wanglab/gogpt-training-data huggingface dataset:
Protein: sn-1-specific diacylglycerol lipase (EC 3.1.1.116) (X2JBS2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MPGLVVFRRRWSVGSDDLVVPGAFLLTIHFICFVIVSVSLVIFEYNTRILSVKLLFYHLIGYLLILFFSICVEIGICVISMRGSILDAEARTSINIWIYLKSLVILFDIAWLAVGSVWLGHYYTTAPIDDPKKVYIAIIICNWALVVITLITIWCTFDAAGRSWVKMKKYQRSMRETESRFNYKRSNSMNRNWRQRKVMRAYQDSWDHRCRLLFCCMGSSERNRNSFTDIARLLSDFFRELDVVPSDVVAGLVLLRKFQRLEREAIVRQRKNGTYEFLSGVPITERTQFLALNDAKNYDFFQTVIHYMYFAQGAYGWPMYVIINRSKMWHLVPELKCFGCCCGTSDDTEVIQDNCCLCNYAALKKTLQLGDIDIVYATYHVDVGETPFFVAIDYTHRAVVISIRGTLSMKDILTDLNAEGEVLPLQPPRDDWLGHKGMVQAAIYIRNKLQEENLIERALQRNPDRQTHTFDLVLVGHSLGAGTAAILAILLKPEHPTLQCFSYSPPGGLLSMPAVEYSKSFITSVVLGKDVVPRIGLNQMEALRADLINAIQRSVDPKWKTISCSVICCGCGPEPTSVVNMSGQDTHINQYQEERGTARSTSAHPTDSSIALTLHQPLYPPGRIIHIVRHHPKPDENVLKNREPVYQAIWADSTDFDEVLISPVMLQDHMPDKVLAALKKVVTTSGPRKPQRQTSNAFSTGSNEAAHDMDLEPPHCSGHSAPTDAMRFETRTDPGQMQNSMSQSQHCKRLSQSSYTNLSNCLVLTPTAQHKLCLETSFTNGSTPHQSGVQPNPRLTSAASSLLSSATTPYDISSALDDSLATVALRQSPSLISAETTATVIVNPEPDAEEIAIPQRLKAVAFDMALTPPPTLPERSMLGRQHSEKKPRSLPLAQVQALRRASDAGAVPGVDLLHDDWYGLAPLASPETLSEISSVSSRTSVPISLANSIERYLQHMGVGVGGPKVPLEDIFESQLHTPKVMRRAPKFSENLAGCAEDTRNLDQYKRLGRVFITFPRIFPDQSPAAHSLDSSDDSFESASAHSLQRLQLPHGANAVQSSKSADPLDGDPDATRQTQPAKKLTFSDSDILTDADCLRLCPHCPCDRDVQRGCCTRSEHGKCGTEISGGCGGAAMGLGSTDTSFYSASSSLEQFATPARQNGGTGASGNHLEEILIRPGVLESHFPVLGGGSAIETPALVAPASPSPLSNGKRPDVVGGRVRKRLSSEEFVFSRSEDLPSLVQIGDRCTGSPAGRRRAKGCVYPAGNSLRLDAAAAVASASASPTSISKFTRTRVAAGGLAAKQAAGNNESNV
Protein: Hydrophobic dipeptide epimerase (EC 5.1.1.-) (L-Hydrophobic-D/L-Hydrophobic epimerase) (B5EFW2)
Organism: Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem) (Geobacter bemidjiensis)
Function: Catalyzes the epimerization of various hydrophobic dipeptides, such as L-Ala-L-Phe. Has epimerase activity with L-Ala-L-Thr, L-Ala-L-Met, L-Ala-L-Tyr, as well as L-Phe-L-Met, L-Phe-L-Ser and L-Phe-L-Thr (in vitro).
Interaction partners:
- DUF819 family protein
Sequence:
MDISFQIQDAVASVIRAPLASPFRIATGQHDELENVFLKLTTRDGVSGYGEAAVASHITGETVPGTLANLQNAAAALRGQTVDDAESACRQFAAAFAGNHAGLAALEMALLDLSSRVRGIPFYRLFAPVAALEPRLAFSTDITVVIGSLDEARATAREFASRGFKAFKIKIGRDEQLDLARVLAVHEIAPDSQIILDANMGFSAGSMLAFLDRLAAKGVRPVLLEQPVPKMDWDGLSEITAALTGSETLVCADESVGSLADARRAIDSNAVSAINVKFMKSGILEGAEIARLAASRGIRLMLGAMMESALAVTASAHFAAGLACFDYLDMDTTFFLKGELAHSPYLDEHGRFDLHDAGPGIGVEPRFS
Protein: ESAT-6-like protein (A0A0H3LDU7)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MTINYQFGDVDAHGAMIRAQAASLEAEHQAIVRDVLAAGDFWGGAGSVACQEFITQLGRNFQVIYEQANAHGQKVQAAGNNMAQTDSAVGSSWA
Protein: PDZ domain-containing protein (Q387S1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLWSTPPQSERVPQVSTTMEELASTSSTLEQLQSFFVLHTFDTSGPFSDLFSVLLSCCKHLVDSSVSQNTVICGQAREIERLAREVEELRGTLVSQQSYFQDLESRRLAHSVASAEEAQGINAEVVGRRLNKLDEAVHAVQKTVEEYRHPCTGGVNEERGMWERVNRLEVDLESLKERVSSTTENIRAEVATIGNAVSSIKTSSAPDYILASQSYTDAKMANVREEILMAKQSKTSTADDSKLYTGTSPPQNWKSDTECVMNRSTRSLESGDPNEKCGRAGYRPCGTEVWENIPARLDELESRLEVLEVYAPHHSAMAARPPLLGVELRDERGGGVRVHEVFSGFAAHAAGVLPGDVVVALNARNVNTRAEMYALIAELTQENEVKRRLLMQMYYEEHSGTCRNEEAKEGCCFLQAPNSAAVSGRWFGSGSGTAGAGNVRTMNKAELTAGMARRWDLPKLQFALHLKRGVFLHEVVVICERASGS
Protein: Cruzioseptin-5 (CZS-5) (A0A193H356)
Organism: Cruziohyla calcarifer (Splendid leaf frog) (Agalychnis calcarifer)
Function: Has antimicrobial activity.
Subcellular location: Secreted {ECO:0000269|PubMed:27321580}.
Interaction partners:
Sequence:
KRGFLDVIKHVGKAVGKAALNAVNDMVNKPEQQS
Protein: Receptor expression-enhancing protein (Q9VYX3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362006}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362006}.
Interaction partners:
- LD43541p
- Reticulon-like protein
- Palmitoyltransferase
- Don juan like
- Glutamate transporter polyphemus
- Uncharacterized protein, isoform A
- AT10852p
- IP12902p
- FI23334p1
- Uncharacterized protein, isoform A
Sequence:
MIYAIVIHILSLLVGCFYPAFASYKILKSQNCSVNDLRGWLIYWIAYGVYVAFDYFTAGLLAFIPLLSEFKVLLLFWMLPSVGGGSEVIYEEFLRSFSCNESFDQVLGRITLEWGELVWQQVCSVLSHLMVLADRYLLPSGHRPALQITPSIEDLVNDAIAKRQLEEKRKQMGNLSDTINEVLGENIDLNMDLLHGSESDLLVIKEPISKPKERPIPPPKPMRQPSSSNQQEMNLSSQFM
Protein: Vta1/callose synthase N-terminal domain-containing protein (Q57XT4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}.
Interaction partners:
- SNF-7-like protein, putative
- Vacuolar transport protein 4A, putative
- Katanin, putative
- Vesicular protein trafficking mediator, putative
- Uncharacterized protein
- IST1 homolog
- Uncharacterized protein
- Uncharacterized protein
- Class-E vacuolar protein-sorting protein 24
- Charged multivesicular body protein 6
Sequence:
MSLADEVPREWASSIRPFLQRADEFQERVPVVAYFLRTHAVYLAMKMWRKEDGPGKAFIVKLLDTLESEKKRLEQELADVDGRVLLTQYALRIFSRADDEERSDGVVANMNLVRLFFTASLLFEATAQFTDDGTLDPIATEKRDYARYIAVEMKKAMDKGVPYVSPNRTGGMVESNKEHEGESTGGGGFSTNFVQSQQPGYGQWSAQYVTPQPPPPSHEPPETPMWSGPESTNTSSTQQQQQSTPLFQTTAQPNNSNDNSNIAAAVSGVAAPKGPTMDAIIEAQNYAKQAVSALQFYDHEVACKMLRSALDLLAQR
Protein: PRKCA-binding protein (Protein interacting with C kinase 1) (Protein kinase C-alpha-binding protein) (Q62083)
Organism: Mus musculus (Mouse)
Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:24068808}; Lipid-anchor {ECO:0000269|PubMed:24068808}. Postsynaptic density {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Also membrane-associated, present at excitatory synapses. {ECO:0000250}.
Interaction partners:
- Glutamate receptor 2
- Protein kinase C alpha type
- Glutamate receptor 3
- Tetraspanin-7
- Glutamate receptor-interacting protein 1
- Disks large homolog 4
- Islet cell autoantigen 1
- Glutamate receptor 1
- Acid-sensing ion channel 1
- Glutamate receptor 4
Sequence:
MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGKSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIGPRRALYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRFVSTMSKYYNDCYAVLQDADVFPIEVDLAHTTLAYGPNQGSFTDGEEEDEEEEDGAAREVSKDACGATGPTDKGGSWCDS
Protein: Secretogranin-3 (Secretogranin III) (SgIII) (P47867)
Organism: Mus musculus (Mouse)
Function: Member of the granin protein family that regulates the biogenesis of secretory granules. Acts as a sorting receptor for intragranular proteins including chromogranin A/CHGA. May also play a role in angiogenesis. Promotes endothelial proliferation, migration and tube formation through MEK/ERK signaling pathway (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:12388744, ECO:0000269|PubMed:16219686}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P47868}; Peripheral membrane protein {ECO:0000250}. Secreted {ECO:0000269|PubMed:12388744}. Note=Associated with the secretory granule membrane through direct binding to cholesterol-enriched lipid rafts. {ECO:0000250|UniProtKB:P47868}.
Interaction partners:
- Chromogranin-A
- Secretogranin-1
- Secretogranin-2
- Carboxypeptidase E
- Neuroendocrine protein 7B2
- Transient receptor potential cation channel subfamily A member 1
Sequence:
MGFLWTGSWILVLVLNSGPIQAFPKPEGSQDKSLHNRELSAERPLNEQIAEAEADKIKKAFPSESKPSESNYSSVDNLNLLRAITEKETVEKERQSIRSPPFDNQLNVEDADSTKNRKLIDEYDSTKSGLDHKFQDDPDGLHQLDGTPLTAEDIVHKIATRIYEENDRGVFDKIVSKLLNLGLITESQAHTLEDEVAEALQKLISKEANNYEETLDKPTSRTENQDGKIPEKVTPVAAVQDGFTNRENDETVSNTLTLSNGLERRTNPHREDDFEELQYFPNFYALLTSIDSEKEAKEKETLITIMKTLIDFVKMMVKYGTISPEEGVSYLENLDETIALQTKNKLEKNTTDSKSKLFPAPPEKSQEETDSTKEEAAKMEKEYGSLKDSTKDDNSNLGGKTDEATGKTEAYLEAIRKNIEWLKKHNKKGNKEDYDLSKMRDFINQQADAYVEKGILDKEEANAIKRIYSSL
Protein: Putative uncharacterized protein YLR173W (Q06247)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MHTNSPLRADNQDLETQPLLRPNTEESQLLNDEVRINVANETLIKSRWRSIKCLIIYLLGIVLLSFFGVSIVQYIRGHVPPTDVIEKNLVQVTNFKLVEFQLDGWKDNMGSDLNNDTGKYLQVSIHSQIWFDYDKWPGTENDSDARSQRDWIRYINEKVLKTICIDLNNVTTFDGDLVFKNKLGDVVGMEPICFNLAHRQINNLQFKILVKPSIWKIVKVLKKFWNRDFESLNIKSNLDMTIFKRKFGTRFNLLKLNDEILDWKDIIDWEKISATPLRMIQNMIDGISLQGFTLRDSSSDGFHADMRLNPITILGGVDWLHLPPGTSIPFINWEIKLPDCNGEPAIAIPTLSCFNEPINLHHDKDNIVVCLQNEIEGPLPDELLYQECPQNSLTPMSQIVNAVLNQNETVTFAARGHVLEDGIDNNSLIPADMLEDIFQEASFIPITTNATFNSSELIQEFQINDLQLRWAARKKLSLVGTFLGFFDLSFYETHQQDRVRIDTIRGQIDLYHNDINFLNLPMKQWINSSSHILHDEDTGNTQMKLQFDLENDDMEVVNSLELTRTLNEILFQGFTVIHFNATIDASLTTALGPWVLTGLAGEGDTLVT
Protein: N-acetyltransferase ESCO2 (EC 2.3.1.-) (Establishment factor-like protein 2) (EFO2) (EFO2p) (hEFO2) (Establishment of cohesion 1 homolog 2) (ECO1 homolog 2) (Q56NI9)
Organism: Homo sapiens (Human)
Function: Acetyltransferase required for the establishment of sister chromatid cohesion. Couples the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during the S phase. Acetylates the cohesin component SMC3.
Subcellular location: Nucleus {ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:19907496}. Chromosome {ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:19907496}. Note=Nuclear in interphase cells, excluded from chromosomes during metaphase but reassociates with chromosomes in telophase. {ECO:0000269|PubMed:15958495}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion protein PDS5 homolog A
- Wings apart-like protein homolog
- Double-strand-break repair protein rad21 homolog
- Chromosome transmission fidelity protein 18 homolog
- Structural maintenance of chromosomes protein 1A
- Sister chromatid cohesion protein DCC1
- Nipped-B-like protein
- Sister chromatid cohesion protein PDS5 homolog B
- Cohesin subunit SA-1
Sequence:
MAALTPRKRKQDSLKCDSLLHFTENLFPSPNKKHCFYQNSDKNEENLHCSQQEHFVLSALKTTEINRLPSANQGSPFKSALSTVSFYNQNKWYLNPLERKLIKESRSTCLKTNDEDKSFPIVTEKMQGKPVCSKKNNKKPQKSLTAKYQPKYRHIKPVSRNSRNSKQNRVIYKPIVEKENNCHSAENNSNAPRVLSQKIKPQVTLQGGAAFFVRKKSSLRKSSLENEPSLGRTQKSKSEVIEDSDVETVSEKKTFATRQVPKCLVLEEKLKIGLLSASSKNKEKLIKDSSDDRVSSKEHKVDKNEAFSSEDSLGENKTISPKSTVYPIFSASSVNSKRSLGEEQFSVGSVNFMKQTNIQKNTNTRDTSKKTKDQLIIDAGQKHFGATVCKSCGMIYTASNPEDEMQHVQHHHRFLEGIKYVGWKKERVVAEFWDGKIVLVLPHDPSFAIKKVEDVQELVDNELGFQQVVPKCPNKIKTFLFISDEKRVVGCLIAEPIKQAFRVLSEPIGPESPSSTECPRAWQCSDVPEPAVCGISRIWVFRLKRRKRIARRLVDTLRNCFMFGCFLSTDEIAFSDPTPDGKLFATKYCNTPNFLVYNFNS
Protein: Perforin-1 (P1) (Cytolysin) (Lymphocyte pore-forming protein) (P35763)
Organism: Rattus norvegicus (Rat)
Function: Pore-forming protein that plays a key role in granzyme-mediated programmed cell death, and in defense against virus-infected or neoplastic cells. Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores (By similarity). Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes (By similarity). Perforin pores allow the release of mature caspase-7 (CASP7) into the extracellular milieu (By similarity).
Subcellular location: Cytolytic granule {ECO:0000269|PubMed:2809217}. Secreted {ECO:0000269|PubMed:2809217}. Cell membrane {ECO:0000269|PubMed:2809217}; Multi-pass membrane protein {ECO:0000269|PubMed:2809217}. Endosome lumen {ECO:0000250|UniProtKB:P14222}. Note=Stored in cytolytic granules of cytolytic T-lymphocytes and secreted into the cleft between T-lymphocyte and target cell. Inserts into the cell membrane of target cells and forms pores. Membrane insertion and pore formation requires a major conformation change. May be taken up via endocytosis involving clathrin-coated vesicles and accumulate in a first time in large early endosomes (By similarity). {ECO:0000250|UniProtKB:P14222}.
Interaction partners:
- Granzyme A
- Granzyme B
- Tumor necrosis factor ligand superfamily member 6
- Natural killer cells antigen CD94
- Interleukin-2 receptor subunit beta
- NKG2-D type II integral membrane protein
- Natural killer cell group 7 sequence, isoform CRA_a.
- Interferon gamma
- T-cell surface glycoprotein CD8 alpha chain
- T-cell surface glycoprotein CD3 zeta chain
Sequence:
MAAYLFLLGLFLLLPRPVPAPCYTATRSECKQNHKFVPGVWAAGEGVDVTTLRRSSSFPVNTGKFLRPDRTCTLCKNALMNDGIQRLPVAIAHWRPHGSHCQRNVATTKVSSTEGVAREAAANINNDWRAGLDVNPKPEANVHVSVAGSHSKIANFAAEKAHQDQYNFNTDTVECRMYSFRLAQKPPLHPDFRKALKNLPHNFNSSTEHAYRRLISSYGTHFITAVDLGGRVSVLTALRTCQLTLDGLTADEVGDCLSVEAQVSIGAQASVSSEYKACEEKKKQHKIATSFHQTYRERHVEVLGGPLDSSNDLLFGNQATPEHFSTWIASLPTRPDVVDYSLEPLHILLEDSDPKREALRQAISHYVMSRARWRDCNRPCRAGQHKSSRDSCQCVCQDSNVTNQDCCPRQRGLAKLMVRNFQAKGLWGDYITSTDAYLKVFFGGQEIRTGVVWNNNHPSWSDKMDFGNVLLSTGGPLRVQVWDADNGWDDDLLGTCDKSPKSGFHEVNCPLNHGSIKFIYQANCLPDLTGETCLEYAPQGLLGDPRGNRSGAVW
Protein: Volume-regulated anion channel subunit LRRC8C (Factor for adipocyte differentiation 158) (Leucine-rich repeat-containing protein 8C) (Q8R502)
Organism: Mus musculus (Mouse)
Function: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine (By similarity). Plays a redundant role in the efflux of amino acids, such as aspartate and glutamate, in response to osmotic stress (By similarity). The VRAC channel also mediates transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol (By similarity). Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition (By similarity). May play a role in adipogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:29769723}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TDW0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TDW0}. Note=In the absence of LRRC8A, resides primarily in a cytoplasmic compartment, probably the endoplasmic reticulum. Requires LRRC8A for expression at the cell membrane. {ECO:0000250|UniProtKB:Q8TDW0}.
Interaction partners:
- Volume-regulated anion channel subunit LRRC8A
- Protein tweety homolog 3
- Protein tweety homolog 2
Sequence:
MIPVTEFRQFSEQQPAFRVLKPWWDVFTDYLSVAMLMIGVFGCTLQVMQDKIICLPKRVQPAQNHSSVPNVSQAVISTTPLPPPKPSPTNPATVEMKGLKTDLDLQQYSFINQMCYERALHWYAKYFPYLVLIHTLVFMLCSNFWFKFPGSSSKIEHFISILGKCFDSPWTTRALSEVSGEDSEEKDNRKNNMNRSGTIQSGPEGNLVRSQSLKSIPEKFVVDKSAAGALDKKEGEQAKALFEKVKKFRLHVEEGDILYAMYVRQTVLKVIKFLIIIAYNSALVSKVQFTVDCNVDIQDMTGYKNFSCNHTMAHLFSKLSFCYLCFVSIYGLTCLYTLYWLFYRSLREYSFEYVRQETGIDDIPDVKNDFAFMLHMIDQYDPLYSKRFAVFLSEVSENKLKQLNLNNEWTPDKLRQKLQTNAHNRLELPLIMLSGLPDTVFEITELQSLKLEIIKNVMIPATIAQLDNLQELCLHQCSVKIHSAALSFLKENLKVLSVKFDDMRELPPWMYGLRNLEELYLVGSLSHDISKNVTLESLRDLKSLKILSIKSNVSKIPQAVVDVSSHLQKMCVHNDGTKLVMLNNLKKMTNLTELELVHCDLERIPHAVFSLLSLQELDLKENNLKSIEEIVSFQHLRKLTVLKLWYNSIAYIPEHIKKLTSLERLFFSHNKVEVLPSHLFLCNKIRYLDLSYNDIRFIPPEIGVLQSLQYFSITCNKVESLPDELYFCKKLKTLKIGKNSLSVLSPKIGNLLFLSYLDIKGNHFEVLPPELGDCRALKRAGLVVEDALFETLPSDVREQMKAD
Protein: ABC transporter G family member 32 (ABC transporter ABCG.32) (AtABCG32) (Pleiotropic drug resistance protein 4) (Protein PERMEABLE CUTICLE 1) (O81016)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a general defense protein (By similarity). Required for the formation of the cuticle layer of the cell wall.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21628525}; Multi-pass membrane protein {ECO:0000269|PubMed:21628525}.
Interaction partners:
- Putative ion channel POLLUX-like 1
- Glycerol-3-phosphate 2-O-acyltransferase 6
- Long chain acyl-CoA synthetase 2
- At3g10570
- 3-ketoacyl-CoA synthase 6
- ABC transporter F family member 3
- Egg cell-secreted protein 1.1
Sequence:
MWNSAENAFSRSTSFKDEIEDEEELRWAALQRLPTYSRIRRGIFRDMVGEPKEIQIGNLEASEQRLLLDRLVNSVENDPEQFFARVRKRFDAVDLKFPKIEVRFQNLMVESFVHVGSRALPTIPNFIINMAEGLLRNIHVIGGKRNKLTILDGISGVIRPSRLTLLLGPPSSGKTTLLLALAGRLGTNLQTSGKITYNGYDLKEIIAPRTSAYVSQQDWHVAEMTVRQTLEFAGRCQGVGFKYDMLLELARREKLAGIVPDEDLDIFMKSLALGGMETSLVVEYVMKILGLDTCADTLVGDEMIKGISGGQKKRLTTGELLVGPARVLFMDEISNGLDSSTTHQIIMYMRHSTHALEGTTVISLLQPSPETYELFDDVILMSEGQIIYQGPRDEVLDFFSSLGFTCPDRKNVADFLQEVTSKKDQQQYWSVPFRPYRYVPPGKFAEAFRSYPTGKKLAKKLEVPFDKRFNHSAALSTSQYGVKKSELLKINFAWQKQLMKQNAFIYVFKFVQLLLVALITMTVFCRTTMHHNTIDDGNIYLGSLYFSMVIILFNGFTEVPMLVAKLPVLYKHRDLHFYPSWAYTLPSWLLSIPTSIIESATWVAVTYYTIGYDPLFSRFLQQFLLYFSLHQMSLGLFRVMGSLGRHMIVANTFGSFAMLVVMTLGGFIISRDSIPSWWIWGYWISPLMYAQNAASVNEFLGHNWQKTAGNHTSDSLGLALLKERSLFSGNYWYWIGVAALLGYTVLFNILFTLFLAHLNPWGKFQAVVSREELDEREKKRKGDEFVVELREYLQHSGSIHGKYFKNRGMVLPFQPLSLSFSNINYYVDVPLGLKEQGILEDRLQLLVNITGAFRPGVLTALVGVSGAGKTTLMDVLAGRKTGGTIEGDVYISGFPKRQETFARISGYCEQNDVHSPCLTVVESLLFSACLRLPADIDSETQRAFVHEVMELVELTSLSGALVGLPGVDGLSTEQRKRLTIAVELVANPSIVFMDEPTSGLDARAAAIVMRTVRNIVNTGRTIVCTIHQPSIDIFESFDELLFMKRGGELIYAGPLGQKSCELIKYFESIEGVQKIKPGHNPAAWMLDVTASTEEHRLGVDFAEIYRNSNLCQRNKELIEVLSKPSNIAKEIEFPTRYSQSLYSQFVACLWKQNLSYWRNPQYTAVRFFYTVVISLMLGTICWKFGSKRDTQQQLFNAMGSMYAAVLFIGITNATAAQPVVSIERFVSYRERAAGMYSALPFAFAQVFIEFPYVLAQSTIYSTIFYAMAAFEWSAVKFLWYLFFMYFSIMYFTFYGMMTTAITPNHNVASIIAAPFYMLWNLFSGFMIPYKRIPLWWRWYYWANPVAWTLYGLLVSQYGDDERSVKLSDGIHQVMVKQLLEDVMGYKHDFLGVSAIMVVAFCVFFSLVFAFAIKAFNFQRR
Protein: Kynurenine 3-monooxygenase (EC 1.14.13.9) (Kynurenine 3-hydroxylase) (Q1RLY6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.
Subcellular location: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03018}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03018}.
Interaction partners:
- Kynureninase
- Kynurenine formamidase
- Kynurenine--oxoglutarate transaminase 3
- 3-hydroxyanthranilate 3,4-dioxygenase
- Aminoadipate aminotransferase.
- Si:ch73-97h19.2.
- Kynurenine aminotransferase 1
- Indoleamine 2,3-dioxygenase 1.
- Cholesterol 7-desaturase nvd
- Ubiquinone biosynthesis O-methyltransferase
Sequence:
METAFSHPPQSSSSKRKVIAVVGGGLVGSLNACFLAKRGFDVEVYESREDIRQAKVVKGRSINLALSHRGRQALKHVGMEDKIISKGIPMHARMIHNVNGKRSPIPYGKKGQYILSVDRANLNKELLTAAEAYPNTRLNFNHKLHDWSPKTGTMTFIGSDGQKTETQADLIVGCDGAFSAVRKQFLRQSRFNYSQTYIPHGYMELTMPPKDGDFAMEPNYLHIWPRNTFMMIALPNLDRTFTCTLFMPFEDFEKIRTGDELLRFFHKYFPDSVPLIGVEALKQDFFRLPAQAMVSVKCCPYHLFEKCVLMGDAAHAVVPFYGQGMNAGFEDCLVFDEIMDQFNENLVAVLQEYTRVRVPDDHAIADLAMYNYIEMRAHVNSKYFIFRKYLDNLLHFFMPKTIVPLYTMVTFTRTRYNDAVNRWHWQNKVITRGLWLCGFVSAAGGTYVLVKNSHKLPSISAEQLWTRILALKLF
Protein: Pentalenolactone D synthase (EC 1.14.13.170) (Pentalenolactone biosynthesis protein E) (E3VWK3)
Organism: Streptomyces exfoliatus (Streptomyces hydrogenans)
Function: Catalyzes the flavin-dependent Baeyer-Villiger oxidation of 1-deoxy-11-oxopentalenic acid to pentalenolactone D in the biosynthesis of pentalenolactone antibiotic.
Interaction partners:
Sequence:
MREKYRQERDKRSVGRTYQFARGDFSRYARDPYTERQEREPLTDEVDVAVVGAGIGGLLTGAHLRKETGLERIRLIDGAGDVGGTWYWNRFPGVRCDVESYIYMPLLEETGTIPREKYSTGPEIFAHLQQIAHRYDLYRDALFQTTVTELRWDEAAGRWLVSTDRGDLIRARYVAMSIGLMHRPKLPGLPGLETFAGHSFHTSRWDFDYTGGDSTGGLTKLKDKKVGVIGTGSTTIQLAPHLAEWAEQLILFQRTPAAVDVRGNRPTPPEWAAGLAPGWQQRRMENFHALTSGVPQDEDLVQDRWTQTTAKLAAAILPTGDTGGDPKERALAAERADFLKMEELRARIDSVVTDPATAAALKPYYRVYCKRPCFHDGYLQTFNRPNVTLVDTQGQGVERLTPAGVVANGREYPLDCLIFATGYEHEFAVPYTERAGYDIVGRDGLRLSEKWADGARTLHGLQVNGFPNCFILSKVQAGRHVNIAYMLGEQTRHLAHIVKCVEERGHQVVEASEAGEKEWVEEILRLATNDIDFLENCTPGLYNNEGDPSGLPLLNSSYGGGSVEFVNILRRWREAGDLAGLELR
Protein: Regulator of G-protein signaling 10 (RGS10) (Q9CQE5)
Organism: Mus musculus (Mouse)
Function: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the muscarinic acetylcholine receptor CHRM2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Modulates the activity of potassium channels that are activated in response to CHRM2 signaling. Activity on GNAZ is inhibited by palmitoylation of the G-protein.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O43665}. Nucleus {ECO:0000250|UniProtKB:O43665}. Note=Forskolin treatment promotes phosphorylation and translocation to the nucleus. {ECO:0000250|UniProtKB:O43665}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Regulator of G-protein signaling 7-binding protein
Sequence:
MFTRAVSRLSRKRPPSDIHDGDGSSSSGHQSLKSTAKWASSLENLLEDPEGVQRFREFLKKEFSEENVLFWLACEDFKKTEDRKQMQEKAKEIYMTFLSNKASSQVNVEGQSRLTEKILEEPHPLMFQKLQDQIFNLMKYDSYSRFLKSDLFLKPKRTEEEEEEPPDAQTAAKRASRIYNT
Protein: Septin homolog spn1 (O36023)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in the cell cycle. Involved in a late stage of septum formation leading to the separation of the daughter cells.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:15385632}. Note=Localizes to the medial ring at the cell cortex of dividing cells.
Interaction partners:
- Septin homolog spn2
- Septin homolog spn4
- Septin homolog spn3
- Septin homolog spn7
- Septin homolog spn6
- Septin homolog spn5
- Septin ring organizing protein mid2
- Rho guanine nucleotide exchange factor gef3
Sequence:
MASMVLADGMPTVKDDSTRSRGSDVDSFTSTDNVTQINVEAAISENKNEEKPIQDNSEQEFNPHVSIIQRQLNGYVGFASLPNQWHRRCVRQGFNFNVLVLGESGSGKSTLVNTLLNRDVYPPTQKSLTGDFGVNPEPTVMINSSAVEIVENGISLQLNVIDTPGFGDFIDNTDCWQPVLTDIEGRYDQYLELEKHNPRSTIQDPRVHACIFFIQPTGHAISAMELRVMLALHEKVNIIPIIAKADTLTDDELNFTKEMILRDIQYHNIRIFFPPTYETDDPESVAENADIMSRIPFAIIASNTFVVNNEGKRVRGRRYPWGVVEVDNEEHSDFPKLREMLIRTHLEELKEQTNKLYEAYRTERLLSSGISQDHSVFREVNPSAKLEEERALHEEKLMKMEAEMKTIFSQKVQEKEDRLKQSENELRTRHREMKAALEKQKADLIDHKNRLMQAKAAAENEKSKRKFFK
Protein: Zcf21p (A0A1D8PL89)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MMDIYQKALKNPDPPKKPASTTTTPPSSTSTDYNTRLPPMNHNNNNVDSMNYNYSHDNGSFTGSTTTTTTTNISNENSNNNSSTNSPNSRPSSTNTNTNAHTSEEIKNNVIRKKKNSRRKHRNSHLGCGTCKKRRIKCDETLPACLNCLKGKLHCAYLNLDNNARNALRVAQYNQTIRQEKLDANSSSSTTANINNNTKLIDPSKDNILVQQQQPVGIVQSLAHGISIVPPHPSTAAAAGSQNAPMMATGPGSYPMAATVLPNNQTLVTAVPQQSQASMSIPPFANSILAPGIQANPSPSITTNNLNSSIANTTSNTNNNTNADMTSSGSTSGNIQNIASTPQVVQSPYGPMIPLLTQSGSVVYAPTHSLVPAQPSQLPPQQLQNNVAFSNTTVPATGTLPPPMSQPSVLSTANTAATTSPNIPPLAAPPPTTGVAGTASTGIMANVSPVLTNKQQPSSTPITSSAASVATIASQTIPVKTGNGTSSTASTSSPTTATVSPPGIANILPPPINTLGNSSNGANSSGTDVFKPNVSDSSIKELKPINDSNGNTPPSTTTSAIGNYGDGVKLSPNSSMTNLKKLTIREDNNSGSDIKLPSITTLKRESSKSPSETNGNVDEKVPTISKLIT