partners:
- Metallothionein-3
Sequence:
MDPGECTCMSGGICICGDNCKCTTCSCKTCRKSCCPCCPPGCAKCARGCICKGGSDKCSCCP
Protein: Receptor protein kinase TMK1 (EC 2.7.11.1) (BARK1-like kinase 1) (Transmembrane kinase 1) (P43298)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transmembrane kinase receptor. Phosphorylates only serine and threonine residues. Involved in auxin signal transduction and cell expansion and proliferation regulation. Forms with ABP1 a cell surface auxin perception complex that activates ROP signaling pathways. Required for auxin promotion of pavement cell interdigitation. Auxin promotes the formation of the ABP1-TMK1 protein complex.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23613767, ECO:0000269|PubMed:24578577}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Auxin-binding protein 1
- Rac-like GTP-binding protein ARAC3
- Rac-like GTP-binding protein ARAC4
- CRIB domain-containing protein RIC4
- Probable membrane-associated kinase regulator 2
- Auxin-responsive protein IAA32
Sequence:
MKKRRTFLLFSFTFLLLLSLSKADSDGDLSAMLSLKKSLNPPSSFGWSDPDPCKWTHIVCTGTKRVTRIQIGHSGLQGTLSPDLRNLSELERLELQWNNISGPVPSLSGLASLQVLMLSNNNFDSIPSDVFQGLTSLQSVEIDNNPFKSWEIPESLRNASALQNFSANSANVSGSLPGFLGPDEFPGLSILHLAFNNLEGELPMSLAGSQVQSLWLNGQKLTGDITVLQNMTGLKEVWLHSNKFSGPLPDFSGLKELESLSLRDNSFTGPVPASLLSLESLKVVNLTNNHLQGPVPVFKSSVSVDLDKDSNSFCLSSPGECDPRVKSLLLIASSFDYPPRLAESWKGNDPCTNWIGIACSNGNITVISLEKMELTGTISPEFGAIKSLQRIILGINNLTGMIPQELTTLPNLKTLDVSSNKLFGKVPGFRSNVVVNTNGNPDIGKDKSSLSSPGSSSPSGGSGSGINGDKDRRGMKSSTFIGIIVGSVLGGLLSIFLIGLLVFCWYKKRQKRFSGSESSNAVVVHPRHSGSDNESVKITVAGSSVSVGGISDTYTLPGTSEVGDNIQMVEAGNMLISIQVLRSVTNNFSSDNILGSGGFGVVYKGELHDGTKIAVKRMENGVIAGKGFAEFKSEIAVLTKVRHRHLVTLLGYCLDGNEKLLVYEYMPQGTLSRHLFEWSEEGLKPLLWKQRLTLALDVARGVEYLHGLAHQSFIHRDLKPSNILLGDDMRAKVADFGLVRLAPEGKGSIETRIAGTFGYLAPEYAVTGRVTTKVDVYSFGVILMELITGRKSLDESQPEESIHLVSWFKRMYINKEASFKKAIDTTIDLDEETLASVHTVAELAGHCCAREPYQRPDMGHAVNILSSLVELWKPSDQNPEDIYGIDLDMSLPQALKKWQAYEGRSDLESSTSSLLPSLDNTQMSIPTRPYGFAESFTSVDGR
Protein: Selenocysteine insertion sequence-binding protein 2 (SECIS-binding protein 2) (Q3U1C4)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9QX72}. Nucleus {ECO:0000250|UniProtKB:Q9QX72}.
Interaction partners:
- Selenocysteine-specific elongation factor
- tRNA selenocysteine 1-associated protein 1
- Large ribosomal subunit protein eL30
- L-seryl-tRNA
- O-phosphoseryl-tRNA
- Thioredoxin reductase-like selenoprotein T
- Selenide, water dikinase 2
- Selenoprotein N
- Eukaryotic initiation factor 4A-III
- Thioredoxin reductase 1, cytoplasmic
Sequence:
MASERPREPDGEDSIKLSADVKPFVPKFAGLNVAWSESSETRVFPGCAATYYPFVQEPPAAEQKMYPEDMAFGAPTFPAQYVSSEIALHPFAYPTYTLESAQSVCSVPTLQYDYSQARCHPGFRTAKPRHEHVCPPPQEAKGVFKKKPSDERRACEEQKSSSRRADNAVPCEARPARGSSHLSSRTESSLKSDGYHKRPDRKSRILAKSASTSKPEFEFSRLDFPELQSPKNSNMPETQKPPRWGPLGPAASNMPLLGDVGKPVADMVEGKMVKSDHTDGAVTSNATTSSPSCTQELSWTPMGYIVRQTVSSDSAAATENVTSMINLKKTTSSADAKNVSVTSEALSSNPSYNREKRVYPAPKAKASQGGELEQNESSKKNKKKKEKSKPSYEVLTVQEPPRIEDAEEFPNLSVASERRHRGQSPKLHSKQQTQNEFKTSGKKSQVPVQLDLGGMLAALEKQQQQQHASHAKPSSRPVVFSVGAVPVLSKDASSSERGRRSSQMKTPHNPLDSSAPLMKKGKQREIPKAKKPTSLKKIILKERQERMQQRLQESAVSLTVASDDSQDVESGASNQTPSQDNPTGPEKTEESVSSTPVVEGESEEPAGTEFQRDPEACQPAPDSATFPKIHSRRFRDYCSQMLSKEVDACVTGLLKELVRFQDRMYQKDPVKAKTKRRLVLGLREVLKHLKLRKLKCIIISPNCEKTQSKGGLDDTLHTIIDCACEQNIPFVFALNRKALGRSLNKAVPVSIVGIFSYDGAQDQFHKMVELTMAARQAYKTMLETMRQEQAGEPGPQSPPSPPMQDPIPSTEEGTLPSTGEEPHYIEIWKKHLEAYSQRALELEDSLEASTSQMMNLNL
Protein: Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR1 (Mitochondrial genome-required protein 1) (P25573)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial inner membrane i-AAA protease supercomplex required for mitochondrial inner membrane protein turnover. Together with MGR3, functions in an adapter complex that targets substrates to the i-AAA protease for degradation. Required for growth of cells lacking the mitochondrial genome.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16267274}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16267274}.
Interaction partners:
- Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR3
- Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1
- Mitochondrial inner membrane m-AAA protease component YTA10
- Protein MRG3-like
Sequence:
MAVFTPPSGNSNSTDHTHTQDDHDKDDNDIKKFYIRPSLGLKLWGPLVPAPDNLPGLYTLITIQSAVGFFALWRLRRLYKLPPPRRIATGTHSDLSFGELPSEMIVNGKTKIKKDIADFPTLNRFSTTHGDIVLAPPPIIPRQSRFVSVRKLLWGLFGSLLLSQSLLELTRLNFLKYDPWCDEMKSVRDKKFFNNIVKYYHEGIDPTKIKVKDAMNGTPLSTNIPEVKQSVALARAQVEAQNPIIKWFGPLEYKPMSFNEYLNRMEFHLDMFEFFQNKRNIRENSIELINSISHNPQSSSTGLEGLSESKKLHLQNVEKRLHFLASSGDSISAPVKKRSSTTLSRGVILPHDTKGPQDIDLDTIRSLYDPWMTLALETSLSIKFIPTTMPSHTKTPTSTDQPLPGPTPKALTNEKTH
Protein: Secreted effector protein SseB (Secretion system effector B) (Q7BVH7)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. May act as a translocator that mediates translocation of SPI-2 TTSS effector proteins from intraphagosomal bacterial cells into the host cells. SseB is required for correct localization of SseC and SseD on the bacterial cell surface.
Subcellular location: Secreted {ECO:0000269|PubMed:11567004}. Cell surface {ECO:0000269|PubMed:11567004}. Note=Secreted via type III secretion system 2 (SPI-2 T3SS). After secretion, localizes mainly on the surface of the bacterial cell.
Interaction partners:
- Secretion system chaparone
- Type III secretion system chaperone SseA
- Secretion system apparatus lipoprotein SsaJ
- SPI-2 type 3 secretion system translocon protein SctB
- Secretion system apparatus protein SsaL
- Secretion system effector
- Secretion system apparatus protein
- Type 3 secretion system secretin
- SPI-2 type 3 secretion system translocon protein SctE
- SPI-2 type 3 secretion system ATPase
Sequence:
MSSGNILWGSQNPIVFKNSFGVSNADTGSQDDLSQQNPFAEGYGVLLILLMVIQAIANNKFIEVQKNAERARNTQEKSNEMDEVIAKAAKGDAKTKEEVPEDVIKYMRDNGILIDGMTIDDYMAKYGDHGKLDKGGLQAIKAALDNDANRNTDLMSQGQITIQKMSQELNAVLTQLTGLISKWGEISSMIAQKTYS
Protein: Beta-mammal toxin Co2 (C0HLF3)
Organism: Centruroides ornatus (Scorpion) (Centruroides infamatus ornatus)
Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin acts on human Nav1.1/SCN1A, Nav1.2/SCN2A, Nav1.4/SCN4A and Nav1.6/SCN8A voltage-gated sodium channels. Also, it reduces the peak of sodium currents in Nav1.5/SCN5A at all potentials. In vivo, is lethal to mice when intraperitoneally injected at a dose of 5ug. No activity is observed when injected into crickets or woodlice.
Subcellular location: Secreted {ECO:0000269|PubMed:31734253}.
Interaction partners:
Sequence:
KEGYIVNYHDGCKYACVKLGDNDYCLRECKLRYGKGAGGYCYAFGCWCTHLYEQAVVWPLPKKRCN
Protein: CCHC-type zinc finger, nucleic acid-binding protein b (E7FCQ0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Muscleblind-like protein 3 isoform X2
- Muscleblind-like-splicing regulator 1.
- Uncharacterized protein
- SERPINE1 mRNA-binding protein 1 isoform X1
- Heterogeneous nuclear ribonucleoprotein K
Sequence:
MSSNECFGCGRTGHWIKNCPNAGRGRGKGRGRGKDLFCYRCGEPGHVARDCERTEDACYNCGRGGHISRDCKEPKKEREQVCYNCGKAGHMARDCDHANEQKCYSCGGFGHIQKGCEKVKCYRCGEIGHVAVQCSKASEVNCYNCGKSGHVAKECTIEATA
Protein: Transketolase-like protein 2 (EC 2.2.1.1) (Q9H0I9)
Organism: Homo sapiens (Human)
Function: Plays an essential role in total transketolase activity and cell proliferation in cancer cells; after transfection with anti-TKTL1 siRNA, total transketolase activity dramatically decreases and proliferation was significantly inhibited in cancer cells. Plays a pivotal role in carcinogenesis.
Interaction partners:
- Transaldolase
- Glucose-6-phosphate isomerase
- Ribulose-phosphate 3-epimerase-like protein 1
- Ribose-5-phosphate isomerase
- Ribulose-phosphate 3-epimerase
- Thiamine pyrophosphokinase 1
- Fructose-1,6-bisphosphatase 1
- Fructose-1,6-bisphosphatase isozyme 2
- Glyceraldehyde-3-phosphate dehydrogenase
- ATP-dependent 6-phosphofructokinase, muscle type
Sequence:
MMANDAKPDVKTVQVLRDTANRLRIHSIRATCASGSGQLTSCCSAAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWVEVGDISESDLLNLRKLHSDLERHPTPRLPFVDVATGSLGQGLGTACGMAYTGKYLDKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDVNRLGQSGPAPLEHGADIYQNCCEAFGWNTYLVDGHDVEALCQAFWQASQVKNKPTAIVAKTFKGRGIPNIEDAENWHGKPVPKERADAIVKLIESQIQTNENLIPKSPVEDSPQISITDIKMTSPPAYKVGDKIATQKTYGLALAKLGRANERVIVLSGDTMNSTFSEIFRKEHPERFIECIIAEQNMVSVALGCATRGRTIAFAGAFAAFFTRAFDQLRMGAISQANINLIGSHCGVSTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAANTKGMCFIRTSQPETAVIYTPQENFEIGQAKVVRHGVNDKVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIISSAKATGGRVITVEDHYREGGIGEAVCAAVSREPDILVHQLAVSGVPQRGKTSELLDMFGISTRHIIAAVTLTLMK
Protein: POU domain, class 3, transcription factor 3 (Brain-specific homeobox/POU domain protein 1) (Brain-1) (Brn-1) (Q63262)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that acts synergistically with SOX11 and SOX4. Plays a role in neuronal development. Is implicated in an enhancer activity at the embryonic met-mesencephalic junction; the enhancer element contains the octamer motif (5'-ATTTGCAT-3') (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00530, ECO:0000269|PubMed:9632656}.
Interaction partners:
- Transcription factor SOX-11
Sequence:
MATAASNPYLPGNSLLAAGSIVHSDAAGAGGGGGGGGGGGGGAGGGGGGMQPGSAAVTSGAYRGDPSSVKMVQSDFMQGAMAASNGGHMLSHAHQWVTALPHAAAAAAAAAAAAVEASSPWSGSAVGMAGSPQQPPRPPPPPPQGPDVKGGVGREDLHAGTALHHRGPPHLGPPPPPPHQGHPGGWGAAAAAAAAAAAAAAAAHLPSMAGGQQPPPQSLLYSQPGGFTVNGMLSAPPGPGGGGGGAGGGAQSLVHPGLVRGDTPELAEHHHHHHHHAHPHPPHPHHAQGPPHHGGGGAGPGLNSHDPHSDEDTPTSDDLEQFAKQFKQRRIKLGFTQADVGLALGTLYGNVFSQTTICRFEALQLSFKNMCKLKPLLNKWLEEADSSTGSPTSIDKIAAQGRKRKKRTSIEVSVKGALESHFLKCPKPSAQEITNLADSLQLEKEVVRVWFCNRRQKEKRMTPPGIQQQTPDDVYSQVGTVSADTPPPHHGLQTSVQ
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (E2CWF0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Calcineurin subunit B type 2
- Calcineurin subunit B type 1
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Nuclear factor of activated T-cells 1
- Glycogen synthase kinase-3 beta
- Nuclear factor of activated T-cells, cytoplasmic 3
- Protein phosphatase 3 catalytic subunit alpha
Sequence:
MSGRRPQFSTTERVIKAVPFPPTRRLTLKEVFENGKPKMDVLKNHLVKEGRVEEDVALKIINDGAAILKQEKTMLEVEAPITVCGDVHGQFFDLMKLFEVGGSPSNTRYLFLGDYVDRGYFSIECVLYLWSLKINHPKTLFLLRGNHECRHLTEYFTFKQECRIKYSELVYEACMHTFDCLPLAALLNQQFLCVHGGMSPEITCLDDIRKLDRFAEPPAFGPVCDLLWSDPLEDYGSEKTLEHYTHNTVRGCSYFFSYPAVCEFLQNNSLLSIIRAHEAQDAGYRMYRKNQATGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNILNICSDEEMSLVEEEDHYISSCPKGATSVRKEVIRNKIRAIGKMARVFTVLREESENVLILKGLTPTGTLPLGVLSGGKQTIETAKLQAAEEREAIRGFTIAHRIRSFEEARGLDRINERMPPRKEASYHHDAGKTHPHPSKRSDHGKKAL
Protein: DNA ligase (EC 6.5.1.1) (A0A096MKE9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTLAFKTLFPRNLCALGRKELCLFSEQHHWPAIRQFSQWSETNLLCGCCLLQRRKPVLSFQRGHLRPRATHLISWSGSHVGLCTGPCEMAEQRFCVDYAKRGTAGCKKCKEKIVKGVCRIGKVVPNPFSESGGDMKEWYHIKCMFEKLERARATTKKIEDLTELEGWEELEDNEKEQISQHIADLSSKTAATPKKKATVQAKLTTTGQVTSPVKGASFITSTNPRKFSGFSAAKPNNSEQDPSSPAPKTSLSASKCDPKHKDCLLREFRKLCAMVAENPSYNTKTQIIHDFLQKGSTGDGFRGDVYLTVKLLLPGVIKSVYNLNDKQIVKLFSRIFNCNPDDMARDLEQGDVSETIRVFFEQSKSFPPAAKSLLTIQEVDAFLLHLSKLTKEDEQQQALQDIASRCTANDLKCIIRLIKHDLKMNSGAKHVLDALDPNAYEAFKASRNLQDVVERVLHNEQEVEKDPGRRRALSVQASLMTPVQPMLAEACKSIEYAMKKCPNGMFSEIKYDGERVQVHKKGDHFSYFSRSLKPVLPHKVAHFKDYIPKAFPGGQSMILDSEVLLIDNNTGKPLPFGTLGVHKKAAFQDANVCLFVFDCIYFNDVSLMDRPLCERRKFLHDNMVEIRNRIMFSEMKQVTKASDLADMINRVIREGLEGLVLKDVKGTYEPGKRHWLKVKKDYLNEGAMADTADLVVLGAFYGQGSKGGMMSIFLMGCYDPDSQKWCTVTKCAGGHDDATLARLQKELDMVKISKDPSKIPSWLKINKIYYPDFIVPDPKKAAVWEITGAEFSRSEAHTADGISIRFPRCTRIRDDKDWKSATNLPQLKELYQLSKDKADFAVVAGDEGSSTTGGSNGEKLAVKSSPVKVGMKRKAADETPGLTKALLDVFTGVRLYLPPSTPDFRRLKRYFVAFNGDLVQEFDMASATHVLGNRDKNTDAQLVSSEWIWACIRKRRLVAPC
Protein: p-hydroxybenzoic acid--AMP ligase FadD22 (p-HB--AMP ligase FadD22) (EC 6.2.1.50) (p-hydroxybenzoic acid-AMP synthetase) (p-HB-AMP synthetase) (B2HIL6)
Organism: Mycobacterium marinum (strain ATCC BAA-535 / M)
Function: Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22. This intermediate primes the biosynthesis of the phenolphthiocerol (PPOL) by presenting the pHBA starter unit for elongation by Pks15/1. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B).
Interaction partners:
- Phenolphthiocerol synthesis polyketide synthase type I Pks15/1
- Phenolpthiocerol synthesis type-I polyketide synthase PpsA
- Medium/long-chain-fatty-acid--CoA ligase FadD17
- Fatty-acid-CoA ligase FadD1
Sequence:
MRNENVAGLLAERASEAGWTDQPAYYAPDVVTHGQIHDGAARLGAVLANRGLCRGDRVLLCMPDSPELVQVLLACLARGILAFLANPELHRDDHAFQERDTQAALVITSGPLCDRFAPSTVVDAADLFSEAARVGPADYEILGGDAAAYATYTSGTTGPPKAAIHRHCDVFAFVEAMCRNALRLTPADIGLSSARMYFAYGLGNSVWFPLATGSSAVVNPLPVGAEVAATLSARFEPSVLYGVPNFFARVVDACSADSFRSVRCVVSAGEALEVGLAERLTEFFGGIPILDGVGSTEVGQTFVSNTVDEWRPGSLGKVLPPYQIRVVAPDGAAAGPGVEGDLWVRGPSIAESYWNWPEPLLTDEGWLDTRDRVCIDDDGWVTYACRADDTEIVGAVNINPREIERLIVEEDAVAEVAVVGVKEATGASTLQAFLVPASAEGIDGSVMRDIHRRLLTRLSAFKVPHRFAVVERLPRTANGKLLRSALRGQTPAKPIWELASAEHRSGAPGQLDDQSASALVSGSREVSLKERLAALQQERHRLVLDAVCGETAKMLGEPDPRSVNRDLAFSELGFDSQMTVELCHRLAAATGLRVPETVGWDYGSISGLAQYLEAELSGADRRVTPQSARSGARALPLIEAQLNKVEELTAAIADGEKPRVAERLRALLGTITEGQEHWGQRIAAASTPDEIFQLIDSEFGES
Protein: Sterile alpha motif domain containing 8 (A0A5F9ZGS6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPARSRHRPRLHSGSPPRAPPPPLEALHSGEAGRAPDSDGGSDADSEVGPGSPTRTAEAAEEEMAGPNQLCIRRWTTKHVAVWLKDEGFFEYVDILCNKHRLDGITLLTLTEYDLRSPPLEIKVLGDIKRLMLSVRKLQKIHIDVLEEMGYNSDSPMGSMTPFISALQSTDWLCNGELSHDCDGPITDLNSDQYQYMNGKNKHSVRRLDPEYWKTILSCIYVFIVFGFTSFIMVIVHERVPDMQTYPPLPDIFLDSVPRIPWAFAMTEVCGMILCYIWLLVLLLHKHRSILLRRLCSLMGTVFLLRCFTMFVTSLSVPGQHLQCTGKIYGSVWEKLHRAFAIWSGFGMTLTGVHTCGDYMFSGHTVVLTMLNFFVTEYTPRSWNFLHTLSWVLNLFGIFFILAAHEHYSIDVFIAFYITTRLFLYYHTLANTRAYQQSRRARIWFPMFSFFECNVNGTVPNEYCWPFSKPAIMKRLIG
Protein: Phospholipase A1 PLIP2, chloroplastic (EC 3.1.1.32) (Galactolipase PLIP2) (EC 3.1.1.26) (Protein PLASTID LIPASE 2) (F4HXL0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sn-1-specific phospholipase A1 that catalyzes the initial step of oxylipins and jasmonate (JA) biosynthesis. Hydrolyzes polyunsaturated acyl groups preferentially from chloroplastic monogalactosyldiacylglycerol (MGDG). May function downstream of abscisic acid (ABA) and provide a link between ABA-mediated abiotic stress responses and oxylipin and JA signalings. In vitro, possesses broad substrate specificity. Can hydrolyze the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), the sulfolipid sulfoquinovosyldiacylglycerol (SQDG), and the phoshpolipids phosphatidylcholine (PC), and phosphatidylglycerol (PG).
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:29666162}; Peripheral membrane protein {ECO:0000305}. Plastid, chloroplast stroma {ECO:0000269|PubMed:29666162}.
Interaction partners:
- Alpha/beta-Hydrolases superfamily protein
- At2g31940/F20M17.2
- Phospholipase A1-Ibeta2, chloroplastic
- Lipase class 3 family protein
- Triacylglycerol lipase 1
- Lipid phosphate phosphatase epsilon 1, chloroplastic
- Probable carboxylesterase 16
Sequence:
MDSLCLNSGLHGVIPAITAVGNGGCGGVVEVRATASAPSQKRGPFGFSFKYPLTPFWSRGGGGGIASRRRSGLCLDDAVLVDSGDSRKPIAEETAVEMDTERRNGSWVLKILDVQSTWKHEEEEDDDEVEDEDGDEDEEVELDDAVVSEDDGGCDVCSVLEDDGNEANKFQLDRESFSKLLRRVTLPESKLYAQLSYLGNLAYSISKIKPANLSKYYGLRFVTSSAEKTESALKAENGEVSGETKPIVEAEEEVEEEEKNKSRKISASAAYEIVASAASYLHSRTNNILPFNSSSKAENSDKHDVNLTNAESSSDVAYSVTSVVAAEEDVKQAVADDLKSTISSPCDWFICDDDQSHTRFVVIQGSESLASWQANLLFEPIEFEGLGAIVHRGIYEAAKGMYEQMLPEVKAHIKTHGTSAKFRFTGHSLGGSLSLLLNLMLLVRGEVPASSLLPVITYGAPFVLCGGDRLLKKLGLPKSHVQAIVMHRDIVPRAFSCNYPYHVAELLKAVNGNFRSHPCLNKQSMLYSPMGELLILQPDETFSPGHELLPSGNGLYLLTSDFESPDIEDSDEERLRAAQTVFLNTPHPLDILSDRSAYGSSGTIQRDHDMNSYLKAVRSVIRKEVNQIRRAKREHRRSLWWPILVARESGSSGIAVSNGQINGQDFSGMMQTGRKSLQRFSRLVASQHMPLIVVMLFPVKLLFLGAFNVFSFR
Protein: Probable phospholipid-transporting ATPase IIB (EC 7.6.2.1) (ATPase class II type 9B) (O43861)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21914794}; Multi-pass membrane protein {ECO:0000269|PubMed:21914794}. Note=Efficient exit from the endoplasmic reticulum does not require TMEM30A, nor TMEM30B.
Interaction partners:
Sequence:
MADQIPLYPVRSAAAAAANRKRAAYYSAAGPRPGADRHSRYQLEDESAHLDEMPLMMSEEGFENEESDYHTLPRARIMQRKRGLEWFVCDGWKFLCTSCCGWLINICRRKKELKARTVWLGCPEKCEEKHPRNSIKNQKYNVFTFIPGVLYEQFKFFLNLYFLVISCSQFVPALKIGYLYTYWAPLGFVLAVTMTREAIDEFRRFQRDKEVNSQLYSKLTVRGKVQVKSSDIQVGDLIIVEKNQRIPSDMVFLRTSEKAGSCFIRTDQLDGETDWKLKVAVSCTQQLPALGDLFSISAYVYAQKPQMDIHSFEGTFTREDSDPPIHESLSIENTLWASTIVASGTVIGVVIYTGKETRSVMNTSNPKNKVGLLDLELNRLTKALFLALVALSIVMVTLQGFVGPWYRNLFRFLLLFSYIIPISLRVNLDMGKAVYGWMMMKDENIPGTVVRTSTIPEELGRLVYLLTDKTGTLTQNEMIFKRLHLGTVSYGADTMDEIQSHVRDSYSQMQSQAGGNNTGSTPLRKAQSSAPKVRKSVSSRIHEAVKAIVLCHNVTPVYESRAGVTEETEFAEADQDFSDENRTYQASSPDEVALVQWTESVGLTLVSRDLTSMQLKTPSGQVLSFCILQLFPFTSESKRMGVIVRDESTAEITFYMKGADVAMSPIVQYNDWLEEECGNMAREGLRTLVVAKKALTEEQYQDFESRYTQAKLSMHDRSLKVAAVVESLEREMELLCLTGVEDQLQADVRPTLEMLRNAGIKIWMLTGDKLETATCIAKSSHLVSRTQDIHIFRQVTSRGEAHLELNAFRRKHDCALVISGDSLEVCLKYYEHEFVELACQCPAVVCCRCSPTQKARIVTLLQQHTGRRTCAIGDGGNDVSMIQAADCGIGIEGKEGKQASLAADFSITQFRHIGRLLMVHGRNSYKRSAALGQFVMHRGLIISTMQAVFSSVFYFASVPLYQGFLMVGYATIYTMFPVFSLVLDQDVKPEMAMLYPELYKDLTKGRSLSFKTFLIWVLISIYQGGILMYGALVLFESEFVHVVAISFTALILTELLMVALTVRTWHWLMVVAEFLSLGCYVSSLAFLNEYFGIGRVSFGAFLDVAFITTVTFLWKVSAITVVSCLPLYVLKYLRRKLSPPSYCKLAS