wanglab/gogpt-training-data huggingface dataset:
Protein: Microfibril-associated glycoprotein 4 (P55083)
Organism: Homo sapiens (Human)
Function: Could be involved in calcium-dependent cell adhesion or intercellular interactions. May contribute to the elastic fiber assembly and/or maintenance.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:26601954}.
Interaction partners:
- Elastin
- Fibrillin-1
- Fibulin-5
- Fibulin-1
- Microfibrillar-associated protein 2
- EGF-containing fibulin-like extracellular matrix protein 1
- Lumican
- Fibulin-2
- Microfibrillar-associated protein 5
- Collagen alpha-1
Sequence:
MKALLALPLLLLLSTPPCAPQVSGIRGDALERFCLQQPLDCDDIYAQGYQSDGVYLIYPSGPSVPVPVFCDMTTEGGKWTVFQKRFNGSVSFFRGWNDYKLGFGRADGEYWLGLQNMHLLTLKQKYELRVDLEDFENNTAYAKYADFSISPNAVSAEEDGYTLFVAGFEDGGAGDSLSYHSGQKFSTFDRDQDLFVQNCAALSSGAFWFRSCHFANLNGFYLGGSHLSYANGINWAQWKGFYYSLKRTEMKIRRA
Protein: Caprin-1 (Cell cycle-associated protein 1) (Cytoplasmic activation- and proliferation-associated protein 1) (GPI-anchored membrane protein 1) (GPI-anchored protein p137) (GPI-p137) (p137GPI) (Membrane component chromosome 11 surface marker 1) (RNA granule protein 105) (Q14444)
Organism: Homo sapiens (Human)
Function: May regulate the transport and translation of mRNAs of proteins involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types. Binds directly and selectively to MYC and CCND2 RNAs. In neuronal cells, directly binds to several mRNAs associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs.
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:17210633, ECO:0000269|PubMed:31439799}. Cytoplasm, cytosol {ECO:0000269|PubMed:28733330}. Cell projection, dendrite {ECO:0000269|PubMed:35979925}. Cell projection, lamellipodium {ECO:0000269|PubMed:28733330}. Note=Mediates formation and localizes to cytoplasmic ribonucleoprotein membraneless compartments (PubMed:31439799). Associated with RNA granules. At the leading edge of migrating fibroblasts, colocalizes with DDX3X (PubMed:28733330). {ECO:0000269|PubMed:28733330, ECO:0000269|PubMed:31439799}.; SUBCELLULAR LOCATION: Cytoplasm, cytosol. Note=(Microbial infection) In case of reovirus infection, associates with the outer peripheries of viral factories in a G3BP1 dependent manner. {ECO:0000269|PubMed:28794026}.
Interaction partners:
- Ras GTPase-activating protein-binding protein 1
- Ras GTPase-activating protein-binding protein 2
- Fragile X messenger ribonucleoprotein 1
- RNA cytidine acetyltransferase
- Ubiquitin carboxyl-terminal hydrolase 10
- RNA-binding protein FXR2
- RNA-binding protein FXR1
- Nucleolysin TIAR
- Cytotoxic granule associated RNA binding protein TIA1
- Polyadenylate-binding protein 1
Sequence:
MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDEVRTDLKQGLNGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKVLKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPAVEDQVPEAEPEPAEEYTEQSEVESTEYVNRQFMAETQFTSGEKEQVDEWTVETVEVVNSLQQQPQAASPSVPEPHSLTPVAQADPLVRRQRVQDLMAQMQGPYNFIQDSMLDFENQTLDPAIVSAQPMNPTQNMDMPQLVCPPVHSESRLAQPNQVPVQPEATQVPLVSSTSEGYTASQPLYQPSHATEQRPQKEPIDQIQATISLNTDQTTASSSLPAASQPQVFQAGTSKPLHSSGINVNAAPFQSMQTVFNMNAPVPPVNEPETLKQQNQYQASYNQSFSSQPHQVEQTELQQEQLQTVVGTYHGSPDQSHQVTGNHQQPPQQNTGFPRSNQPYYNSRGVSRGGSRGARGLMNGYRGPANGFRGGYDGYRPSFSNTPNSGYTQSQFSAPRDYSGYQRDGYQQNFKRGSGQSGPRGAPRGRGGPPRPNRGMPQMNTQQVN
Protein: UV excision repair RAD23 protein, putative (Q587D1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-repair protein, putative
- Proteasome regulatory non-ATP-ase subunit 10
- Polyubiquitin, putative
- 26S proteasome regulatory subunit 4 homolog
- Telomerase-associated protein, putative
- Katanin p60 ATPase-containing subunit A-like 2
- 26S proteasome regulatory non-ATPase subunit
- Proteasome regulatory non-ATP-ase subunit 9
- 40S ribosomal protein S25
- 40S ribosomal protein S24
Sequence:
MRIILKSVLGKKREHEVSPDTKVEDIKKFLESEYTPQSLRLCYNNRVLEDPMTMEQLGIGEDTVIVYVGKKQSVQQLASKSGGCASPSAPAEGPAKGELNENPGVAGASSVPVDVPAPSPSAQAPATTQQPSGPAPASLRSVDPALIDSIVAMGFNDREQVSLALRAAYMNADRAVEFLCTGIPPHVQQQLAEADLQASAMGRAAVPSAGTPPSDAGSGGTQSDLRRALSAIPHIDDFRSLLQNNPQAFSALAGQLLENFPQVGELAQQDPEEFARFMMAGSVPDNADQTLVTAGETEVDDAQPLGEEDRAAVNRLVLLGEGAWGEREATEAYRMCGRREDAAAHFLLFNFLGITD
Protein: Nuclear receptor subfamily 5, group A, member 5 (F1QKV6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MRHKRDRQHELKPDPESSATQEEGCPVCGDRVSGYHYGLLTCESCKGFFKRSVQNNKRYTCAEAQNCPMDLAQRKRCPYCRFQKCVAVGMKKEAVRADRMRGGRNKFGPLYRRDRQLKQQRGTYHQANIAPYRVKIEGPQQLVPALPHDFHVINPNPASLGTDHYHPTQHFHPNMSQSEFPVLLDCTMPRDRTFSDPSLPIHTVCYPGIHGYPPDKREIPFNYNPASVTPPGPMSPTVLSTPAPTLTPASTPSSTPTPSQSLTPTSTTAPSSFFLNQLLQAEPDEKQLCMRVLASLQREQACRGKHDRLNTFSIMCKMADQTLFGLVEWARNCELFKELKVDDQMVLLQSCWSELLVLDHLCRQVAYGRDGSICLITGQQIEASTILSQAGMTLSSLVSRAQDLVTKLRSLQLDREEFVCLKYLVLFNPDVKSVQNRRQVEQTQERVNKALMDHTMQTHPGHSDKFGQLLLRLPEVRSISLQVEEYLYQRHLLGDLPCNSLLTEMLHAKHT
Protein: Calumenin (Crocalbin) (O35887)
Organism: Mus musculus (Mouse)
Function: Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low affinity (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43852}. Golgi apparatus {ECO:0000250|UniProtKB:O43852}. Secreted {ECO:0000250|UniProtKB:O43852}. Melanosome {ECO:0000250|UniProtKB:O43852}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:O43852}.
Interaction partners:
- Calreticulin
- Calreticulin
- Translocation protein SEC63 homolog
- Endoplasmic reticulum chaperone BiP
Sequence:
MDLRQFLMCLSLCTAFALSKPTEKKDRVHHEPQLSDKVHNDAQNFDYDHDAFLGAEEAKSFDQLTPEESKERLGKIVSKIDDDKDGFVTVDELKGWIKFAQKRWIHEDVERQWKGHDLNEDGLVSWEEYKNATYGYVLDDPDPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQETMEDIDKNADGFIDLEEYIGDMYSHDGNADEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDLFVGSQATDFGEALVRHDEF
Protein: Transmembrane protease serine 11D (EC 3.4.21.-) (Adrenal secretory serine protease) (AsP) (Airway trypsin-like protease) (AT) [Cleaved into: Transmembrane protease serine 11D non-catalytic chain; Transmembrane protease serine 11D catalytic chain] (Q8VHK8)
Organism: Mus musculus (Mouse)
Function: May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Preferentially cleaves the C-terminal side of arginine residues at the P1 position of certain peptides (By similarity). Plays a role in the proteolytic processing of ACE2. Isoform 2 may play a key role in regulating adrenal proliferation by specifically cleaving N-POMC.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Transmembrane protease serine 11D catalytic chain]: Secreted {ECO:0000250}. Note=Activated by cleavage and secreted. {ECO:0000250}.
Interaction partners:
- Furin
Sequence:
MYRPRPMLSPSRFFTPFAVAFVVIITVGLLAMMAGLLIHFLAFDKKAYFYHSSFQILNVEYTEALNSPATHEYRTLSERIEAMITDEFRGSSLKSEFIRTHVVKLRKEGTGVVADVVMKFRSSKRNNRKVMKTRIQSVLRRLSSSGNLEIAPSNEITSLTDQDTENVLTQECGARPDLITLSEERIIGGMQAEPGDWPWQVSLQLNNVHHCGGALISNMWVLTAAHCFKSYPNPQYWTATFGVSTMSPRLRVRVRAILAHDGYSSVTRDNDIAVVQLDRSVAFSRNIHRVCLPAATQNIIPGSVAYVTGWGSLTYGGNAVTNLRQGEVRIISSEECNTPAGYSGSVLPGMLCAGMRSGAVDACQGDSGGPLVQEDSRRLWFVVGIVSWGYQCGLPNKPGVYTRVTAYRNWIRQQTGI
Protein: Putative ATP-dependent RNA helicase SoYb (EC 3.6.4.13) (Sister of Yb) (Q9VL52)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in primary piRNA biogenesis in germline cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21863019}. Note=Localizes to Yb bodies.
Interaction partners:
- Protein vreteno
- Probable RNA helicase armi
- Inactive peptidyl-prolyl cis-trans isomerase shutdown
- Tudor domain-containing protein krimp
- Mitochondrial cardiolipin hydrolase
- Probable ATP-dependent RNA helicase spindle-E
- Qin
- Protein aubergine
- Splicing factor 3A subunit 2
- Splicing factor 3B subunit 4
Sequence:
MEHQLDPDQEESILITHFVNPHQFSYVRCIDVENSAMLVRQIEQDLKDYCSSERTKQVYVEDERVIVRYQRWSPPKLVRGVVRRRQNEEYLVWILDYGFNLCCSVWDLWPLPDHLSRSLCDFKEGGVALIAPHSGSVWSRSAIESLDKQLEDANQLTFQVVHRGKSNRNFGLLKFRSSCQTEDAANFLIKQDQGRCKETLTMAIPYEDISFEKAEINDMAIDTRPRLRRILELVVLLSENAKESTPTPSAIQQKKLDALLQSHETYLIPNSVKLLSKVQSISESSMQTALANRSKQISKELPHKANQSEDNRKKEVKYLESENLSECLSKVKLSSYQQKNTDSSTLSGPRNLASSSTNSNSNVRKSMTLFKSSGAHLTTSLSVPLTENCTNQSNNRTVVFSMDKMEQIFNDMLGKNPSERSVQKNRSQMPNSNVSTTKRCVEKMHVCRSENMGDRKPSVCLKHLVLAHSPEPVNPVTSYKELPLGNTILNAMDDLNFQTPLPTQIYAWPHLVNRGSLVLVNPSGTGRSWSYLPVICSSVLSSFENVTSNLDTRIAPGPLAILIVDSVENAKKLASHCEFLMKDFNTQNLKVVNTHAHSMMDVYMMLLNSCGVLVTTLAHLNNILSNELPLVNPTRLEFIIFDDYDRKRLDNAELLKEVFQKVNSIGGLSKQLVLVAQQWHSERFQKLLNRTTKPLILFGDFLEAALYGGLKFNVTLRSSALKARQLLDILAEQDGSKKRTLIYCKNQMELEELSAILIEAGLQCVDISKAQNQSPNRLMLVDDSQVRKQLPVRNIQLLIHFSLPESWLRFSRRFHTMADNIRNLFTKPIGRGQDLITYILMDENNAKEWPRIMKFLQDHGLTTQSMPDSEQQLDNTLPYCPYKLSNGNCNRNQCNKRHHFLKTDLPKIGNPLLQPGTLIRCKFLKAYDPAHMAVMPMKYKSKDSTIWIDVPYPSYPSTLVFKMSFGVPRKVHNPCKINDVCFVQHKELLSRVRIVDNPARPQVTVQLMDYGTELLQVKASQLLECPEQFRDLQQLAMDIRLSGLAGSGQGGMWSTDSIQWVQDRFADINEEIMQITVDFGVLDVAYVKEIALIEECPTMLTSVYKTFLRKELLRQGFAKIDSTSILELRAIHEQWKQEMEELRANKENIVCSSTDLDNRDSKITSLQNKQATCSSGKEEDLNPVETPLIIASPNSNETLEERKHVSDKVQNKIDELNDFNKSVEIEHVQDASPLDSSTALINTLIHELNTKSPTKKKNTQEFIKNIVHEDETQSIHHEISSSTNSLKQDKTIVVGPQDPPKELFLQYLNCATKSRESVYPMVKWHQTLTHIELVVEQQMLEYKLGLDGNTLEYKVNETTPPQRFILNLLGEVRIDSVKQHGYYLHIKLTKVGLLFHWPTLLNSLYVQKHAHWLIYDSERSHGPPPSFGLVLWEGYLTHKKTKSYSDSESSEFSSTPEDFIEPGVEYCEMDSNLYED
Protein: Meiotic driver wtf33 (A0A482AS24)
Organism: Schizosaccharomyces kambucha (Fission yeast)
Function: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele.
Subcellular location: [Isoform 1]: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
Interaction partners:
Sequence:
MKNKYYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSENLNLKDPKQMGANNPNLFNTDESTTPPDYGEDSLSTTHRENHSSGTADNSCASTLKKAILSFIPIFVLNVSAVCYLTYKDALFKDYGKDEWVYFGMWCASCLMILISLWCFYETWIKAVKVTAVFLAQCIKVTAVFLPQCIKVTAVFLAKCVKVTAVFLAKCIKVTAVFLAQCVKVTAISLAKCVKVISIGLFNIRREMMIIIWILWLIICCILFGCVKDGRLNFNKALICSTCTISAVLFLIVSSVCIPIWTLWRALSGMLQVLGIHGIIAVLVNGSMSLFGKHFGWRGYEIEGFVLFFTSSALFLYEMERPGVLKRMRNTTGNVIGYICGVIGDAFRRIENAFRGANDNNNIPLGEMDVEGEV
Protein: Transposon Ty1-DR5 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) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (P0C2I2)
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:
MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: NFX1-type zinc finger-containing protein 1 (Q9P2E3)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that initiates the antiviral response and is required to restrict the replication of RNA viruses. Acts as a double-stranded RNA (dsRNA) sensor that recognizes viral RNA and then interacts with MAVS to initiate the type I interferon response (By similarity). Also required for immunity against some bacteria, such as mycobacteria.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8R151}. Cytoplasm, Stress granule {ECO:0000269|PubMed:33876776}.
Interaction partners:
Sequence:
MEERRPHLDARPRNSHTNHRGPVDGELPPRARNQANNPPANALRGGASHPGRHPRANNHPAAYWQREERFRAMGRNPHQGRRNQEGHASDEARDQRHDQENDTRWRNGNQDCRNRRPPWSNDNFQQWRTPHQKPTEQPQQAKKLGYKFLESLLQKDPSEVVITLATSLGLKELLSHSSMKSNFLELICQVLRKACSSKMDRQSVLHVLGILKNSKFLKVCLPAYVVGMITEPIPDIRNQYPEHISNIISLLQDLVSVFPASSVQETSMLVSLLPTSLNALRASGVDIEEETEKNLEKVQTIIEHLQEKRREGTLRVDTYTLVQPEAEDHVESYRTMPIYPTYNEVHLDERPFLRPNIISGKYDSTAIYLDTHFRLLREDFVRPLREGILELLQSFEDQGLRKRKFDDIRIYFDTRIITPMCSSSGIVYKVQFDTKPLKFVRWQNSKRLLYGSLVCMSKDNFETFLFATVSNREQEDLCRGIVQLCFNEQSQQLLAEVQPSDSFLMVETTAYFEAYRHVLEGLQEVQEEDVPFQRNIVECNSHVKEPRYLLMGGRYDFTPLIENPSATGEFLRNVEGLRHPRINVLDPGQWPSKEALKLDDSQMEALQFALTRELAIIQGPPGTGKTYVGLKIVQALLTNESVWQISLQKFPILVVCYTNHALDQFLEGIYNCQKTSIVRVGGRSNSEILKQFTLRELRNKREFRRNLPMHLRRAYMSIMTQMKESEQELHEGAKTLECTMRGVLREQYLQKYISPQHWESLMNGPVQDSEWICFQHWKHSMMLEWLGLGVGSFTQSVSPAGPENTAQAEGDEEEEGEEESSLIEIAEEADLIQADRVIEEEEVVRPQRRKKEESGADQELAKMLLAMRLDHCGTGTAAGQEQATGEWQTQRNQKKKMKKRVKDELRKLNTMTAAEANEIEDVWQLDLSSRWQLYRLWLQLYQADTRRKILSYERQYRTSAERMAELRLQEDLHILKDAQVVGMTTTGAAKYRQILQKVEPRIVIVEEAAEVLEAHTIATLSKACQHLILIGDHQQLRPSANVYDLAKNFNLEVSLFERLVKVNIPFVRLNYQHRMCPEIARLLTPHIYQDLENHPSVLKYEKIKGVSSNLFFVEHNFPEQEIQEGKSHQNQHEAHFVVELCKYFLCQEYLPSQITILTTYTGQLFCLRKLMPAKTFAGVRVHVVDKYQGEENDIILLSLVRSNQEGKVGFLQISNRICVALSRAKKGMYCIGNMQMLAKVPLWSKIIHTLRENNQIGPMLRLCCQNHPETHTLVSKASDFQKVPEGGCSLPCEFRLGCGHVCTRACHPYDSSHKEFQCMKPCQKVICQEGHRCPLVCFQECQPCQVKVPKTIPRCGHEQMVPCSVPESDFCCQEPCSKSLRCGHRCSHPCGEDCVQLCSEMVTIKLKCGHSQPVKCGHVEGLLYGGLLVKCTTKCGTILDCGHPCPGSCHSCFEGRFHERCQQPCKRLLICSHKCQEPCIGECPPCQRTCQNRCVHSQCKKKCGELCSPCVEPCVWRCQHYQCTKLCSEPCNRPPCYVPCTKLLVCGHPCIGLCGEPCPKKCRICHMDEVTQIFFGFEDEPDARFVQLEDCSHIFEVQALDRYMNEQKDDEVAIRLKVCPICQVPIRKNLRYGTSIKQRLEEIEIIKEKIQGSAGEIATSQERLKALLERKSLLHQLLPEDFLMLKEKLAQKNLSVKDLGLVENYISFYDHLASLWDSLKKMHVLEEKRVRTRLEQVHEWLAKKRLSFTSQELSDLRSEIQRLTYLVNLLTRYKIAEKKVKDSIAVEVYSVQNILEKTCKFTQEDEQLVQEKMEALKATLPCSGLGISEEERVQIVSAIGYPRGHWFKCRNGHIYVIGDCGGAMERGTCPDCKEVIGGTNHTLERSNQLASEMDGAQHAAWSDTANNLMNFEEIQGMM
Protein: Target of rapamycin complex 1 subunit toc1 (TORC1 subunit toc1) (Q9HDW0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Tor2 is essential for growth. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls cell growth and ribosome biogenesis by regulating ribosomal protein gene expression. TORC1 negatively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Represses mating, meiosis and sporulation efficiency by interfering with the functions of the transcription factor ste11 and the meiosis-promoting RNA-binding protein mei2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Target of rapamycin complex 1 subunit tco89
- Target of rapamycin complex 2 subunit bit61
- Serine/threonine-protein kinase tor2
- Target of rapamycin complex 2 subunit sin1
- Serine/threonine-protein kinase tor1
- Uncharacterized protein C22H10.11c
- Target of rapamycin complex 2 subunit ste20
- Target of rapamycin complex subunit wat1
- Target of rapamycin complex 1 subunit mip1
Sequence:
MQLQSPFGDGISCECLNIRVLGIPNETKHQWIFVPRDLIKIKIYSLLQICKAENCSAVACRGCNLCILAVQGNIEISEEPQKLFQEENVKVYIYDSAISLSSVRASFPISELGIRMDIIKARAEPREDEIRASFSSLVNKEIKRTVEELLLSKRSTNRLSLLAFMRNQQLNYEAYETKLLEDASTIEKSLEKEVKTIYDSNIASPKESSDAIDADHAMIDESRSTQRRKSKPKKHVAFTDEYQVAFSDKPGKYFNQPMQYSKQFKLDNPDYEASSDSLNDIENLSTLTFRSDEELEFDFDTNNINNNKSGDSLEMSTTIPSDEENEDFTSKVDAMEIHSGSLPLNIDSSPIFTNHSPSSSLSSESSFEASPSSFVDRKNRWIQMLKKADEHSRSIQARSMGYVLSDDLDNSKAFRPYKQSFLAQGWKSLN
Protein: Gamma-aminobutyric acid receptor subunit alpha-4 (GABA(A) receptor subunit alpha-4) (GABAAR subunit alpha-4) (P48169)
Organism: Homo sapiens (Human)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9D6F4}; Multi-pass membrane protein {ECO:0000269|PubMed:35355020, ECO:0007744|PDB:7QN5}. Postsynaptic cell membrane; Multi-pass membrane protein {ECO:0000269|PubMed:35355020, ECO:0007744|PDB:7QN5}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit delta
- Gamma-aminobutyric acid receptor subunit beta-3
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid receptor subunit gamma-2
- Vesicle-fusing ATPase
- Inactive phospholipase C-like protein 1
- Huntingtin-associated protein 1
- Trafficking kinesin-binding protein 2
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid receptor-associated protein
Sequence:
MVSAKKVPAIALSAGVSFALLRFLCLAVCLNESPGQNQKEEKLCTENFTRILDSLLDGYDNRLRPGFGGPVTEVKTDIYVTSFGPVSDVEMEYTMDVFFRQTWIDKRLKYDGPIEILRLNNMMVTKVWTPDTFFRNGKKSVSHNMTAPNKLFRIMRNGTILYTMRLTISAECPMRLVDFPMDGHACPLKFGSYAYPKSEMIYTWTKGPEKSVEVPKESSSLVQYDLIGQTVSSETIKSITGEYIVMTVYFHLRRKMGYFMIQTYIPCIMTVILSQVSFWINKESVPARTVFGITTVLTMTTLSISARHSLPKVSYATAMDWFIAVCFAFVFSALIEFAAVNYFTNIQMEKAKRKTSKPPQEVPAAPVQREKHPEAPLQNTNANLNMRKRTNALVHSESDVGNRTEVGNHSSKSSTVVQESSKGTPRSYLASSPNPFSRANAAETISAARALPSASPTSIRTGYMPRKASVGSASTRHVFGSRLQRIKTTVNTIGATGKLSATPPPSAPPPSGSGTSKIDKYARILFPVTFGAFNMVYWVVYLSKDTMEKSESLM
Protein: Delta(1)-pyrroline-2-carboxylate reductase (Pyr2C reductase) (EC 1.5.1.49) (D7A0Y0)
Organism: Ancylobacter novellus (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIMB 10456) (Starkeya novella)
Function: Catalyzes the reduction of Delta(1)-pyrroline-2-carboxylate (Pyr2C) to L-proline, using NADPH as the electron donor. Is likely involved in a degradation pathway that converts cis- and trans-3-hydroxy-L-proline (c3LHyp and t3LHyp) to L-proline, which would allow S.novella to grow on c3LHyp or t3LHyp as a sole carbon source.
Interaction partners:
- Trans-3-hydroxy-L-proline dehydratase
- Malate dehydrogenase
Sequence:
MDEPVRLSLAEVHVLCRDTLVAAGLGEEHAQAIARSITRAEADECHSHGLYRLIGYVASVRSGKAERHALPALARATPAVLRVDAKHGFAPLAVETGVPALIAAAKEIGIAALAIHDCYHFSALWADIEPAVEAGLAAWCFTVGQCCVAPAGGTTPLLGTNPFAFGWPGPSGRPFIFDFATSAAARGEIELKRRGGEKIPPGWAVGPDGAPTTDPAAALAGALLPFGGHKGSALSMMVELIAGPLIGDLTSRQSKAVENGDGGPPLGGELFIAIDPAVFGTGNLSSRLADADELFALAKAQPGVRLPSERRYQARERSRTNGIAVPAALFAELQALGPRGS
Protein: Tropomyosin Mac r 1.0101 (Major allergen Mac r 1.0101) (allergen Mac r 1.0101) (V5NBV4)
Organism: Macrobrachium rosenbergii (Giant fresh water prawn)
Function: Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
Interaction partners:
Sequence:
MDAIKKKMQAMKLEKDNAMDRADTLEQQNKEANNRAEKSEEEVFSLQKRMQQLENDLDSVQEALLKANQHLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELSGY
Protein: Uncharacterized protein (Q38C58)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEDTAAFSAVLQRSAPVTRRRVLVVLFALGKYAKRENTELSPSAIMTLLEYVMVGKPVRFLFASGAGGSVLRSHDRGFTWRVVYRIRDNVTDVVPTRRQPAGTLGAVGETKALSETGGNIASKDEVIPPSAVEPENHTSCIATMDDRVAVCGDNGFLAVSVDRGLSFSKLAKEAFHPFGEGGSNNESNCSDFRGVEFLSECALVFFSKRHLFRCPLNQKSYNSVEFGDISLLQAFSDPIGCVRTFSRAGRGCMRELFVATNGFVHYSHDGGAVLLKIPHKLGVIRSIEPMDVVLRHREIPQLPPSLIDAMTAPAVERHLSAEKEKYSYSVVVRATGAQDKGVGDSGCDFCEGWVDGISLPHRLGSVCYRVLLVAGCGANILPYDCTALLFVAASSNGPDTTPDVLGSLAEHVDYVPYIKSGITEPLSVALTRRPGSGGCVFARSNIAGVSFSSDMGRSWSIPKQAYVVSVLASDGGEFVCCNRRNVVNFPNSVCEEVHALQTDLRVPFLTDIAMMT