wanglab/gogpt-training-data huggingface dataset:
Protein: Inactivation-no-after-potential D protein (Q24008)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the negative feedback regulation of the light-activated signaling cascade in photoreceptors through a calcium-mediated process. Interacts with tetrapeptide ligand located in C-terminal sequence of 3 key components of the visual cascade, tethering them and forming a macromolecular signaling phototransduction complex.
Subcellular location: Cell projection, rhabdomere {ECO:0000269|PubMed:9010208}.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Protein kinase C, eye isozyme
- Transient-receptor-potential-like protein
- Transient receptor potential protein
- Neither inactivation nor afterpotential protein C
- Opsin Rh1
- Calmodulin
- Calmodulin-related protein 97A
- MIP05401p
- FI14603p
Sequence:
MVQFLGKQGTAGELIHMVTLDKTGKKSFGICIVRGEVKDSPNTKTTGIFIKGIVPDSPAHLCGRLKVGDRILSLNGKDVRNSTEQAVIDLIKEADFKIELEIQTFDKSDEQQAKSDPRSNGYMQAKNKFNQEQTTNNNASGGQGMGQGQGQGQGMAGMNRQQSMQKRNTTFTASMRQKHSNYADEDDEDTRDMTGRIRTEAGYEIDRASAGNCKLNKQEKDRDKEQEDEFGYTMAKINKRYNMMKDLRRIEVQRDASKPLGLALAGHKDRQKMACFVAGVDPNGALGSVDIKPGDEIVEVNGNVLKNRCHLNASAVFKNVDGDKLVMITSRRKPNDEGMCVKPIKKFPTASDETKFIFDQFPKARTVQVRKEGFLGIMVIYGKHAEVGSGIFISDLREGSNAELAGVKVGDMLLAVNQDVTLESNYDDATGLLKRAEGVVTMILLTLKSEEAIKAEKAAEEKKKEEAKKEEEKPQEPATAEIKPNKKILIELKVEKKPMGVIVCGGKNNHVTTGCVITHVYPEGQVAADKRLKIFDHICDINGTPIHVGSMTTLKVHQLFHTTYEKAVTLTVFRADPPELEKFNVDLMKKAGKELGLSLSPNEIGCTIADLIQGQYPEIDSKLQRGDIITKFNGDALEGLPFQVCYALFKGANGKVSMEVTRPKPTLRTEAPKA
Protein: Luciferase-like monooxygenase (P0ADV5)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Alkanesulfonate monooxygenase
Sequence:
MTDKTIAFSLLDLAPIPEGSSAREAFSHSLDLARLAEKRGYHRYWLAEHHNMTGIASAATSVLIGYLAANTTTLHLGSGGVMLPNHSPLVIAEQFGTLNTLYPGRIDLGLGRAPGSDQRTMMALRRHMSGDIDNFPRDVAELVDWFDARDPNPHVRPVPGYGEKIPVWLLGSSLYSAQLAAQLGLPFAFASHFAPDMLFQALHLYRSNFKPSARLEKPYAMVCINIIAADSNRDAEFLFTSMQQAFVKLRRGETGQLPPPIQNMDQFWSPSEQYGVQQALSMSLVGDKAKVRHGLQSILRETDADEIMVNGQIFDHQARLHSFELAMDVKEELLG
Protein: tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (Pombe glycoprotease 1) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein pgp1) (tRNA threonylcarbamoyladenosine biosynthesis protein pgp1) (O94710)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179, ECO:0000269|PubMed:16823372}.
Interaction partners:
- EKC/KEOPS complex subunit SPAP27G11.07c
- EKC/KEOPS complex subunit SPAC4H3.13
- EKC/KEOPS complex subunit cgi121
- Probable U3 small nucleolar RNA-associated protein 18
- Threonylcarbamoyl-AMP synthase
Sequence:
MLCLVYNSILCKQRRISLKVLQQFRCWNISKTFLSYRTLTALAIETSCDDTSVSVVRTSDSSSHCQNEIICLNTHRTISKYEAYGGIHPTIVIHEHQKNLAKVIQRTISDAARSGITDFDLIAVTRGPGMIGPLAVGLNTAKGLAVGLQKPLLAVHHMQAHALAVQLEKSIDFPYLNILVSGGHTMLVYSNSLLNHEIIVTTSDIAVGDYLDKCAKYLGIPWDNEMPAAALEQFASPEINSTSYSLKPPIPLNTREKVHSASFSFSGLESYACRIIRKTPLNLSEKKFFAYQLQYAAFQHICQKTLLALKRLDLSKVKYLVCSGGVARNELLKKMLNDTLMVLQFEHQPTDIKLVYPSPDICSDNAAMIGYTAIQMFKAGYTSSFDVEPIRKWPINQILTVEGWLTKKNKKV
Protein: FG-GAP repeat protein, putative (Q584V4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- FG-GAP repeat protein, putative
- PTHB1 N-terminal domain-containing protein
- Bardet-Biedl syndrome 8 protein
- BBSome complex member BBS5 PH domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- propanoyl-CoA C-acyltransferase
- Nonspecific lipid-transfer protein, putative
- Anaphase-promoting complex subunit 5
- Kinesin-like protein
Sequence:
MRTAFQLSLNASLNEGLAAIGRFDGKTPSLVCATNTRQVIVHTHDTSNPLAAHREDASVAPLRTFNFGKALTALATGPIGGRYENEGVDALFLGEANSLLAYDVERNCEYYYKQVEDGVSAVVGGVVGPTAKSGPAPLAIVGGDCAISGFNSSGEEVFSTITGDRVTALMLMPWPDAGVCASTSTLNGSPALVAASEDFELRVFDGEEPITSVGLADRVHSLVYSGVPGRFAYLSNSGTVGIYDRCERLYRLKDNQRPVSAAFCDVDMDGVPELIIGWNNGRVEVRSGDGNEGTVLCKETFDAPISSVLVDDYRQNGQPLPIICTVDGTVCGLQLTGTMGRHEAMVAQREGALKLDMLMREKQALEKELANVKEQLVRQKSGRTDVTLPKVGTGVDCKLQPNSQTGKLDVVFSVINGQQDTIIYACILSSEAMFPEKGHILFMSQDPLPTLVCGLDVPRGPEVTLKASVMVGSTNAVNYQVHEVDVVVPKFVMCRLWPNEWCRGSFSEPTGSVTLQLSKDFDFGSVSLWLQKTFDVPLDRVPDTASDFSVPFVDLQDRSGLVIRGILSRCELQICGNSMDICSILVESFATTCVTEATSRCDFPEDFQQLQETVERVIDLDKVRQKLSDDIAEAATNIKPLLVRAEDSRLISDIVSMRRHYSQLYELDKELIDENLKLSNNFKELKSALKRLNGFIAKAGKLRIGRARTQLVAECRECVKASNMQSLINLIRTGEK
Protein: Fat1 protein (Q80XT9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
GSPFTIDPVRGEVKVTKPLDRETISGYTLTVQAADNGNPPRVNTTTVNIDVSDVNDNAPLFSRDNYSVIIQENKPVGFSVLKLVVTDKDSSHNGPPFFFTIVSGNDENAFEVNQHGVLLTAATIKRKVKDHYLLHVKVADSGKPQLSSMTHIDIRVIEESIHPPAILPLEIFITAFGEEYSGGVIGKIHATDQDVYDTLMYSLDPHMDGLFSVSSTGGKLIAHRKLDIGQYLLNVSVTDGKFTTVADITVHIQQVTQEMLNHTVAIRFANLTPEEFVGDYWRNFQRALRNILGVRKNDIQIVSLQPSEPHSHLDVLLFVERSGGTHVSTKQLLHKINSSVTDVEEIIGVRILEVFQKLCAGLDCPWKFCDEKVSVDENVMSTHSTARLSFVTPRHHRTAVCLCKDGTCPPVHHGCEDNPCPAGSECVADPREEKYSCVCPGGGFGKCPGSSSITFTGNSFVKYRLLENENRLEMKLSMRLRTYSSHAVVMYARGTDYSILEIHTGRLQYKFDCGSGPGIVSVQSIQVNDGQWHAVSLEVEGNYAKLVLDEVHTASGTAPGALKTLNLDNYVFFGGHLRQQGTKHGRGAQVASGFRGCMDSIYLNGQELPLNNKPRAYAHIEEWVDLSHGCLLTATEDCSSSPCQNGGVCNPSPTGGYYCKCSALYVGTFCEVSVNPCSSNPCLYGGTCMVDNGGFVCQCRGLYTGQRCQLSPYCKDDPCKNGGTCFDSLDGAVCQCDSGFRGERCQSDIDECAGNPCRNGALCENTHGSYHCNCSQEYRGKHCEDASPNHYVSTPWNIGLAEGIGIIVFIAGIVLLVMVFVLCRKMISRKKKRQAEPEDKRLGPTTAFLQRPYFDSKLNKNIYSDIPPQVPVRPISYTPSIPSDSRNNLDRNSFEGSAIPEHPEFSTFNPESMHGHRKAVAVCSVAPNLPPPPPSNSPSDSDSIQKPSWDFDYDAKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNGYHWDTSDWMPSVPLPDIQEFPNYEAIDEHTPLYSADPNAIDTDYYPGGYDIESDFPPPPEDFPAPDELPPLPPEFSDQFESIHPPRDMPAAGSLGSSSRSRQRFNLNQYLPNFYPADMSEPQKQGAGENSPCREPYTPYPPGYQRNFEAPTIENMPMSVYASTASCSDVSACCEVESEVMMSDYESGDDGHFEEVTIPPLDSQQHTEV
Protein: Spindle pole body component alp4 (Altered polarity protein 4) (Q9Y705)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the gamma tubule complex that is required for the regulation of both interphase microtubules and mitotic bipolar spindles. Required for correct septation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:11080156, ECO:0000269|PubMed:16111942, ECO:0000269|PubMed:16823372}. Note=Localizes to the SPB and also to the equatorial MTOC.
Interaction partners:
- Tubulin gamma chain
- Spindle pole body component alp6
- Mitotic-spindle organizing protein 1
- Spindle pole body component alp16
- Gamma-tubulin complex subunit mod21
- Gamma-tubulin complex component gfh1
- Gamma tubulin complex adapter mto1
- DASH complex subunit ask1
- Kinesin-like protein 1
- Kinesin-like protein cut7
Sequence:
MVRSISSVLAKEESENGSPIPALEEGSVYHVSLKSEGVSPFSDRIQLNYLYDGKTFSDPSNLNIHQQEACLINELLNAFMGMEGVFVHLQDMKASSEFETIIMPPSFYILPGFDLGIKDIASEMLEMGSHYLSITAFIESRSHFEYGFVNHALCAALRKFVMDYVVLIMQCENQSRIDPNFSLQTLRLYTLPTSRSLRQVYLILRDLLLSMEKNASSSDDLGLSNIDDLLEQLNEGNDISHVVNATRSKKKVCKGGQVISFLTESLTKYAGDPVARKILTYLLREASRPYTKMLNEWIHLGLVNDPYDEFMIKIHKGITSMQLDEDYTDEYWEKRYVIREDQVPPQLLDLQNKVLFAGKYLNVVLECRKGVNNLASLNAKDDTQNQLLWPSTFDDDNFTLNIMNAYVYANESLLQLLQSSQSLYAHLYSLKHYFFLDQSDFFTTFLDNAQHELRKPAKYISITKLQSQLDLALRQPGTITATDPHKEYVTVEVNQTSLIDWLMHIVSISGLEEGTSSQGNEVWNESITKQADVGNETRNFESEHNRSTQGTSKVGSDKDINGFETMQLCYKVPFPLSLILSRKAIIRYQLLFRYFLLLRHVEMQLENSWVQHSKNSAWRLNSSNAKIEQWKRNSWLLRTRMLSFVQKIIYYTTSEVIETHWGKFMGELENARTVDNLMQEHIDFLDTCLKECMLTNSRLLKVQSKLLNTCAMFASYTSTFTRSLYLLENSEESFDEGRMDKMEEILRRYEDSFSRHLKSLVNACNYFASTETAALLSLVMKLTG
Protein: Gibberellin-regulated protein 6 (GAST1 protein homolog 6) (Q6NMQ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Gibberellin-regulated protein that may function in hormonal controlled steps of development such as seed germination, flowering and seed maturation.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Cytomegalovirus UL139 protein
- DELLA protein GAI
Sequence:
MAKLITSFLLLTILFTFVCLTMSKEAEYHPESYGPGSLKSYQCGGQCTRRCSNTKYHKPCMFFCQKCCAKCLCVPPGTYGNKQVCPCYNNWKTQQGGPKCP
Protein: Transposon Ty1-NL1 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q12112)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQTAQSHSPQNGPYQQQCMMTQNQANPSGWSFYGRPSMIPYTPYQMSPMYFPPGPHSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFLNWVKTYIKFLQNSNLGDIIPTATRKAVRQMTDDELTFLCHTFQLFAPSQFLPTWVKDILSADYTDIMKILSKSINKMQSDTQEVNDITTLATLHYNGSTPADAFEAEVTNILDRLNNNGIPINNKVACQFIMRGLSGEYKFLRYARHRYIHMTVADLFSDIHSMYEEQQESKRNKSTYRRNPSDEKKDSRTYTNTTKPKSITRNSQKPNNSQSRTARAHNVSTSNNSSGPDNDLIRGSTTEPIQLKNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPGINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISKSNILPSKKRSSTPQISDIESTGSGGMHRLDVPLLAPMSQYNTHESSHTSKSKDFRHSDSYSDNETNHTNVPISSTGGTNNKTVPQTSEQETEKRIIHRSPSIDTSSSESNSLHHVVPIKTSDTCPKENTEESIIADLPLPDLPPEPPTKLSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDRYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIEKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Uncharacterized MFS-type transporter YhjX (P37662)
Organism: Escherichia coli (strain K12)
Function: Part of a nutrient-sensing regulatory network composed of the two-component regulatory systems BtsS/BtsR and YpdA/YpdB, and their respective target proteins, BtsT and YhjX.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23222720}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23222720}.
Interaction partners:
- Sensor histidine kinase YpdA
- Transcriptional regulatory protein YpdB
- Sensor histidine kinase BtsS
- Pyruvate/proton symporter BtsT
- Transcriptional regulatory protein BtsR
- Kdo
- Oxalyl-CoA decarboxylase
- Glycerol-3-phosphate transporter
Sequence:
MTPSNYQRTRWLTLIGTIITQFALGSVYTWSLFNGALSAKLDAPVSQVAFSFGLLSLGLAISSSVAGKLQERFGVKRVTMASGILLGLGFFLTAHSDNLMMLWLSAGVLVGLADGAGYLLTLSNCVKWFPERKGLISAFAIGSYGLGSLGFKFIDTQLLETVGLEKTFVIWGAIALLMIVFGATLMKDAPKQEVKTSNGVVEKDYTLAESMRKPQYWMLAVMFLTACMSGLYVIGVAKDIAQSLAHLDVVSAANAVTVISIANLSGRLVLGILSDKIARIRVITIGQVISLVGMAALLFAPLNAVTFFAAIACVAFNFGGTITVFPSLVSEFFGLNNLAKNYGVIYLGFGIGSICGSIIASLFGGFYVTFYVIFALLILSLALSTTIRQPEQKMLREAHGSL
Protein: D(1A) dopamine receptor (Dopamine D1 receptor) (B8YLW8)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell projection, cilium membrane {ECO:0000256|ARBA:ARBA00004272}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004272}.
Interaction partners:
Sequence:
MTWNDTTMDGEGLLVERDSSFRILTGCFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVSEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPKAAFIMISVAWTLSVLISFIPVQLNWHKATTTSFLDLNASLQGISMDNCDSSLNRMYAISSSLISFYIPVAIMIVTYTRIYRIAQKQIRRISALERAAVHAKNCQNTSGNRSSMDCQQPESNFKMSFKRETKVLKTLSVIMGVFVCCWLPFFVLNCMIPFCEPTQPSKGAEAFCINSTTFDVFIWFGWANSSLNPIIYAFNADFRKAFSTLLGCYRLCPMSGNAIETVSINNNGAVVFSSQHEPKGSSPKESNLVYLIPHAIICPEEEPLKKEEEGELSKTLEKMSPALSGILDYEADVSLEKINPITQNGQHKT
Protein: Probable magnesium transporter NIPA2 (B3LFA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+) (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Note=Recruited to the cell membrane in response to low extracellular magnesium. {ECO:0000250}.
Interaction partners:
- Purple acid phosphatase 22
- Gamma-glutamylcyclotransferase 2-1
- Cation/H
- Glutaredoxin-C11
- Protein NRT1/ PTR FAMILY 6.1
- Transmembrane 9 superfamily member 4
- Protein ECERIFERUM 26
- Probable beta-D-xylosidase 2
- DNA repair DEAD helicase RAD3/XP-D subfamily protein
- Disease resistance like protein
Sequence:
MEEMSPDNIHGVILAVSSSIFIGSSFIIKKKGLKKAGVSGARAGEGGYGYLYEPWWWAGMITMIVGEIANFAAYAFAPAILVTPLGALSIIFSAVLAHFILEEKLHMFGILGCVLCVVGSTTIVLHAPHEQGIESVKQVWHLATEPGFLAYSAVVLVVVLALIFYYEPRYGKTHMIVYVGICSLMGSLTVMSVKAVAIAIKLTFSGMNQFKYFHAWIFIIVVTICCILQINYLNKALDNFNTAVISPVYYVMFTTFTILASMIMFKDWASQSGLQIATELCGFVTILSGTFLLHKTKDMGNSTSLRGSTSHSPRDTPVFINSGSSRSSNSTRPAIL
Protein: Caspase-7 (CASP-7) (EC 3.4.22.60) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11] (F1NV61)
Organism: Gallus gallus (Chicken)
Function: Thiol protease involved in different programmed cell death processes, such as apoptosis, pyroptosis or granzyme-mediated programmed cell death, by proteolytically cleaving target proteins. Has a marked preference for Asp-Glu-Val-Asp (DEVD) consensus sequences, with some plasticity for alternate non-canonical sequences (By similarity). Its involvement in the different programmed cell death processes is probably determined by upstream proteases that activate CASP7 (By similarity). Acts as an effector caspase involved in the execution phase of apoptosis: following cleavage and activation by initiator caspases (CASP8 and/or CASP9), mediates execution of apoptosis by catalyzing cleavage of proteins. Compared to CASP3, acts as a minor executioner caspase and cleaves a limited set of target proteins (By similarity). Acts as a key regulator of the inflammatory response in response to bacterial infection by catalyzing cleavage and activation of the sphingomyelin phosphodiesterase SMPD1 in the extracellular milieu, thereby promoting membrane repair (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P55210}. Nucleus {ECO:0000250|UniProtKB:P55210}. Secreted, extracellular space {ECO:0000250|UniProtKB:P97864}. Note=Following cleavage and activation by CASP1 or granzyme B (GZMB), secreted into the extracellular milieu by passing through the gasdermin-D (GSDMD) pores or perforin (PRF1) pore, respectively. {ECO:0000250|UniProtKB:P97864}.
Interaction partners:
- E3 ubiquitin-protein ligase XIAP
- Inhibitor of apoptosis protein
- Poly [ADP-ribose] polymerase 1
- Actin, cytoplasmic 1
- Baculoviral IAP repeat containing 5
- Caspase 9
- Caspase-8
- Apoptotic protease-activating factor 1
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MSGDQHADRSSGEKSNGDQDDTVDAKPDRSSRLSLFAKKKKNGEEEQPKSSLSNQYRIVTPTFQYNMNYKKVGKCIIINNKNFEDKTGMGTRNGTDKDAGDLSKSFRSLGFDVYTYNDRSCEDMQTLLKQAAEENHSDAACFACILLSHGEEGLIYGTDGPMAIKHLTTLFRGDKCKTLIGKPKLFFIQACRGSEFDEGIQTDSGPANDTLETDANPRYKIPVEADFLFAYSTVPGYYSWRNPGRGSWFVQSLCSVLNEHGKQLEIMQILTRVNYVVATNFESQSDDPRFSEKKQIPCVVSMLTKELYF
Protein: Antiviral protein SKI8 (Superkiller protein 8) (Q02793)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in double-strand break (DSB) formation during meiotic recombination through stabilization of SPO11 association with meiotic chromosome and helping SPO11 to recruit other DSB proteins like REC102 and REC104 to meiotic chromosomes. Also a component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for controlling the propagation of M double-stranded RNA (dsRNA) and thus for preventing virus-induced cytopathology.
Subcellular location: Cytoplasm. Nucleus. Chromosome. Note=Relocalizes from the cytoplasm to the nucleus and is recruited to chromosomes by SPO11 during meiotic prophase.
Interaction partners:
- RNA polymerase-associated protein CTR9
- Superkiller protein 3
- Cell division control protein 73
- Antiviral helicase SKI2
- Superkiller protein 7
- RNA polymerase-associated protein RTF1
- Meiotic recombination protein REC104
- Meiosis-specific protein SPO11
- Meiotic recombination protein REC102
- RNA polymerase II-associated protein 1
Sequence:
MSKVFIATANAGKAHDADIFSVSACNSFTVSCSGDGYLKVWDNKLLDNENPKDKSYSHFVHKSGLHHVDVLQAIERDAFELCLVATTSFSGDLLFYRITREDETKKVIFEKLDLLDSDMKKHSFWALKWGASNDRLLSHRLVATDVKGTTYIWKFHPFADESNSLTLNWSPTLELQGTVESPMTPSQFATSVDISERGLIATGFNNGTVQISELSTLRPLYNFESQHSMINNSNSIRSVKFSPQGSLLAIAHDSNSFGCITLYETEFGERIGSLSVPTHSSQASLGEFAHSSWVMSLSFNDSGETLCSAGWDGKLRFWDVKTKERITTLNMHCDDIEIEEDILAVDEHGDSLAEPGVFDVKFLKKGWRSGMGADLNESLCCVCLDRSIRWFREAGGK
Protein: Golgi reassembly stacking protein 1 (B1WBR1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004394}.
Interaction partners:
Sequence:
MGLGASSEQPAGGEGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEHVWHVLDVEPSSPAALAGLRPYTDYIVGSDQILQESEDFFTLIESHEGKPLKLMVYNSESDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPSSQYKKPPSASSPGTPAKTPQPNAFPLGAPPPWPIPQDSSGPELGSRQSDYMEALPQVPGGFMEEQLPGPGSPGHGTADYGGCLHSMEIPLQPPPPVQRVMDPGFLDVSGMSLLDSSNTSVCPSLSSSSLLTPTAVSALGPEDIGSSSSSHERGGEATWSGSEFEISFPDSPGSQAQVDHLPRLTLPDGLTSAASPEEGLSAELLEAQTEEPADTASLDCMAETEGPAGQVQAAPDPEPGL
Protein: Large ribosomal subunit protein uL22A (60S ribosomal protein L17-A) (L20A) (YL17) (P05740)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS19
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein eL21A
- Large ribosomal subunit protein eL34A
- Large ribosomal subunit protein eL24A
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL33A
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL31A
Sequence:
MARYGATSTNPAKSASARGSYLRVSFKNTRETAQAINGWELTKAQKYLEQVLDHQRAIPFRRFNSSIGRTAQGKEFGVTKARWPAKSVKFVQGLLQNAAANAEAKGLDATKLYVSHIQVNQAPKQRRRTYRAHGRINKYESSPSHIELVVTEKEEAVAKAAEKKVVRLTSRQRGRIAAQKRIAA
Protein: Pumillio RNA binding protein, putative (Q389G5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSTKEPLHMFSLGVTERSWDDDDGNAQHQQRQQPMPLKIGSEQGGGVYNSNVAQLQAHGRSDFGATGEILGSSSYPSNTPPPGTGSNAMGWVRYTAMDFELLLHEGKQPTDDMRRSQVYAKWYQTKRLTDDRVLPPLTNPRYDAKGDAEAPWDPVVPMRIQGQQSVAGGGGSELVGKGGIRMELDTKNLQQAHEQQTFNPYAMCFQQQDDNIMSPGTQFFGAYAPTPLATMATPNTLRAYAHSRMGTQVRNNNNVNRGEITQIMAPVAGQTLYNSDWNATGDFTAAQGMVPNVCQQYYTQEQMNTFDYYADPTVVNYYNTATTNVTDHTQMQPAIMAIAPTGDMGALRGPAGSAGPMAGPSGGATRGGRRSGGRGRGGNSGKWGSGAARGRGTAPRESTQPCSELLEHFRTDAASGGVSQWRIAHILNHAVEFAQDQEGSRFIQRAVESATHDEVDALFREIFESPLELVVDVFGNYVLQKLLEVGNARQLAYAATRLQNNVVNLTLQTYGCRVIQKCIEVMPPEGLDIILSELRGNVAKCIQDQNGNHVVQKCVEVIPQRCGFIVSAFSGRVMELATHAYGCRVIQCIMDHCPDQEEAIFSELLDCVGTLATDQYGNYVIQHVLQHMKDDEKVGRIFDALKGNFYESSKQKFASNVMEKLFVRADPQQRMELVNMMCSPIGDDSGEPVEVLSFKRSSAPKKENVEKQRNEYAKKGRRDRERDREKENSLGLVVEVQLAGREPPSMLCLMMQNPFANYVAQRVLDAAHVDQYVCLIDNIQKFLLPISTYTYGAPIVQRLVRRELVKAPDDVSLNLAVSAVSAGGRGSYGHHRREAREHFDAE
Protein: Ribosyldihydronicotinamide dehydrogenase [quinone] (EC 1.10.5.1) (NRH dehydrogenase [quinone] 2) (NRH:quinone oxidoreductase 2) (Quinone reductase 2) (QR2) (P16083)
Organism: Homo sapiens (Human)
Function: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MAGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLEPRATDKDITGTLSNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ
Protein: Olfactory receptor (Q9JKA6)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
Sequence:
MTWGNWTTVREFILMSFSSLSYEVQALLFLLFLIIYLVTLMGNVLIILVTTADSALQSPMYFFLRNLSFLEIGFNLVIVPKMLSTLILQDKTISFLGCATQMYFFFFFGAAECCLLATMAYDRYMAICDPLHYPIIMSRRSCAQLAAASWFSGFPVATVQTTWIFSFPFCGPNMVNHFFCDSPPVIALVCADTSLFELEALTATVLFILFPFLLILGSYVRILSTIFRMPSAEGKRKAFSTCSSHLLVVSLFYSTAILTYFRPRSNTSPENKKMLSLSYTVITPMLNPIIYSLRNNEVKAALRRIIHRTLGPQKL
Protein: Synaptogyrin-2 (Cellugyrin) (O54980)
Organism: Rattus norvegicus (Rat)
Function: May play a role in regulated exocytosis. In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles. May also play a role in GLUT4 storage and transport to the plasma membrane.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:12928441, ECO:0000269|PubMed:26071524}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:12928441, ECO:0000269|PubMed:9446595}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to cytoplasmic vesicles associated with the recycling endosomes. {ECO:0000269|PubMed:10967091}.
Interaction partners:
- Transmembrane channel-like protein
Sequence:
MESGAYGAANAGGSFDLRRYVSQPQVVTRLVSMVLALIVFSCIFGEGYINLHSSDQLHCVFNRNEDACRYGSAIGVLAFLASAFFLVVDAFFSQISNATDRKYLVIGDLLFSALWTFLWFVGFCFLTNQWAATKPDDVLVGADSARAAITFSFFSIFSWGVLASLAYQRYKAGVDAFIQNYVDPTPDPTTAYASYPSASVENYQQPPFTQNVETTEGYQPPPVY