wanglab/gogpt-training-data huggingface dataset:
Protein: Gamma-glutamylanilide synthase (Gamma-GA synthase) (EC 6.3.1.18) (Glutamine synthetase-like protein) (Q44249)
Organism: Acinetobacter sp
Function: Involved in the initial oxidation of aniline to catechol by the release of its amino group. Catalyzes the ATP-dependent ligation of L-glutamate to aniline to yield gamma-glutamylanilide. AtdA1 has a broad substrate range and is able to convert the following anilines: aniline (100%), o-chloroaniline (92%), m-chloroaniline (69%), p-chloroaniline (92%), o-methylaniline (40%), m-methylaniline (27%), and p-methylaniline (45%). It can also accept chlorinated and methylated forms of aniline, preferably in the o- and p-positions.
Interaction partners:
Sequence:
MSEKLDFITKNNLWTDKQRDAADKVLAEIDSLGLEMIRLSWADQYGLLRGKALSVAALKAAFSEGSEVTMAPFSFNLVSEWVFNPFTAGGGFGIDEFDELGGVPSVVMVPDPTTFKVLPWADKTGWMLADLHWKSGEPFPLCPRGIMKKAVKSLSDEGYLFKCGIELEWYLTKIVDRSLSPESLGAPGVQPDAIQVQPVAQGYSYLLEYHLDQVDDIMSKVRKGLLELNLPLRSIEDELAPSQMETTFDVMEGLEAADAALLIKSAIKQICSRHGYHATFMCKPAINGFSVASGWHMHQSLVDKDTRKNLFIPSEGEVVSPLGRAYAGGLLANGSAASSFTTPTVNGYRRRQPHSLAPDRRAWAKENKAAMVRVISATGDPASRIENRIGEPGANPYLYMASQIVSGLDGIKIKRDPGGLQGAPYGAQVPMLPTALAEALDALEHDSELFRSCFGDTFIKYWLQLRRSEWARFLDAEGAEAAEPTGAVTQWEQKEYFNLL
Protein: Interleukin-6 (IL-6) (Q0GGL7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway. The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P05231}.
Interaction partners:
Sequence:
MNSSTRYLSLLSALVVLVKGNPVPSALAELMTSGWTSGEELGTDGETGAPPKWEKMIKMLVHEVTTLRNQQFVEEFQKPVEEISSFSQHQVPSTPPHLSKTLCSASNKEACLQEISRGLQVYQLLLQHVKAEYPQSTLLPSVTHQTTVLIGLVKDQMKVAEVVEDLSASERKRVLGEVSTGTEWERKTSVHAILRELRNFLVDTKRALRRMGKRGKDFQ
Protein: Archaic translocase of outer membrane 11 kDa subunit (Q389N6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMFGRPAVPQATWEEKYFYQKLHHLFDHAADWFVTKVNWWMPSIGAGMVLSLFVLSGPNAIAEGASVLIPTLSPVVRAPPFGLQMPEREGGPQEEDEEEF
Protein: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 (BRG1-associated factor 47) (BAF47) (Integrase interactor 1 protein) (SNF5 homolog) (hSNF5) (Q12824)
Organism: Homo sapiens (Human)
Function: Core component of the BAF (hSWI/SNF) complex. This ATP-dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Involved in activation of CSF1 promoter. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1.
Subcellular location: Nucleus.
Interaction partners:
- PHD finger protein 10
- Protein polybromo-1
- SWI/SNF complex subunit SMARCC2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2
- AT-rich interactive domain-containing protein 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- Actin-like protein 6A
- AT-rich interactive domain-containing protein 1A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3
Sequence:
MMMMALSKTFGQKPVKFQLEDDGEFYMIGSEVGNYLRMFRGSLYKRYPSLWRRLATVEERKKIVASSHGKKTKPNTKDHGYTTLATSVTLLKASEVEEILDGNDEKYKAVSISTEPPTYLREQKAKRNSQWVPTLPNSSHHLDAVPCSTTINRNRMGRDKKRTFPLCFDDHDPAVIHENASQPEVLVPIRLDMEIDGQKLRDAFTWNMNEKLMTPEMFSEILCDDLDLNPLTFVPAIASAIRQQIESYPTDSILEDQSDQRVIIKLNIHVGNISLVDQFEWDMSEKENSPEKFALKLCSELGLGGEFVTTIAYSIRGQLSWHQKTYAFSENPLPTVEIAIRNTGDADQWCPLLETLTDAEMEKKIRDQDRNTRRMRRLANTAPAW
Protein: Y+L amino acid transporter 1 (Monocyte amino acid permease 2) (MOP-2) (Solute carrier family 7 member 7) (y(+)L-type amino acid transporter 1) (Y+LAT1) (y+LAT-1) (Q9UM01)
Organism: Homo sapiens (Human)
Function: Involved in the sodium-independent uptake of dibasic amino acids and sodium-dependent uptake of some neutral amino acids. Requires coexpression with SLC3A2/4F2hc to mediate the uptake of arginine, leucine and glutamine. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Involved in the transport of L-arginine in monocytes.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:15756301}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Amino acid transporter heavy chain SLC3A2
- Amino acid transporter heavy chain SLC3A1
Sequence:
MVDSTEYEVASQPEVETSPLGDGASPGPEQVKLKKEISLLNGVCLIVGNMIGSGIFVSPKGVLIYSASFGLSLVIWAVGGLFSVFGALCYAELGTTIKKSGASYAYILEAFGGFLAFIRLWTSLLIIEPTSQAIIAITFANYMVQPLFPSCFAPYAASRLLAAACICLLTFINCAYVKWGTLVQDIFTYAKVLALIAVIVAGIVRLGQGASTHFENSFEGSSFAVGDIALALYSALFSYSGWDTLNYVTEEIKNPERNLPLSIGISMPIVTIIYILTNVAYYTVLDMRDILASDAVAVTFADQIFGIFNWIIPLSVALSCFGGLNASIVAASRLFFVGSREGHLPDAICMIHVERFTPVPSLLFNGIMALIYLCVEDIFQLINYYSFSYWFFVGLSIVGQLYLRWKEPDRPRPLKLSVFFPIVFCLCTIFLVAVPLYSDTINSLIGIAIALSGLPFYFLIIRVPEHKRPLYLRRIVGSATRYLQVLCMSVAAEMDLEDGGEMPKQRDPKSN
Protein: 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Antisecretory factor 1) (AF) (ASF) (Multiubiquitin chain-binding protein) (P55036)
Organism: Homo sapiens (Human)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. Displays a preferred selectivity for longer polyubiquitin chains.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 5
- Proteasome subunit alpha type-6
- Ubiquitin-ribosomal protein eS31 fusion protein
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome non-ATPase regulatory subunit 7
- Proteasome subunit beta type-1
- 26S proteasome non-ATPase regulatory subunit 2
- Proteasome subunit alpha type-4
- Proteasome subunit alpha type-5
Sequence:
MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTLNGKDGTGSHLVTVPPGPSLADALISSPILAGEGGAMLGLGASDFEFGVDPSADPELALALRVSMEEQRQRQEEEARRAAAASAAEAGIATTGTEDSDDALLKMTISQQEFGRTGLPDLSSMTEEEQIAYAMQMSLQGAEFGQAESADIDASSAMDTSEPAKEEDDYDVMQDPEFLQSVLENLPGVDPNNEAIRNAMGSLASQATKDGKKDKKEEDKK
Protein: Flavin-containing monooxygenase (EC 1.-.-.-) (Q7K3U4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- ATP synthase subunit alpha, mitochondrial
Sequence:
MIKTSVDKRRVCVIGAGTAGLCALKNSLEAGLDAVAYERGTEIGGTWIFSEEMPKDEYDEVHSSMYEGLRTNLPKEVMGYPDYSYPDDITESFITSNQVLEFLRSYAEHFKLKAHIKLQHEVIRVRPRLDDWEVYVWDHSTDTCDPVYYDFVYVCNGHYTEPDLPEVEGLDLFEGNKMHSHLYRKADKFKDARVLIIGAGPSGMDITNHVRLAAKQVFLSHHLSTTPNTAFMGNVTQKPDVKRFTKDGAVFTDGSTESFDHVMFCTGYKYTFPCLSTDVGVQVIDNFVQPLWKHCININHPTMAFVGLPFNVIPTHIFDMQVRFTLKFFTGQRKFPSREQMIADLEQEIGERWGCGVRNQKKAHQMGERQFVYYNELASIAGIENIKPVIHKLMKDCGKKYIFELDTYRSNKYTILDDENFLKNGEAIV
Protein: Sodium/hydrogen exchanger (A8DYW5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004195}.
Interaction partners:
Sequence:
MLLIVGFALCVLAPGCSATDTDIALDAKATLNHRIQSLDLLVFVFLLALTVLTIWLFKHHRVSWLHETGLAVIYGLIVGAIIRYAGTSATLVHMQVEPQGVPTYSDKLPPDTLWFRYPVNQTNGTKPPEGIKTYAYVFRGQVHDVDENEIDLKATFDPEVFFNIILPPIIFYAGYSLKKKYFFRNLGAILTFAIVGTTLSAFLIGGFMYGCVKLMPKYLSSSFTFLDSLYFGALISPTDPLTILAIFNDLRVDVNLYALVLGESVLNDAVAIVLSGAIQNYGEHYSNTGEFETTAFLRSLSDFFSIFLLSLMIGAAMGCLTALMTKFTRVRDFPLLESALFVLMSYSTFLLAEATELTGVVAVLFCGICQAHYTYNNLSEDSRQRTKQIFELLNFLAENFIFSYIGVSMFTFPKHHFDAGFIITAFICAAIGRAVNVYPLSWLLNIKRKPKISTNFQHMLFFAGLRGAMSFALAIRNTVSDERQTMLTATSLIVIFTVVIQGGAANFLLNWLKIPVGVDDETEQLNNYQVHSDVEGGGVNRNKMRLSGGTDTNLDTPVDGTNGSLGGASGGRRRNSHEKAILARIWGNFDTKYMKPLLTHSRPTLLETLPVCCNPIARLLTTTQQLTQDGSEFRRVDSDSDICIDNDTGNGLSQDGSGAAPGVGRRNSLSRMEILEHVQSPVSTRIRLLGFYGKKL
Protein: Pyruvate carboxylase 1 (EC 6.4.1.1) (Pyruvic carboxylase 1) (PCB 1) (O17732)
Organism: Caenorhabditis elegans
Function: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11154}.
Interaction partners:
- Malic enzyme
- Probable citrate synthase, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Glutamate dehydrogenase
- Bifunctional glyoxylate cycle protein
- Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Malate dehydrogenase, mitochondrial
- Phosphoenolpyruvate carboxykinase
- L-lactate dehydrogenase
- Pyruvate kinase
Sequence:
MRFSRIPPIFANVVRQTHYRNYANGVIKPREFNKVMVANRGEIAIRVFRALTELNKTSVAIYAEQDKNSMHRLKADEAYLVGKGLPPVAAYLTIDQIIETALKHNIDAIHPGYGFLSERSDFAAACQNAGIVFIGPSPDVMARMGDKVAARQAAIEAGVQVVPGTPGPITTADEAVEFAKQYGTPIILKAAYGGGGRGIRRVDKLEEVEEAFRRSYSEAQAAFGDGSLFVEKFVERPRHIEVQLLGDHHGNIVHLYERDCSVQRRHQKVVEIAPAPALPEGVREKILADALRLARHVGYQNAGTVEFLVDQKGNYYFIEVNARLQVEHTVTEEITGVDLVQAQIRIAEGKSLDDLKLSQETIQTTGSAIQCRVTTEDPAKGFQPDSGRIEVFRSGEGMGIRLDSASAFAGSVISPHYDSLMVKVIASARNHPNAAAKMIRALKKFRIRGVKTNIPFLLNVLRQPSFLDASVDTYFIDEHPELFQFKPSQNRAQKLLNYLGEVKVNGPTTPLATDLKPAVVSPPIPYIPAGAKPPTGLRDVLVQRGPTEFAKEVRSRPGCMITDTTFRDAHQSLLATRVRTYDMAAISPFVAQSFNGLFSLENWGGATFDVSMRFLHECPWERLQTLRKLIPNIPFQCLLRGANAMGYSNYPDNVIYKFCELAVKNGMDVFRVFDSLNYLPNLLVGMEAVGKAGGVVEAAIAYTGDVTDKSRDKYDLKYYLNLADQLVKAQAHILSIKDMAGVLKPEAAKLLIGALRDKFPDIPIHVHTHDTSGAGVAAMLECAKAGADVVDAAVDSMSGMTSQPSMGAIVASLQGTKHDTGLSLDDISKYSAYWESTRQLYAPFECATTMKSGNADVYKHEIPGGQYTNLQFQAFSLGLGPQFDEVKRMYREANLVLGDIIKVTPSSKIVGDLAQFMVQNNLTRETLVDRADDLSFPKSVVDFMQGNVGQPPYGFPEPLRTKVLRGKPKVDGRPGENAKPVDLDAVKVELEEKHGRTLSEEDVMSYSMFPTVFDEFETFRQQYGPVDKLPTRLFLTGLEIAEEVDVEIESGKTLAIQLLAEGKLNKRGEREVFFDLNGQMRSIFVVDKEASKEIVTRPRALPGVRGHIGAPMPGDVLELKIKEGDKVTKKQPLFVLSAMKMEMVIDSPIAGTVKAIHAPQGTKCSAGDLVVEVEP
Protein: Myc box-dependent-interacting protein 1 (Amphiphysin II) (Amphiphysin-like protein) (Bridging integrator 1) (O08839)
Organism: Rattus norvegicus (Rat)
Function: Is a key player in the control of plasma membrane curvature, and membrane shaping and remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (By similarity). Is a negative regulator of endocytosis. Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (By similarity). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates. May be involved in the regulation of MYC activity and the control cell proliferation (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O08539}. Cytoplasm {ECO:0000250|UniProtKB:O08539}. Endosome {ECO:0000250|UniProtKB:O08539}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:9182667}.
Interaction partners:
- Dynamin-1
- Ras and Rab interactor 3
- Synaptojanin-1
- Dynamin-2
- Amphiphysin
- Myc proto-oncogene protein
- Clathrin heavy chain 1
- Protein B-Myc
- Clusterin
- Synaptojanin-2
Sequence:
MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLSECLQEVYEPEWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVSLEKQHGSNTFTVKAQPSDSAPEKGNKSPSPPPDGSPAATPEIRVNHEPEPASGASPGATIPKSPSQLRKGPPVPPPPKHTPSKEMKQEQILSLFDDAFVPEISVTTPSQFEAPGPFSEQASLLDLDFEPLPPVASPVKAPTPSGQSIPWDLWEPTESQAGVLPSGEPSSAEGSFAVAWPSQTAEPGPAQPAEASEVVGGTQEPGETAASEATSSSLPAVVVETFSATVNGAVEGSTTTGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVQ
Protein: Stx8 protein (Syntaxin-8) (Q7T361)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Vesicle transport through interaction with t-SNAREs 1B
- Vesicle-associated membrane protein 8
- Syntaxin-7
- Vesicle transport through interaction with t-SNAREs 1A
- Synaptobrevin homolog YKT6
- Syntaxin 16
- Syntaxin-12
- Syntaxin-18
- Vesicle-associated membrane protein 4.
- Syntaxin-5
Sequence:
MSKDLWLENYDAACRLAQEIAENIHERNRQQRTGGNPAKINMTLRASLQKLKQNIAQLRETLNRAAVQRHIMQAEADRRQSLVDDLASRETRLNASFKGDITEAEPSRSTLMAGGNGSGSAVNPWLINESEETKGLSFGEIKNQQQQIIEAQDAGLDALASVLSRQKQMGQEIGNELDEQNEIIDDLAQLVDKTDGRIKNETKRVKLLDSKSASCGMMVVIVLLLIAIIVVACWQ
Protein: Rhamnose binding lectin STL3 (Q9IB51)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MCILRLTVVTLLATACCTLTDGAISITCEGSDALLQCDGGKIHIKRANYGRRQHDVCSIGRPDHQLTDTNCLSQSSTSKMAERCGGKSECIVPASNFVFGDPCVGTYKYLDTKYSCVQQHETISSIICEGSDSQLLCDRGEIRIRLANYGRRQHDVCSIGRPHKQLKNTNCLSQSTTSKMAERCDGKRQCIVKVSNSVFGDPCVGTYKYLDVAYTCD
Protein: Egalitarian, isoform B (Egalitarian, isoform C) (Q9W1K4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein bicaudal D
- Dynein light chain 1, cytoplasmic
- Dumpy, isoform Q
- Protein gurken
- Maternal effect protein oskar
- DNA-binding protein K10
- FI20148p1
- Homeotic protein bicoid
Sequence:
MESMEYEMARNMTLLFFLERLLDKGEPRTVHDLSCQFGNKEFTKEMRQIAGGSQSGLKKFLAQYPAIFLVDGDYVQVNAYQHHNADDGGCGGKRDYIQEAKDYFKNKMLQYGAAAEVPVRSLLGHRSQASPQVRHISGQHIKEFTDFLMKHTDTFKVTDDYVMLVGCENMTDLPARDRLHLPQSNIDTRGTQQMLDFFAQCIEVKGPLLVDQLFHLLTTNFPQDQWLRMFKTPGDLSSFLKLFADCFHIQANLVTLLQKPKLSDTHIQQAQAQTREQFNALNNNNSASIRKQEPTPGGGGVGGVSSVQQRLQSPALRTNGHTNNNNGSNGSNNNNNNNNSIACPNFKLNAPVSNVMGGQSQGFGQPKSEPSSGFDSYVPMSELKLENLCENNYPSANTCYGPINNSSQQTQQVQTQQQQQPQHATQNPAEQRLNSVNQTLKQRINTLVIRTLAENLEKDKQSLANQQGGPISPHASPVHSIANSSSNQNAGSAANNANSNSNANPNNANHSPSHSYFVGDTWKIKVLQNTTVIANVKQSVFVTDIILKYAAKNESIVVSLDCEGINLGLKGEITLIEIGTTRGEAFLFDVQSCPAMVTDGGLKTVLEHDQVIKVIHDCRNDAANLYLQFGILLRNVFDTQAAHAILQYQESGKQVYKAKYISLNSLCEQYNAPCNPIKDQLKQIYRRDQKFWAKRPLTREMMLYAAGDVLVLIHDQLFGNLARQIKPENRALFSELCTEQILMQIKPNEVKIRKKQRKVSTEVSDLKQKLAQTSKSIVLSNREIRLLRYMDLTEDEKERLKGYYKVAKKLEKMESAGNPSKDQSDSEDEQEPNENDAFPSLDSVPSDNSLSGTFSPRFSSEPPSLTESMQMLEEILQNKSMDRIARIDKLEAILTTATSLPCEQIIASNSMQEQLGSSIATTENLQIIREKSKNIKNCNCQGERSVTPIMRTTDKRVVKLVDAESQTLSTGDVVITKIFFQDEHERAKEAALLSNSPAKRVSPT
Protein: Exocyst complex component sec8 (O74562)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the exocyst complex involved in the delivery of secretory vesicles to the plasma membrane. Also required for polarized cell growth and division septum assembly. The exocyst complex plays an important role in the targeting of rho3, as well as the two main hydrolases required for cell separation, eng1 and agn1, to the cell wall surrounding the septum before cell separation begins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16141239, ECO:0000269|PubMed:16823372}. Cell tip {ECO:0000269|PubMed:11854409}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11854409}. Cytoplasmic vesicle {ECO:0000269|PubMed:16141239}. Note=Associated with the actinomyosin ring at the division site and at the cell tips. {ECO:0000269|PubMed:11854409}.
Interaction partners:
- Exocyst complex component exo70
- Exocyst complex component sec10
- Exocyst complex component exo84
- Exocyst complex component sec15
- Exocyst complex component sec6
- Exocyst complex component sec5
- Uncharacterized protein C17G8.12
- GTP-binding protein rho3
- F-box protein pof6
- Cell division control protein 42 homolog
Sequence:
MDTRGYSETKKGRYPVGKKSLESPNGYSNYGTSMDNELSSEYASRGMHIGDLENLVNEIEDEWKDLGREDYQPISTALELLDDSSFGRDYKSFLNVYDRISAALQTIAHTHKDDFTRGISAYGEIMEGIQKCNSRIIALKQSLEASQECIGNTNSKELQQTLARSSQYKKVISVLKELNEANQLFDNFHTLVDSKQYYHASDLIRRVWDELSRSDFDGILVVEQFKSRMTGLLSHLEDILSEELVSITFLKDAVAYPIVSYCSPNPLRETSNPYFLRDFLKNNANTSTLGQSEQLRYLEEALSLKLSDCLKMDYGRDSLRDIRIVLESLNLLGKLPNAISSLKSRTSAEMFTTVDSTSRAIVNKYSLGNNVSTVNPFSKSLYDIGLHAETDREHTMISEFLTNLFTKLRCVLMHYRGISEFMTKLETKTPKHASSSHKSSIMSVNSDPTSPKVSKFDTSDSTFPFDTLLQAFESEIRLMLKDYLISKEEYIENSGNFVVGTEMSIYNLPGENEEDKLFDVTNEIAVENKSNAFYARINELVNEKAPELILNKSNASVSTIELFSGSSKEIVRLAGHVVFVGPSVFHASSVLPQTVFFLEDSVSILKNPNIPPQFAVNFMKEFLRGSYIPQLYKFMSSHFDTIMKDVGAFQLHRDWKIYSKIPIFKCHVAIVQYFHDLQDYLPIVALNLVEFYELLHTLLVRFRNHCSDYLSDLCRTAVLKEYKHVNEDTEDVDDTVRVKLLHDDVTYPQFIKFLKQKNPSLEGLNELCRMENKRLLQYEDRAITSEVKLPVSVLSKDSDLVNSVSYLHNSMEWFLQRCFSRFMNGSRRMNVLQQNQANFGGDFLPIDNLLGNNSDLMKGAYKEVFDSLQRLQFDALLLIRMEVRLQYIHSINQSVNLPDYVVEYRGRPDASIMALNSTIVTTNLKLETCLNEWERRFVFQGLSELVDSSLYSIFYKIESMNRGSCLQMLKNMSAMIQILKTVKEIHGDVEFPKSSRVFGIYQNGAKKIIEHFIAAPKKELLPDVKQMVRIYYQRLMKDAKRNGRDDLYRQYQKKIGSVLTQFDNTVGGARKNP
Protein: Adenosine kinase (AK) (EC 2.7.1.20) (Adenosine 5'-phosphotransferase) (A0A5K1VW94)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU368116}.
Interaction partners:
Sequence:
MTSVRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGDGVLLCHQAGVQWHDLGSLQPLPLGFKRLPCLSLPSSWRLQVFCLNWSLTSL
Protein: Insulin receptor substrate 1 (IRS-1) (P35569)
Organism: Mus musculus (Mouse)
Function: May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P35568}. Nucleus {ECO:0000250|UniProtKB:P35568}. Note=Nuclear or cytoplasmic localization of IRS1 correlates with the transition from proliferation to chondrogenic differentiation. {ECO:0000250|UniProtKB:P35568}.
Interaction partners:
- Insulin-1
- Growth factor receptor-bound protein 2
- Insulin-like growth factor 1 receptor
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Insulin-2
- Tyrosine-protein phosphatase non-receptor type 11
- Insulin receptor
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Insulin-like growth factor 1
- Insulin receptor substrate 2
Sequence:
MASPPDTDGFSDVRKVGYLRKPKSMHKRFFVLRAASEAGGPARLEYYENEKKWRHKSSAPKRSIPLESCFNINKRADSKNKHLVALYTRDEHFAIAADSEAEQDSWYQALLQLHNRAKAHHDGAGGGCGGSCSGSSGVGEAGEDLSYDTGPGPAFKEVWQVILKPKGLGQTKNLIGIYRLCLTSKTISFVKLNSEAAAVVLQLMNIRRCGHSENFFFIEVGRSAVTGPGEFWMQVDDSVVAQNMHETILEAMRAMSDEFRPRSKSQSSSSCSNPISVPLRRHHLNNPPPSQVGLTRRSRTESITATSPASMVGGKPGSFRVRASSDGEGTMSRPASVDGSPVSPSTNRTHAHRHRGSSRLHPPLNHSRSIPMPSSRCSPSATSPVSLSSSSTSGHGSTSDCLFPRRSSASVSGSPSDGGFISSDEYGSSPCDFRSSFRSVTPDSLGHTPPARGEEELSNYICMGGKGASTLAAPNGHYILSRGGNGHRYIPGANLGTSPALPGDEAAGAADLDNRFRKRTHSAGTSPTISHQKTPSQSSVASIEEYTEMMPAAYPPGGGSGGRLPGYRHSAFVPTHSYPEEGLEMHHLERRGGHHRPDTSNLHTDDGYMPMSPGVAPVPSNRKGNGDYMPMSPKSVSAPQQIINPIRRHPQRVDPNGYMMMSPSGSCSPDIGGGSSSSSSISAAPSGSSYGKPWTNGVGGHHTHALPHAKPPVESGGGKLLPCTGDYMNMSPVGDSNTSSPSECYYGPEDPQHKPVLSYYSLPRSFKHTQRPGEPEEGARHQHLRLSSSSGRLRYTATAEDSSSSTSSDSLGGGYCGARPESSLTHPHHHVLQPHLPRKVDTAAQTNSRLARPTRLSLGDPKASTLPRVREQQQQQQSSLHPPEPKSPGEYVNIEFGSGQPGYLAGPATSRSSPSVRCPPQLHPAPREETGSEEYMNMDLGPGRRATWQESGGVELGRIGPAPPGSATVCRPTRSVPNSRGDYMTMQIGCPRQSYVDTSPVAPVSYADMRTGIAAEKASLPRPTGAAPPPSSTASSSASVTPQGATAEQATHSSLLGGPQGPGGMSAFTRVNLSPNHNQSAKVIRADTQGCRRRHSSETFSAPTRAGNTVPFGAGAAVGGSGGGGGGGSEDVKRHSSASFENVWLRPGDLGGVSKESAPVCGAAGGLEKSLNYIDLDLAKEHSQDCPSQQQSLPPPPPHQPLGSNEGNSPRRSSEDLSNYASISFQKQPEDRQ
Protein: E3 ubiquitin-protein ligase HEL1 (EC 2.3.2.31) (Histone E3 ligase 1) (RING-type E3 ubiquitin transferase HEL1) (P36113)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation.
Interaction partners:
- RING-box protein HRT1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin
- Translation initiation factor eIF2B subunit epsilon
- E3 ubiquitin-protein ligase ITT1
- Cell division control protein 53
- F-box protein YDR131C
- Phosphatidylinositol 4-phosphate 5-kinase MSS4
- NEDD8-like protein RUB1
- Ubiquitin-conjugating enzyme E2 13
Sequence:
MSSGTENDQFYSFDESDSSSIELYESHNTSEFTIHGLVFPKLISVTSQDSEFDINEDEDGVDTIYEGMLDAPLTKNNKRILCEGSVPNLSYECLTTKGIFERMLQRVDHLQPIFAIPSADILILLQHYDWNEERLLEVWTEKMDELLVELGLSTTANIKKDNDYNSHFREVEFKNDFTCIICCDKKDTETFALECGHEYCINCYRHYIKDKLHEGNIITCMDCSLALKNEDIDKVMGHPSSSKLMDSSIKSFVQKHNRNYKWCPFADCKSIVHLRDTSSLPEYTRLHYSPFVKCNSFHRFCFNCGFEVHSPADCKITTAWVKKARKESEILNWVLSHTKECPKCSVNIEKNGGCNHMVCSSCKYEFCWICEGPWAPHGKNFFQCTMYKNNEDNKSKNPQDANKTLKKYTFYYRLFNEHEVSAKLDWNLGQTLGTKVHALQERIGISWIDGQFLSESLKVLNEGRTVLKWSFAVAYYSDASHNLTKIFVDNQMLLANAVESLSELLQIKTPEVIMKRRPEFYNKAGYVENRTTALMECGRELLCKGICKAAE
Protein: Putative sphingosine-1-phosphate lyase (Q67PY4)
Organism: Symbiobacterium thermophilum (strain DSM 24528 / JCM 14929 / IAM 14863 / T)
Interaction partners:
- Xylulose kinase
Sequence:
MLSAFSPPLPCDPARSHPTPEFPSSLQDYCEIRGIQSQPPARRDPTMDWLASLRSQIKPYRDRFPSHARLPRAGLPRAEILAEIAAMGAAESPAWRDGYASGAVYHGDEHHIAFLNEVYALQSQSNPLHPDLWPSTAKFEAEVVAMTAHMLGGDAAGGTVCGTVTSGGTESLLLAMKTYRDWARATKGITAPEAVVPVSAHAAFDKAAQYFGIKLVRTPLDADYRADVAAMREAITPNTVVVAGSAPGYPHGVVDPIPEIAALAAEHGIGCHVDACLGGFILPWAERLGYPVPPFDFRLEGVTSVSADTHKYGYGAKGTSVILYRRPDLLHYQYFIAADWPGGLYFSPTFAGSRPGALSATAWAAMLSLGEEGYLDATRRILQAADRLKAGVRAIPSLKILGDPLWVIAVASDELNIYQVMEEMAGRGWRLNGLHRPPAFHVALTLRHTEPGVVDRFLADLQDAVAQVRAHPEKATGMAPVYGMAAAAPPELVRQVLTGFIDLLYEV