wanglab/gogpt-training-data huggingface dataset:
Protein: polynucleotide adenylyltransferase (EC 2.7.7.19) (A0A0B4KG96)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Symplekin
- Probable cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor 73
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 4
- Factor interacting with poly
- LD24014p
- Cleavage stimulation factor 64 kD subunit
- Polyadenylate-binding protein 2
- Protein suppressor of forked
Sequence:
MWNSEPTHRQHHQHNGNSTSGGPPAKQLGMTSAISLAEPRPEDLQRTDELRGSLEPYNVFESQDELNHRMEILAKLNTLVKQWVKEISVSKNMPESAAEKLGGKIYTFGSYRLGVHHKGADIDALCVAPRNIERTDYFQSFFEVLKKQPEVTECRSVEEAFVPVIKMNFDGIEIDLLFARLSLKEIPDDFDLRDDNLLRNLDHRSVRSLNGCRVTDEILALVPNIENFRLALRTIKLWAKKHGIYSNSLGYFGGVTWAMLVARTCQLYPNAAAATLVHKFFLVFSRWKWPNPVLLKHPDNVNLRFQVWDPRVNASDRYHLMPIITPAYPQQNSTFNVSESTKKVILTEFNRGMNITDEIMLGRIPWERLFEAPSFFYRYRHFIVLLVNSQTADDHLEWCGLVESKVRLLIGNLERNPHIALAHVNPKCFEFKKGQSANNSQNNSGNEDDLKQSQGNQSAVTSAPFCSMWFIGLEFERSENLNVDLTESIQNFTEHVMMHGVNIKMLKEGMTIDARHVKRKQLSLYLDSDFLKRERKSMESHNNFNNTLLANRKRLSTELAQSQDPLPPGQQPSSGNRGRDSGAKIQRLSDSLTEENSNASSDMGAGTPTTPTTAQLSAPSFKSSGKNGSEIDVVEQEPTQPHNNGNASSNTTTTEVACSXQPPTLHPHPPHQQPPPAPPQPPAHHHHHQKFRKNNNAAAAAASNSIFNQRSILHAASSLSAALSITGHKRKQQTATSTTMISSSNIAHSNYTQHSTHNNNGGGGGSHYNKTYYIDDDDEDNNQPLLTPNNQTQQQQKAVRITATSASPATSVPVAASAAPPAPTISL
Protein: Pro-opiomelanocortin protein (Proopiomelanocortin) (Proopiomelanocortin a precursor) (Q7ZT18)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Melanocortin 2 receptor.
- Melanocortin receptor 4
- Melanocyte-stimulating hormone receptor
- Melanocortin 3 receptor
- Agouti-related neuropeptide.
- Prodynorphin.
- Corticotropin-releasing hormone b.
- Melanocortin receptor 5
- Melanocortin receptor 5
- Melanocortin 2 receptor accessory protein.
Sequence:
MVRGVRMLCPAWLLALAVLCAGGSEVRAQCWENARCRDLSTEENILECIQLCRSELTDETPVYPGESHLQPPSEPEQIDLLAHLSPVALAAPEQIEPESGPRHDHKRSYSMEHFRWGKPVGRKRRPIKVYTNGVEEESAETLPAEMRRELANNEVDYPQEEMPLNPLGKKDPPYKMTHFRWSVPPASKRYGGFMKSWDERAQKPLLTLFKNVMHKDQPRKDE
Protein: Uncharacterized protein, isoform C (A0A0B4LI09)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH01369p
- Sidestep VI, isoform B
Sequence:
MHLTKLPTRSSSSSSRIAYKFECHSNSKQNSKTGKMAAEARTISKPGHIRDRRVGSLPHILFLAIAVVSLHFESVSAQSMMTKNEPMFISRSETFKFITGETIVLPCEVANTDTYVVAWKRGIAILTAGSVKVTPDPRVRLVNGFNLQIRDALPTDAGDYICQIATMDPREITHTVEILVPPRIHHISTGGHLQVKKGSSVRIECSATGNPMPNVTWSRKNNILPNGEEKLHSHVLSIENVDRHKGGVYICTANNRVGQPASSQVVLHVLFSPEISVERPVVFSGEGHEATLVCIVHGETQPEVIWFKDTMQLDTTERHIMETRGSRHTLIIRKVHPQDFGNYSCVAENQLGKARKTLQLSGKPNVAVFNSPPISQYKDRYNISWAVDSHSPIEEYKLSFRKLPQGHEVVGNAIDSSSSSSSMSSSSSQMYGSGLHAHRIGSNMGGLSGLSGSGSYSGYGNVIHWGHNDWRNVVLPAVPVSHHYAQGMSYMVRGLDPDQHYEATVQSRNRYGWSDLTNSFVFSTSSNDGPVDLSTFLNHGLSDNEMRDLSVTFYGSSAINRQKLGLLALSSATLALSLLVA
Protein: Acetyl-CoA hydrolase (EC 3.1.2.1) (Acetyl-CoA deacylase) (G8B6P2)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Acetyl-coenzyme A synthetase
- Acetyl-coenzyme A synthetase
- Malate synthase
- acetyl-CoA C-acetyltransferase
- Acetyltransferase component of pyruvate dehydrogenase complex
- Aldehyde dehydrogenase domain-containing protein
- Aldehyde dehydrogenase domain-containing protein
- 2-isopropylmalate synthase
Sequence:
MSSILKQRVRYAPYLKKLRTGQECIELFQNGQYLGWSGFTGVGAPKVIPTVLADHVENNKLQDKLGFHLFVGASAGPEESRWANNNMLLSRSPHQVGKPIAAAINDGRTQFFDKHLSMFPQDLTYGFYTKDKPNGSNLDITIIEATAIKEDGSIVPGPAVGASPEMISVSDKVIIEVNTKTPSFEGIHDIDMPVNPPFRQPYPHTSADYKIGQTSIPVDPSKVVAIVESTSGDKVPPNTASDEQSKAIANHLVEFLEHEVKQGRLPENLHPLQSGIGNIANAVVEGLASSNFKNLTVWTEVLQDSFLDFFESGSLDYATATSIRLTEEGFEKFYSHWDTYSKKLCLRSQAVSNSPEIIRRLGVIAMNTPVEVDIYGHANSTNVMGSRMLNGLGGSGDFLRNAKLSIMHTPSARPSKIDPTGVSCIVPMAPHVDQTEHDLDVIVTEQGLADLRGLSPKERARVIIQKCAHPDYKDQLSDYLDRAIYECTKRKTLHEPHSLRDVFKMHLNFQDNGTMKLDSW
Protein: AA9 family lytic polysaccharide monooxygenase cel61A (LPMO9 cel61A) (EC 1.14.99.56) (Cellulase-61A) (Cel61A) (Endo-beta-1,4-glucanase cel61A) (Endoglucanase cel61A) (Endoglucanase IV) (Glycosyl hydrolase 61 family protein cel61A) (O14405)
Organism: Hypocrea jecorina (Trichoderma reesei)
Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. May be involved in the degradation of complex natural cellulosic substrates.
Subcellular location: Secreted {ECO:0000305|PubMed:9370370}.
Interaction partners:
Sequence:
MIQKLSNLLVTALAVATGVVGHGHINDIVINGVWYQAYDPTTFPYESNPPIVVGWTAADLDNGFVSPDAYQNPDIICHKNATNAKGHASVKAGDTILFQWVPVPWPHPGPIVDYLANCNGDCETVDKTTLEFFKIDGVGLLSGGDPGTWASDVLISNNNTWVVKIPDNLAPGNYVLRHEIIALHSAGQANGAQNYPQCFNIAVSGSGSLQPSGVLGTDLYHATDPGVLINIYTSPLNYIIPGPTVVSGLPTSVAQGSSAATATASATVPGGGSGPTSRTTTTARTTQASSRPSSTPPATTSAPAGGPTQTLYGQCGGSGYSGPTRCAPPATCSTLNPYYAQCLN
Protein: Accessory Sec system protein Asp2 (Accessory secretory protein Asp2) (Orf2) (Q9AET8)
Organism: Streptococcus gordonii
Function: Part of the accessory SecA2/SecY2 system specifically required to export GspB, a serine-rich repeat cell wall protein encoded upstream in the same operon.
Interaction partners:
Sequence:
MKNKLKILQIGSIDWSKEVVIPDNMDWYYFFSLTLRLAIKKVMEMEKINHFSAIIVDDLDLIPDLFLIESRIIPYTIFYSKKQQAIQEPIAFFLKRYCAQQIDLSDRPNLLRKLSKALFRGQYGDKMTPLDMVVSPGFKGRICHNGYENLELEGNFGSDFRPIVSWKYNIVASKKNPVEIWLEYEKDLSCELRLRIYNIQEGSAADLVRESVFSETDMEETIVLDNDFTSFLGITLEARGFGTLKIGAFHQRLTRYQFGKFVLGGKILKDSHRQEINYFFYPGDFKPPLVVYFSGYRRAEGFEGFGMMRGLGCPFLLISDQRLDGGVFYLGSDELEEGIRRIIQEHMELLGFSERELILSGISMGTYGAAYYGADFSPRAIILCKPLANLGTIAQRGRLRLPEVFPMALDILHRHTGGKDRENVMELDNRYWKKFKKADFSRTIFGLAYMKEEDYDPTAYEDLVQYLYPTETQLMSNGLSGRHNDDSTMVINWFMNYHRIILEKEFGRKK
Protein: Zinc finger MYM-type containing 3 (A6NL54)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDPSDFPSPFDPLTLPEKPLAGDLPVDMEFGEDLLESQTAPTRGWAPPGPSPSSGALDLLDTPAGLEKDPGVLDGATELLGLGGLLYKAPSPPEVDHGPEGTLAWDAGDQTLEPGPGGQTPEVVPPDPGAGANSCSPEGLLEPLAPDSPITLQSPHIEEEETTSIATARRGSPGQEEELPQGQPQSPNAPPSPSVGETLGDGINSSQTKPGGSSPPAHPSLPGDGLTAKASEKPPERVQKRSERVRRAEPPKPEVVDSTESIPVSDEDSDAMVDDPNDEDFVPFRPRRSPRMSLRSSVSQRAGRSAVGTKMTCAHCRTPLQKGQTAYQRKGLPQLFCSSSCLTTFSKKPSGKKTCTFCKKEIWNTKDSVVAQTGSGGSFHEFCTSVCLSLYEAQQQRPIPQSGDPADATRCSICQKTGEVLHEVSNGSVVHRLCSDSCFSKFRANKGLKTNCCDQCGAYIYTKTGSPGPELLFHEGQQKRFCNTTCLGAYKKVGPRE
Protein: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 (EC 3.6.4.-) (HepA-related protein) (mharp) (Sucrose nonfermenting protein 2-like 1) (Q8BJL0)
Organism: Mus musculus (Mouse)
Function: ATP-dependent annealing helicase that binds selectively to fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA. May play an important role in DNA damage response by acting at stalled replication forks (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Note=Recruited to damaged DNA regions. {ECO:0000250}.
Interaction partners:
- DNA-directed primase/polymerase protein
- Replication protein A 14 kDa subunit
- Replication protein A 70 kDa DNA-binding subunit
- Replication protein A 32 kDa subunit
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- DNA helicase B
- Tonsoku-like protein
- Fanconi anemia group M protein homolog
- DNA repair protein RAD51 homolog 1
- DNA polymerase delta subunit 3
Sequence:
MSLPLTEEQRKKIEENRQKALARRAEKLSEQPQSAASGSSAAGPSQSKQGSLLNLLAEPSKPVGHASIFKQQNLSNSFPTDQRPHSSRCSQPSPAEETTGLWKTQGEMSTACPKPNPSPPGASNQPLLGYKSSEGQPQATWDTGASSSGPFPRDPELEAKAARPSTSRQSISDSFYVLGGKTPRTEGRPPNILQTTPQNTGFLRGACIKTGDRFRVKIGYNQELIAVFKSLPSRHYDSFTKTWDFSMSDYRALMKAVERLSTVSLKPLDEAGGSVGGQTSLPSAPSLTFVTGKCMLISRVRFEVDIGYSEAVIGLFKQMESRSYDIKTRKWSFLLEEHNKLIARSRELKQVQLDPLPKTVTLAFASQLEKTSPKLKADVPEADLSGVDAKLVSSLMPFQREGVSFAISKRGRLLLADDMGLGKTVQAICIAAFYRKEWPLLVVVPSSVRFTWEQAFLRWLPSLSPENINVVVTGKGRLTAGLVNIVSFDLLCKLERQLKTPFKVVIIDESHFLKNIKTARCRAAVPILKVAKRVILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAKRLPWGWDYSGSSNLGELKLLLEEAIMLRRLKSDVLSQLPAKQRKMVVVNPGRISSRAKAALDAAAKEMTKDKTKQQQKEALLVFFNRTAEAKIPCVVEYILDLLDSGREKFLVFAHHKVILDAVAKELERKNVQHIRIDGSTPSADREAQCQRFQLSKGHTVALLSITAANMGLTFSTADLVVFAELFWNPGVLIQAEDRVHRIGQTNSVSIHYLVAKGTADDYLWPLIQEKIKVLGEAGLSETNFSEMTEATDYVHKDPKQKTIYDLFQQSFEDDGNDMEFLEAAESFELGSTSGTSGNISQDLGDLLDEDEGSPPKKSRFEFFDNWDSFSSPF
Protein: Midkine-A (MK-A) (XMK) (Pleiotrophic factor-alpha-1) (PTF-alpha-1) (X-PTF-alpha1) (P48530)
Organism: Xenopus laevis (African clawed frog)
Function: Secreted protein that functions as cytokine and growth factor and mediates its signal through cell-surface proteoglycan and non-proteoglycan receptors. Binds cell-surface proteoglycan receptors via their chondroitin sulfate (CS) groups. Thereby regulates many processes like inflammatory response, cell proliferation, cell adhesion, cell growth, cell survival, tissue regeneration, cell differentiation and cell migration (By similarity). Inhibits mesoderm formation and promotes neural formation during development. Plays a role in development of the neuromuscular junction (NMJ). Has antibacterial activity against both Gram-positive and Gram-negative bacteria.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MELRAFCVILLITVLAVSSQAAKNKKEKGKKGASDCTEWTWGSCIPNSKDCGAGTREGTCKEETRKLKCKIPCNWKKAFGADCKYKFENWGECNATTGQKVRSGTLKKALYNADCQQTVEATKPCSLKTKSKSKGKKGKGKE
Protein: Type IV pilus inner membrane component PilM (G3XD28)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19857645}. Note=Localizes to the inner membrane through interaction with PilN. {ECO:0000269|PubMed:19857645}.
Interaction partners:
- Fimbrial assembly protein PilQ
- Type IV pilus inner membrane component PilO
- Type IV pilus inner membrane component PilN
- Type IV pilus inner membrane component PilP
- Type IV pilus retractation ATPase PilT
- Type IV pilus ATPase PilU
- Type IV pilus non-core minor pilin PilE
- Type IV pilus assembly protein PilF
- Prepilin leader peptidase/N-methyltransferase
- Type 4 fimbrial biogenesis protein PilZ
Sequence:
MLGLIKKKANTLLGIDISSTSVKLLELSRSGGRYKVEAYAVEPLPPNAVVEKNIVELEGVGQALSRVLVKAKTNLKSAVVAVAGSAVITKTIEMEAGLSEDELENQLKIEADQYIPYPLEEVAIDFEVQGLSARNPERVDVLLAACRKENVEVREAALALAGLTAKVVDVEAYALERSYALLSSQLGADTDQLTVAVVDIGATMTTLSVLHNGRTIYTREQLFGGRQLTEEIQRRYGLSVEEAGLAKKQGGLPDDYDSEVLRPFKDAVVQQVSRSLQFFFAAGQFNDVDYIVLAGGTASIQDLDRLIQQKIGTPTLVANPFADMALNGKVNAGALASDAPALMIACGLALRSFD
Protein: Small ribosomal subunit protein eS6 (40S ribosomal protein S6) (P62755)
Organism: Rattus norvegicus (Rat)
Function: Component of the 40S small ribosomal subunit (By similarity). Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62753}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62753}.
Interaction partners:
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein eS24
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein eS1
- Ubiquitin-ribosomal protein eL40 fusion protein
- Small ribosomal subunit protein uS9
Sequence:
MKLNISFPATGCQKLIEVDDERKLRTFYEKRMATEVAADALGEEWKGYVVRISGGNDKQGFPMKQGVLTHGRVRLLLSKGHSCYRPRRTGERKRKSVRGCIVDANLSVLNLVIVKKGEKDIPGLTDTTVPRRLGPKRASRIRKLFNLSKEDDVRQYVVRKPLNKEGKKPRTKAPKIQRLVTPRVLQHKRRRIALKKQRTKKNKEEAAEYAKLLAKRMKEAKEKRQEQIAKRRRLSSLRASTSKSESSQK
Protein: Protein NUCLEOLAR FACTOR 1 (Q8H1E7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2 (By similarity). Involved in the control of rRNA expression. Required for embryo development and female gametogenesis.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:20877469, ECO:0000269|PubMed:27792779}.
Interaction partners:
- Protein THALLO
- AT1G07840 protein
- Nucleolar protein
- Putative WD-repeat membrane protein
- M phase phosphoprotein 10
- rRNA biogenesis protein RRP36
- Nucleolar-like protein
- Protein SLOW WALKER 1
- Putative U3 small nucleolar ribonucleoprotein
- DEAD-box ATP-dependent RNA helicase 36
Sequence:
MAPNATGVLKRHRSHEKFDKKRDTKKHKHVEKTIVSNPSTDSPEESSIEAESEAMVYREPTQYQNLLVSLGSSNKVVADMNKRRQREEEGKSDTEEDEDDEDEDEEENSGSDDLSSTDGEDDKSQGDDQETLGGLTDDTQEDNDNQSEEEDPDDYETDEEVHELSTNGQSFVDASSSISAFSEHLSHKLSSEEVETLPKGKWKFKWESPAFDMPNCKWKGTSENFLDGIQSDAPYGLKPKLYNHWLQLYKKCGGKDLDSSKRRKFFSICNSYLDILHSNKKPFYHCGSDEDSSAMDAYLMHSLNHIFKTRDLVKKNESKIAKHRETSEEEILSDDGFLDQGFTRPKVLILLPLRSIAFRVVKRLIQLTPESQRVNVEHLDRFNDEFGCEEDTDDCDGEKTTSKNGNSIKQKSSKPSDWQALFGANNNDDEFMLGIKHTRKSIRLYGDFYSSDIIVASPLKLHMAIGAAEENKERDVDYLSSIEVLVIDHADIISMQNWSFLATVVDYLNRLPTKQHGTNVMRIRPLYLDGHARFYRQSIILSSYLTPEMNSLFGRHCLNYKGKMKMACEYKGVLEKVLLPVRQIYERFDAASITQVDDARLEYFTKKIFPKIKDSVQGGVMIFIHSYFEFVRLRNFLNTQNTSFCLLGDYAKNADISRAREQFFVGSRKIMLYTERAYFYKRYKIRGIKNLILYSLPERKEFYPEIMNMLEEGSHDMMSTALFSRFDMLQLERIVGSTSAKRMITSEKNMFAFC
Protein: Flagellin (Q48824)
Organism: Legionella pneumophila
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362073}. Bacterial flagellum {ECO:0000256|RuleBase:RU362073}.
Interaction partners:
Sequence:
MAQVINTNVASLTAQRNLGVSGNMMQTSIQRLSSGLRINSAKDDAAGLAISQRMTAQIRGMNQAVRNANDGISLSQVAEGAMQETTNILQRMRELSVQAANSTNNSSDRASIQSEISQLKSELERIAQNTEFNGQRILDGSFSGASFQVGANSNQTINFSIGSIKASSIGGIATATGTEVAGAAATDITIAIGGGAATSINSSANFTGALNGQDATSAYAKAAAINDAGIGGLSVTASTSGTQAVGAIGGTAGDTYNLTINGVAIYTNLDVATALTNSDLRDAINGVSNQTGVVASLNGGNMTLTAADGRNITVTESGTGFTAGTDGLTVTGGAFDGRLRGTLSISAVDTIAIGGTVANIGLSANISKDTVGIDSLDVSTGSGRQTAIKRIDAALNSVNSNRANMGALQNRFESTIANLENVSDNLSAARSRIQDADYAAEMASLTKNQILQQAGTAMLAQANSLPQSVLSLLGR
Protein: Kinesin-like protein 2 (EC 5.6.1.4) (Q9US03)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Microtubule-dependent motor that is involved in microtubule organization in the mitotic spindle. Required for the polarization of interphase microtubules where it orients the microtubule plus ends toward the cell ends and the minus ends toward the cell center. Mediates minus end-directed sliding of cytoplasmic microtubules relative to each other, thereby promoting mitotic spindle disassembly.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16002618}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18256284}. Nucleus {ECO:0000269|PubMed:16002618, ECO:0000269|PubMed:18256284}. Note=When in the nucleus, it associates with chromatin (PubMed:16002618). Localizes to nuclear microtubules (PubMed:18256284). {ECO:0000269|PubMed:16002618, ECO:0000269|PubMed:18256284}.
Interaction partners:
- Kinesin-like protein cut7
- Anaphase spindle elongation protein 1
- Microtubule integrity protein mal3
- Dynein heavy chain, cytoplasmic
- Kinesin-like protein 6
- Kinesin-like protein 5
- ADP-ribosylation factor 1
- Tubulin alpha-2 chain
- Kinesin-like motor protein 9
- Spindle pole body component alp14
Sequence:
MEEEGHKSLTSHLPQSSSSLSQSREIAKEFTSNIPPPTIKTNSSSSNILKPRLSLQNEVNQLKPAKFPSKMLPPGSLASVKSSSLAKKARPFTASSNPRMPKSAHPISSRSVSASSHFGRPASAVSSSLNSSDDVRSMSDESMESYNDEKSVNASALRTTEDRLRSMEMAYAQLSAKVIPSPSKRPANYKFYEQRIAMLEESLEVERSRTSELQEQFSVALREKAEAEANKIVSQKGMESLEIMLNSMKSENHQRMAMLEENHARVMETAELQHQAELQDFASNIEQKANSLIMEYKNELQSAEEHFSHKIKELTSENELKISRLQEEKDSLLKKVQEGASLAMQRVQNKHDLEKKRLQSAIQPLQEENNSLKQQIEQLQRELASETVVKENLKSSLDQQSANVQKLESTNRALESTIKTLEEDVYTMKNKIIELEGILKSANVERDGLVEKLIAEETLRRKLHNTIQELKGNIRVFCRVRPPLGDGESAQIAFPDQNSEASTIEIVAQAPGSSLTGNGIKQYAFNFDRVFSPETTNEDVFNELSQLIQSAMDGYNVCIFAYGQTGSGKTHTMSSNTGMIPSSVRMIYNRSTSLKERGWEYRMEGQFLEIYNETIIDLLASGNEEEKGKKKLEIYHDTKAGRTTITNITSEPLDTPEQVTWLLDQASKNRSVAATNANEHSSRSHSVFMLHLNGSNSTTGETCRSTLNLIDLAGSERLSSSQSVGERLKETQAINKSLSCLGDVIHALGSGKEGTYIPYRNSKLTNLLQYSLGGNSKTLMFVNISPLKQHVPETLCSLRFATKVNNTQIGTARKVTK
Protein: Interferon-induced GTP-binding protein Mx1 (Interferon-induced protein p78) (IFI-78K) (Interferon-regulated resistance GTP-binding protein MxA) (Myxoma resistance protein 1) (Myxovirus resistance protein 1) [Cleaved into: Interferon-induced GTP-binding protein Mx1, N-terminally processed] (P20591)
Organism: Homo sapiens (Human)
Function: Interferon-induced dynamin-like GTPase with antiviral activity against a wide range of RNA viruses and some DNA viruses. Its target viruses include negative-stranded RNA viruses and HBV through binding and inactivation of their ribonucleocapsid. May also antagonize reoviridae and asfarviridae replication. Inhibits thogoto virus (THOV) replication by preventing the nuclear import of viral nucleocapsids. Inhibits La Crosse virus (LACV) replication by sequestering viral nucleoprotein in perinuclear complexes, preventing genome amplification, budding, and egress. Inhibits influenza A virus (IAV) replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. Enhances ER stress-mediated cell death after influenza virus infection. May regulate the calcium channel activity of TRPCs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11880649, ECO:0000269|PubMed:21859714, ECO:0000269|PubMed:21992152, ECO:0000269|PubMed:9060610}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15355513, ECO:0000269|PubMed:16413306, ECO:0000269|PubMed:21992152}; Peripheral membrane protein {ECO:0000269|PubMed:16413306}; Cytoplasmic side. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15047845}. Note=Binds preferentially to negatively charged phospholipids (PubMed:21900240). Colocalizes with CCHFV protein N in the perinuclear region (PubMed:15047845). {ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:21900240}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:20603636}. Nucleus {ECO:0000269|PubMed:20603636}. Note=Translocates into the nuclei of HSV-1 infected cells (PubMed:20603636). {ECO:0000269|PubMed:20603636}.
Interaction partners:
- Ubiquitin-like protein ISG15
- Antiviral innate immune response effector IFIT1
- 2'-5'-oligoadenylate synthase 1
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon regulatory factor 9
- Interferon-induced GTP-binding protein Mx2
- Interferon-induced, double-stranded RNA-activated protein kinase
- 2'-5'-oligoadenylate synthase 2
- Interferon-induced protein with tetratricopeptide repeats 3
- Antiviral innate immune response receptor RIG-I
Sequence:
MVVSEVDIAKADPAAASHPLLLNGDATVAQKNPGSVAENNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEIEISDASEVEKEINKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIKKYIQRQETISLVVVPSNVDIATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFENHPYFRDLLEEGKATVPCLAEKLTSELITHICKSLPLLENQIKETHQRITEELQKYGVDIPEDENEKMFFLIDKVNAFNQDITALMQGEETVGEEDIRLFTRLRHEFHKWSTIIENNFQEGHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLHTVTDMVRLAFTDVSIKNFEEFFNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQIVYCQDQVYRGALQKVREKELEEEKKKKSWDFGAFQSSSATDSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARLTQARRRLAQFPG
Protein: Target of rapamycin complex 2 subunit bit61 (TORC2 subunit bit61) (O74547)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of TORC2, which regulates multiple cellular processes to control cell growth in response to environmental signals. TORC2 is required for cell survival under various stress conditions. TORC2 positively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Positively regulates amino acid uptake through the control of expression of amino acid permeases.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Serine/threonine-protein kinase tor2
- Target of rapamycin complex 2 subunit sin1
- Serine/threonine-protein kinase tor1
- Target of rapamycin complex 1 subunit tco89
- Target of rapamycin complex subunit wat1
- Target of rapamycin complex 1 subunit toc1
- Target of rapamycin complex 1 subunit mip1
- Target of rapamycin complex 2 subunit ste20
- Serine/threonine-protein kinase gad8
- Cytoskeletal signaling protein slm1
Sequence:
MVGRGSFSSTSSASSINWIPKNTKTSIESVSNTISLSENGQNQDLETVTTKESNVGDSDTTENIKSPFNGQWPFSRRSSQSSSHPVFEETHWSKHSKRPGKLNVLTPTSPSNVNAEVQSISTKTQLSLLNLSPHKHKKPKDGLDLSALQKTLNGSRNFLRGRRDAGGIFGASIPQSLVTNQIINGFGAASLAFAKLGKVRSPLEGRFNLVPISADETWLIVESEVCSLYSGEALHYSLEDLNGILILHLQALIRDTKMNEFVGHLETLFRKATKCLSDSLSPVPEELFLNRIIETWLFFFSSVLPYVQGVFLPIKTKLFDEQEKTQLPYEVNEFCSTNREKLNVHRLALMTFRDYMVLPIANRIQICIGRAESAENALDNAGEVFARLFQILSLLASVRTNDSKEQEITNLATKVRCLLIAS
Protein: Protein yippee-like (O01314)
Organism: Caenorhabditis elegans
Interaction partners:
- V-type proton ATPase subunit
- GILT-like protein F37H8.5
Sequence:
MELIDKFITLHDQLRKDLNLASLCISKAKTTHGIGLFSVNSVDTHDLEPSIRLDTKNGKFVLLKNSENEEEKNDKKNKKKKDENKSEKKNSGESEDVEEAKKTFSGQFRPFGVLEPAAAKDARKIYRNSIQTILDLVSTQQSILAKSRQLVEDC
Protein: DnaJ homolog subfamily B member 1 (Heat shock 40 kDa protein 1) (HSP40) (Heat shock protein 40) (Q9QYJ3)
Organism: Mus musculus (Mouse)
Function: Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P25685}. Nucleus {ECO:0000250|UniProtKB:P25685}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P25685}. Note=Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock. {ECO:0000250|UniProtKB:P25685}.
Interaction partners:
- Heat shock protein HSP 90-beta
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 1B
- Heat shock protein HSP 90-alpha
- Heat shock 70 kDa protein 4
- Heat shock protein 105 kDa
- Heat shock 70 kDa protein 1A
- Stress-induced-phosphoprotein 1
- BAG family molecular chaperone regulator 1
- Hsc70-interacting protein
Sequence:
MGKDYYQTLGLARGASDDEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGGSPSGGSSGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDTFSSFPMGMGGFTNMNFGRSRPSQEPTRKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKRGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLVIEFEVIFPERIPVSSRTILEQVLPI