wanglab/gogpt-training-data huggingface dataset:
Protein: Stardust protein MAGUK1 isoform (Q8WRS3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLSVNQDNGPHREMAVDCPDTFIARNKTPPRYPPPRPPQKHKKSTNTTTTTTITALTNNDHANKMLIVAYHSSHQHEQLQQQHPSKTSTTTTTIALDVATQNLYNQKQQNKLEQIENYENCLQSERNEQHEQQFEQQKQHQATTAMAATQVAQQQTPSHKLQATLSSDPNGNSNSNNNSHIVGISSSSSSNNSSITDDFLCVVDGLYQGRKDTASPSSSAFDEVMSKHTLDSFGSIAYRHLHQQHQATSNGNSSSNTSNTNSNTNSNTNSNSNTNGNTSNNTAVSTKTATVTKTGVSSSNSNSNSLNSSNSSMHTSSSSSGHSSNIASATSSSSATSSSTVPDDLSLAPPGYEVSQQQQQQHLVATPVTMLLPPMAKHRELPVDVPDSFIEMVKTTPRYPPPAHLSSRGSLLSNGSASTAHTTLSSMGVAPSPVTATAAAAASASAACATTAVAAAAVSGVADGDARRVADELNGNAKPVPPPRDHLRVEKDGRLVNCSPAPQLPDRRAPGNASSGSSGATTHPLQHQQIAQIVEPTLEQLDSIKKYQEQLRRRREEEERIAQQNEFLRNSLRGSRKLKALQDTATPGKAVAQQQQQATLATQVVGVENEAYLPDEDQPQAEQIDGYGELIAALTRLQNQLSKSGLSTLAGRVSAAHSVLASASVAHVLAARTAVLQRRRSRVSGPLHHSSLGLQKDIVELLTQSNTAAAIELGNLLTSHEMEGLLLAHDRIANHTDGTPSPTPTPTPAIGAATGSTLSSPVAGPKRNLGMVVPPPVVPPPLAQRGAMPLPRGESPPPVPMPPLATMPMSMPVNLPMSACFGTLNDQNDNIRIIQIEKSTEPLGATVRNEGEAVVIGRIVRGGAAEKSGLLHEGDEILEVNGQELRGKTVNEVCALLGAMQGTLTFLIVPAGSPPSVGVMGGTTGSQLAGLGGAHRDTAVLHVRAHFDYDPEDDLYIPCRELGISFQKGDVLHVISREDPNWWQAYREGEEDQTLAGLIPSQSFQHQRETMKLAIAEEAGLARSRGKDGSGSKGATLLCARKGRKKKKKASSEAGYPLYATTAPDETDPEEILTYEEVALYYPRATHKRPIVLIGPPNIGRHELRQRLMADSERFSAAVPHTSRARREGEVPGVDYHFITRQAFEADILARRFVEHGEYEKAYYGTSLEAIRTVVASGKICVLNLHPQSLKLLRASDLKPYVVLVAPPSLDKLRQKKLRNGEPFKEEELKDIIATARDMEARWGHLFDMIIINNDTERAYHQLLAEINSLEREPQWVPAQWVHNNRDES
Protein: Nucleoporin Nup54 alpha-helical domain-containing protein (Q9U3C1)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSLFGSSTPQKQAFTFPTPNAPTTSSGTLFGSTTPSKPLFGSTAQASSTPSLFGTTNTSTPSGGLFGKTGTSTTTTSTAGTLFGAAPTTSTATPSLFGASTTGSTPFGAASTGTAAGSTLFGSSTAKPATGGFFGSSSGSTLGGLGATQQQQQPVVQQQQVIQQYHPFVKAVGDPKLFGNDNDGVVAKLNQVAAGLGVGKAPYKDGNQLLSFSMEGNLFERFVGIGYNRISERTDDEGFVTLVLRHPITNLNTEERRDKILEIIKAILGGGPNVEVRYAPGTSMRTLSDGCTEICIIAKEGGFVAGAIKLAQILNDAPKMTQLESQLQVDKTRVLPKVGMSKAQRDRYLETVPDGIDERIWRQAIKENPAPNKLLPVPVRGWEALRDRQKAQVGESKLFHEAINALGNRVEEANHEHADAVVKMEIIRNRHKTLSYRIVRVMLAQWIVSRYSRQIDTDEDVIEAKADTLLAQMNRHNQVKFYVDKFYEILESKPDKLQESMWKMFDMTIEDEHYARRVLTKFVNICSGLYESTHQQIESLEACRRALEG
Protein: Puff-specific protein Bx42 (P39736)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play a role in chromatin structure and function.
Subcellular location: Nucleus.
Interaction partners:
- Protein crooked neck
- Pleiotropic regulator 1
- Cell division cycle 5, isoform A
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor syf1 homolog
- Protein BUD31 homolog
- Pre-mRNA-splicing factor RBM22
- RE31520p
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-splicing factor Syf2
Sequence:
MSLSSLLPTPTNAIWDREDERRLVARGAPKIGALVSAKIAAPPYGQRKDWVPHTDADFGDGGAFPEIHVAQYPLGLGAPGNVGKKSDALAVRLDDKGKVKYDAIARQGHGKDKIVYSSISQLLPAEVLAEDADELQRPDEETVMETTEETRLALEKLTNQKITSALPVRHAQKAGPAQYIRYTPSQQGDTFNSGAKQRVIRMVEAQLDPMEPPKFRINKKIPRGPPSPPAPVLHSPSRKVTVKEQKEWKIPPCISNWKNAKGYTIPLDKRLAADGRGLQQVHINEKFAKMAEALYIADRKAREAVEARSQLEKKLAQKEKEKKEDMLRMMAQRAREERAGLRNPEAAEPSGSGATGSEVRERNDLRAERQRERQRDRNLQRAAPEKRSKLQKERERDISEQIALGLPAKSAGNGETLFDQRLFNTTKGMDSGYGDDEAYNVYDKPWRDSNTLGAHIYRPSKQADSDNYGGDLDAIVNTKRFVPDKQFSGASKEAAAGQRSGPVEFEKEEDPFGLDQFLNMAKKAPKRAEEKNNERSSHSDRKRSKRD
Protein: Doublecortin domain-containing protein 2 (D3ZR10)
Organism: Rattus norvegicus (Rat)
Function: Protein that plays a role in the inhibition of canonical Wnt signaling pathway (By similarity). May be involved in neuronal migration during development of the cerebral neocortex. Involved in the control of ciliogenesis and ciliary length (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q9UHG0}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UHG0}. Cell projection, kinocilium {ECO:0000269|PubMed:25601850}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25601850}. Note=Localizes to the ciliary axoneme and to mitotic spindle fibers in a cell-cycle-dependent manner. {ECO:0000250|UniProtKB:Q9UHG0}.
Interaction partners:
- Dynein axonemal assembly factor 4
- Dyslexia-associated protein KIAA0319 homolog
- Acyl-coenzyme A thioesterase 13
- Tyrosyl-DNA phosphodiesterase 2
Sequence:
MNGPSPRSSHLSQPVVKSVLVYRNGDPFFAGRRVVIHEKKVSSFDIFLKEVTGGVQAPFGAVRNIYTPRTGHRIRKLDQIESGGNYVAGGQEAFKKLNYLDIGEIKKRPMEAVNTEVKPVIHSKINVSARFRKALHEPCTIFLIANGDLISPASRLLIPRKALNQWDHVLQMVTEKITLRSGAVHRLYTLEGKLVESGAELENGQFYVAVGRDKFKRLPYSELLFDKSAMRRPYGQKASSLPPMVGSRKSKGSGNYRQSKSTIGSSDNSSPQPLKRKGKKDSNSEKPTKVKQSVKSKNSHQAIPDNDEGIFKAGAERSETRGAAEVQEDEDTQVEVPVDQRPAEIVDEEEDGEKTSKDANQKDDFSAMNGEAEDRAGSKVADAPEEEEGIPDQGEKKASPSRVNGGTDEENGEELDQVTEELQPTVDEKGKAEGDNSAQDEAGLDAQRPPRPEVTVTSPQENEGNESNKASSAVA
Protein: AfuFlbB beta (E1ABP3)
Organism: Aspergillus fumigatus (Neosartorya fumigata)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASMNGGVMPVDYGHTRGAPSQTSLKTPTSMSTNFFQFFGGQKKVTRDGQPAKRRGPKPDSRPALTRRQELNRQAQRTHRERKEQYIRSLEIEVSRLREAFTQEMSAANLAVVQHREMLQTVNDENAILKELLTAHGIQFEAELERRRAERRSAGRGFQSSPLAGSSVVSQAPAALAASDGNTYTTPPTTVSNVSTDVSPLANGMERVEISPTHEITPPPPIAMTASSCEIPADLDLSAIARNQEPVQAVGGVFEADPQLQIDFILTLESPCREHTDYLCRRSITEADDEDMPFSGHALMATCPPPSYIANTTPEQAYPHKTYDLPHANLTTLLNLSRQLVTEGQITPIMALQCLKNHELYRTLTKDDVKIIIETLNTKVRCYGFGAVVEDFELMDCLSSVLGSKVDTSFSCAGDDTMYS
Protein: Katanin p80 WD40 repeat-containing subunit B1 (Katanin p80 subunit B1) (p80 katanin) (F7FLI5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03022}. Note=Predominantly cytoplasmic. Localized to the interphase centrosome and mitotic spindle poles. Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis. {ECO:0000256|HAMAP-Rule:MF_03022}.
Interaction partners:
Sequence:
CACPKEIVAHASNVSSLVLGKASGRLLATGGDDCRVNLWSINKPNCIMSLTGHTSPVESVRLNTPEELIVAGSQSGSIRVWDLEAAKILRTLMGHKANICSLDFHPYGEFVASGSRDGEGHSQAVRCLRFSPDGKWLASAADDHTVKLWDLTAGKMMSEFPGHTGPVNVVEFHPNEYLLASGSSDRTIRFWDLEKFQVVSCIEGEPGPVRSVLFNPDGCCLYSGCQDSLRVYGWEPERCFDVVLVNWGKVADLAICNDQLIGVAFSQSNVSSYVVDLTRVTRTGTVTQDPVQASQPQTQQTPNPGVSLRRIYERPSTTCSKPQRVKHNSESERRSPSSEDDKDERESRAEIQNAEDYNEIFQPKNSISRTPPRRSEPFPAPPEDDIATAKEASKPSPAMDVQLPVPSQEVPARPSVMTSTPAPKGEPVIIPATRNEPIGLKASDFLPAVKVPQQAELVDEDAMSQIRKGHDTMCVVLTSRHKNLDTVRAVWTTGDIKTSVDSAVAINDLSVVVDLLNIVNQKASLWKLDLCTTVLPQIEKLLQSKYESYVQTGCTSLKLILQRFLPLITDILAAPPSVGVDISREERLHKCRLCFKQLKSISGLVKSRSGLSGRHGSAFRELHLLMASLD
Protein: Serine (Or cysteine) peptidase inhibitor, clade B, member 3C (A2RSF9)
Organism: Mus musculus (Mouse)
Interaction partners:
- Cathepsin G
- Albumin
- Thyroglobulin
- T-cell surface glycoprotein CD4
- Interleukin-4
- Granulocyte-macrophage colony-stimulating factor
- Interferon gamma
- Interleukin-5
- Interleukin-13
- H-2 class II histocompatibility antigen, A beta chain
Sequence:
MILFPEADGKFTVEMYRQLRESDKNIFYSPISMITALGMLKLGAKGNTEIQIEKVLQCNETTEKTTEKSAHCDDEDNVHEQFQKLITQLNKSNDDYDLKAANSIYGAKGFPLLQTFLEDIKEYYHANVESLDFEHAAEESEKKINFWVKNETNGKIKDLFPSGSLSSSTKLVLVNAVYFKGRWNHKFDENNTIEEMFWLNKNTSIPVPMMKQRNKFMFSFLEDVQAQIVEIPYKGKELSMFVLLPMEIDGLKQLEKQLTAAKLLEWTRAENMHLTELYLWLPRFKVEEKYDLPVPLECMGMVNAFDPQKADFSGMSSTQGLVVSKVLHKSFVEVNEEGTEADPASGEEVILRLAQVADFRCDHPFLFFIIHSKTNSILFFGRISSP
Protein: L-ornithine N(5)-monooxygenase (OMO) (EC 1.14.13.196) (Deferriferrichrysin biosynthesis protein A) (L-ornithine N(5)-oxygenase) (Q2TZB2)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as deferriferrichrysin.
Interaction partners:
- Alanine--tRNA ligase
Sequence:
MEPVERKLEIGSRSYSKMPLTQQRSSGEPPRLKATPKDELHDLLCVGFGPASLAIAIALHDALDPCLNKTPNSNWQPKVCFLERQKQFAWHSGMLVPGSKMQISFIKDLATMRDPRSSFTFLNYLHQKDRLIHFTNLSTFLPARMEFEDYMRWCAQRFAHVVSYGEEVIEVIPGKTNPSSTLVDFFTVKSRNVETGEISARMARKVVVALGGTAKLPKELPQDPRIMHSSKYCTTLPAMLKDSREAYNIAVLGSGQSAAEIFHDLQKRYPNSKTTLIMRDTAMRPSDDSPFVNEVFNPERVDKFFSLSSAERQRSLTADKATNYSVVRLELIEQIFNDMYLQRVQNPDETQWQHRILPGRKITRVEHYGPHRRMRLHVRAVKDEKDSLVGNGKETLEVDALMVATGYNRNAHEQLLKNVQHLRPAGQENWTPNREYRVELDPSKVNAQAGIWLQGCNEQTHGLSDSLLSILASRSGEMVNSIFGGEFAGTTVPDTTHIRAML
Protein: Leucine-rich repeat protein kinase family protein (Leucine-rich repeat receptor-like protein kinase) (Putative receptor protein kinase) (T1F15.2 protein) (O64794)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- CRIB domain-containing protein RIC2
- Protein trichome birefringence-like 34
- RING-type E3 ubiquitin transferase
- Protein trichome birefringence-like 3
- Rop guanine nucleotide exchange factor 4
- Rac-like GTP-binding protein ARAC2
- Transcription factor bHLH78
Sequence:
MILLSLLLHLLLHLLNTSPSLSLSPDGIALLSLKSAVDHSSSSAFSDWNDNDTDPCHWSGISCMNISDSSTSRVVGISLAGKHLRGYIPSELGSLIYLRRLNLHNNELYGSIPTQLFNATSLHSIFLYGNNLSGTLPPSICKLPKLQNLDLSMNSLSGTLSPDLNKCKQLQRLILSANNFSGEIPGDIWPELTNLAQLDLSANEFSGEIPKDIGELKSLSGTLNLSFNHLSGQIPNSLGNLPVTVSLDLRNNDFSGEIPQSGSFSNQGPTAFLNNPKLCGFPLQKTCKDTDENSPGTRKSPENNADSRRGLSTGLIVLISVADAASVAFIGLVLVYLYWKKKDSEGGCSCTGNAKLGGGSVKGKSCCCITGFPKEDDSEAEGNERGEGKGDGELVAIDKGFSFELDELLRASAYVLGKSGLGIVYKVVLGNGVPVAVRRLGEGGEQRYKEFVTEVQAMGKVKHPNVVKLRAYYWAPDEKLLISDFVNNGSLADALRGRNGQPSPSLTWSTRIKIAKGAARGLAYLHECSPRKLVHGDVKPSNILLDSSFTPYISDFGLTRLITITAASASSNEPSSSSAAGGFLGGALPYTSIKPSDRSNGYKAPEARLPGGRPTQKWDVYSFGVVLMELLTGKSPDSSPLSSSSTSTVVVEVPDLVKWVRKGFEEETPLSDMVDPMLLQEVHAKQQVLSVFHLALACTEGDPEVRPRMKNVSENIDKI
Protein: LD24920p (Q961B0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTLNESDATRLELTRNFLELSRNPETCTALRSSDCIQLLVQILHANDEGLSTAKKYASQALHNIVHNNPEEKERQREVKMLRLLDQILDYCNFLHTQLQSGGEAIADDEDRHPLAAMKLLMKASFDEEHRQTMCELGALKAIPNLVHLDHAVHGPAAGMEQCNALRSYGLMALTNLTFGDENVHNKSYLCGQRQFMEVVIAQLNTAPDELLQVLAGVLRNLSWRADKHMKTIFNELGTVTSLARAAMQNKNENTLKAILSALWNLSAHCSTNKAEFCAVDGALAFLVGMLSYEGPSKTLKIIENAGGILRNVSSHIAVCEPYRQILRRYNCLAILLQQLKSESLTVVSNSCGTLWNLSARCPEDQQYLIDHNAIPLLRALISSKNSMIAEGSASALKNLVNFRATQELMPNGDGGSLPLDKEAGHGGTLPRRFSSLRLSSNPTGSLKKVRPSTVSTTGFLNRKCESRESIYSGKSDSTKYSTKSEGAKNPFEIVTPTEEQPIDYSMKYMEHKPNSSKTFEIDLDQPTDFSARYKERRSAQTAQPELKSETNEIRSKELQLTKSSSATELRNSPGLVAVSAAKQKIATETETETAERPINYCEEGTPGSFSRFDSLNSLTEKPEKCMPPKTPTKTAVLPVHVDGNTPQNIDSALETPLMFSRRSSMDSLVGDDETVACEDNGSVISEYSRMQSGVISPSELPDSPTQSMPQSPRRDRKVSTQNNLDTPEQKPSTVFEDKLNRFHVEHTPAAFSCATSLSNLSMMDDSNANAIRGQRGNDINGNGDAPRSYCTEDTTAVLSKAPSNSDLSILSIPNDLNANEAQPVPAPRADVTGMDTRMPAEDAISKMRCGGNALPSYLPVSDEMSKYYVEDSPCTFSVISGLSHLTVGSAKAGPVLKLPMRTAEEAQAPKLPPRRSAVQGDAEPRLPPKKSDSLSSLSMDSDDDCNLLSQAIAAGSCRPQPSGASTSSSLANASTSTLCRENGQSKKQVEHGDKPNYSSDDSLDDDDDDARSKSLFEQCILSGMHKSNDALESEGEPPGQRQEISARDRFVSNQVRQIESMLAGRQH
Protein: L-threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) (L-threo-3-hydroxyaspartate dehydratase) (P36007)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the deamination of L-threo-3-hydroxyaspartate to oxaloacetate and ammonia. Shows a high specificity towards L-threo-3-hydroxyaspartate as other 3-hydroxyaminoacids, i.e. D,L-erythro- and D-threo-3-hydroxyaspartate, D-threonine, L-threonine, D,L-allothreonine, D-serine, and L-serine, are not substrates for this enzyme. Exhibits no detectable serine racemase activity. Is responsible for the 3-hydroxyaspartate resistance of S.cerevisiae, and thus may be involved in the detoxification of naturally occurring 3-hydroxyaspartate.
Interaction partners:
- Protein COS9
- Acetolactate synthase small subunit, mitochondrial
- Dihydroxy-acid dehydratase, mitochondrial
- Proteasome subunit alpha type-6
- Threonine synthase
- Tryptophan synthase
- Putative UPF0377 protein YKL223W
- Multifunctional tryptophan biosynthesis protein
Sequence:
MIVPTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLISGKEDGPTI
Protein: Endothelial zinc finger protein induced by tumor necrosis factor alpha (Zinc finger protein 71) (Q9NQZ8)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein 69
Sequence:
MKELDPKNDISEDKLSVVGEATGGPTRNGARGPGSEGVWEPGSWPERPRGDAGAEWEPLGIPQGNKLLGGSVPACHELKAFANQGCVLVPPRLDDPTEKGACPPVRRGKNFSSTSDLSKPPMPCEEKKTYDCSECGKAFSRSSSLIKHQRIHTGEKPFECDTCGKHFIERSSLTIHQRVHTGEKPYACGDCGKAFSQRMNLTVHQRTHTGEKPYVCDVCGKAFRKTSSLTQHERIHTGEKPYACGDCGKAFSQNMHLIVHQRTHTGEKPYVCPECGRAFSQNMHLTEHQRTHTGEKPYACKECGKAFNKSSSLTLHQRNHTGEKPYVCGECGKAFSQSSYLIQHQRFHIGVKPFECSECGKAFSKNSSLTQHQRIHTGEKPYECYICKKHFTGRSSLIVHQIVHTGEKPYVCGECGKAFSQSAYLIEHQRIHTGEKPYRCGQCGKSFIKNSSLTVHQRIHTGEKPYRCGECGKTFSRNTNLTRHLRIHT
Protein: Testis secretory sperm-binding protein Li 206a (A0A024R542)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKVSTLRESSAMASPLPREMEEELVPTGSEPGDTRAKPPVKPKPRALPAKPALPAKPSLLVPVGPRPPRGPLAELPSARKMNMLAGPQPYGGSKRPLPFAPRPAVEASTGGEATQETGKEEAGKEEPPPLTPPARCAAPGGVRKAPAPFRPASERFAATTVEEILAKMEQPRKEVLASPDRLWGSRLTFNHDGSSRYGPRTYGTTTAPRDEDGSTLFRGWSQEGPVKSPAECREEHSKTPEERSLPSDLAFNGDLAKAASSELPADISKPWIPSSPAPSSENGGPASPGLPAEASGSGPGSPHLHPPDKSSPCHSQLLEAQTPEASQASPCPAVTPSAPSAALPDEGSRHTPSPGLPAEGAPEAPRPSSPPPEVLEPHSLDQPPATSPRPLIEVGELLDLTRTFPSGGEEEAKGDAHLRPTSLVQRRFSEGVLQSPSQDQEKLGGSLAALPQGQGSQLALDRPFGAESNWSLSQSFEWTFPTRPSGLGVWRLDSPPPSPITEASEAAEAAEAGNLAVSSREEGVSQQGQGAGSAPSGSGSSWVQGDDPSMSLTQKGDGESQPQFPAVPLEPLPTTEGTPGLPLQQAEERYESQEPLAGQESPLPLATREAALPILEPVLGQEQPAAPDQPCVLFADAPEPGQALPVEEEAVTLARAETTQARTEAQDLCRASPEPPGPESSSRWLDDLLASPPPSGGGARRGAGAELKDTQSPSTCSEGLLGWSQKDLQSEFGITGDPQPSSFSPSSWCQGASQDYGLGGASPRGDPGLGERDWTSKYGQGAGEGSTREWASRCGIGQEEMEASSSQDQSKVSAPGVLTAQDRVVGKPAQLGTQRSQEADVQDWEFRKRDSQGTYSSRDAELQDQEFGKRDSLGTYSSRDVSLGDWEFGKRDSLGAYASQDANEQGQDLGKRDHHGRYSSQDADEQDWEFQKRDVSLGTYGSRAAEPQEQEFGKSAWIRDYSSGGSSRTLDAQDRSFGTRPLSSGFSPEEAQQQDEEFEKKIPSVEDSLGEGSRDAGRPGERGSGGLFSPSTAHVPDGALGQRDQSSWQNSDASQEVGGHQERQQAGAQGPGSADLEDGEMGKRGWVGEFSLSVGPQREAAFSPGQQDWSRDFCIEASERSYQFGIIGNDRVSGAGFSPSSKMEGGHFVPPGKTTAGSVDWTDQLGLRNLEVSSCVGSGGSSEARESAVGQMGWSGGLSLRDMNLTGCLESGGSEEPGGIGVGEKDWTSDVNVKSKDLAEVGEGGGHSQARESGVGQTDWSGVEAGEFLKSRERGVGQADWTPDLGLRNMAPGAVCSPGESKELGVGQMDWGNNLGLRDLEVTCDPDSGGSQGLRGCGVGQMDWTQDLAPQNVELFGAPSEAREHGVGGVSQCPEPGLRHNGSLSPGLEARDPLEARELGVGETSGPETQGEDYSSSSLEPHPADPGMETGEALSFGASPGRCPARPPPSGSQGLLEEMLAASSSKAVARRESAASGLGGLLEEEGAGAGAAQEEVLEPGRDSPPSWRPQPDGEASQTEDVDGTWGSSAARWSDQGPAQTSRRPSQGPPARSPSQDFSFIEDTEILDSAMYRSRANLGRKRGHRAPVIRPGGTLGLSEAADSDAHLFQDSTEPRASRVPSSDEEVVEEPQSRRTRMSLGTKGLKVNLFPGLSPSALKAKLRPRNRSAEEGELAESKSSQKESAVQRSKSCKVPGLGKPLTLPPKPEKSSGSEGSSPNWLQALKLKKKKV
Protein: Uncharacterized protein (Q388Z6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLPELDSAAESLLRDPQYLLKLHHRVAQCLRNCNPSTFVRSMSTAFTAIDSKYRARDREQSTELWLLKGILRQIFPVKSFSDRELAILLAALPLSEYSGAAASEEGCIRVSPVTLLRCLRQMCPMRSSMLYETLRGMDAKSPRPHASEFPCGRELAAHTQVGKEDMCVLDSAMLVDHLTQTHGLTLSEAFFLIDYCSTNTAPSATKVAIEAPYLYALLYLRPLPAELHYQLILSVFAEAVGDPNREGHSGTLALITELRQVPLEPLDTSGGTELSRACADIDQDLVRCGLSASSFEKLCSGIRVGLTKDDIRELFSYLRGREGGFHEVLSVKTLMQEFVCHFAPVGESLFAIVVEAVRRYVVKEGGMLALPRLYLNLPDGELPIETFVASFRKAGVPDTVSDVEVEWLRFKARNKTQLIALLGGKCSAKREALIKQLFGRMAGGCDASGGVVNVTTEHLLASFHPGNAEGGLVSGEEWRHVMSSCLGEKFAYDRFFYFWNSISAACSDDSVFTMILWRCFNMHTKP
Protein: Zinc finger protein 696 (Q9H7X3)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MEPGGEPTGAKESSTLMESLAAVKAAFLAQAPSGSRSAEVQAAQSTEPAAEAGAPEGEGHRGGPPRALGSLGLCENQEARERPGGSPRGPVTSEKTGGQSGLESDVPPNAGPGAEGGGSWKGRPFPCGACGRSFKCSSDAAKHRSIHSGEKPYECSDCGKAFIHSSHVVRHQRAHSGERPYACAECGKAFGQSFNLLRHQRVHTGEKPYACADCGKAFGQRSDAAKHRRTHTGERLYACGECGKRFLHSSNVVRHRRTHHGENPYECRECGQAFSQSSNLLQHQRVHTGERPFACQDCGRAFSRSSFLREHRRIHTGEKPHQCGHCGRAFRALSGFFRHQRLHTGEKPFRCTECGRAFRLSFHLIQHRRVHGAE
Protein: ATP-dependent RNA helicase dbp8 (EC 3.6.4.13) (Q9HGM5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-binding RNA helicase involved in 40S ribosomal subunit biogenesis and is required for the normal formation of 18S rRNAs through pre-rRNA processing at A0, A1 and A2 sites. Required for vegetative growth (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Uncharacterized protein C3B8.09
- Pre-rRNA-processing protein esf2
- Probable ATP-dependent RNA helicase prh1
- Ribosomal RNA-processing protein 15
- U3 small nucleolar RNA-associated protein 22
- 60S ribosomal export protein nmd3
- U3 small nucleolar RNA-associated protein 25
- Putative ATP-dependent RNA helicase PB1A10.06c
- rRNA biogenesis protein rrp5
- Ribosomal RNA small subunit methyltransferase mra1
Sequence:
MSEHTRKSFSDLGISPWLIDTLKALAIYEPTDIQEGVIAQILEGRNCIGGAKTGSGKTAAFALPIIEKWSKDPSGIFALILTPTRELAIQIDEQFAALGANLNLKHALIVGGMDMIRQSIDLSKRPHVVVATPGRLADLIRSNGEETIAGLRRIKFLVMDEADRLLSPTFADDLDDCFSVLPASEDRQTLLFTATVTDAIRQLKYQPQKNNKPPLWLYEVETDNISVPSTLQQSYIFVSSQVREAYLVHLLTIPENAKKSAIIFVNRTRTAELIYSILRLLELRVTELHSEMVQRERINSLGRFRAEAAKILVATDVASRGLDIPSVQLVINFDLPRDPDDYIHRVGRTARAGRSGESISIVTERDVDLVHAIEDRVGTKLSEYEHVSENKMLEYIKEVTDAKRQASLEMIDRGFGERRQKRNEKRLMANGISNKLKNSGRKKKAKNTLSTEK
Protein: Probable glycosidase CRH2 (EC 3.2.-.-) (Congo red hypersensitive protein 2) (Unknown transcript 2 protein) (P32623)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable glycosidase that plays a role in cell wall architecture. Required for the transfer of chitin to 1,6-beta-glucan in the cell wall.
Subcellular location: Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP), localized particularly in chitin-rich areas. Localizes to sites of polarized growth. Found at the incipient bud site, as a ring at the bud neck as the bud grows, and in the septum at the time of cytokinesis. Redistributes uniformly over the cell cortex upon heat stress.
Interaction partners:
- Congo red hypersensitive protein 1
- 1,3-beta-glucanosyltransferase GAS1
Sequence:
MAIVNSWLICLVSIFSFVVRVEAATFCNATQACPEDKPCCSQYGECGTGQYCLNNCDVRYSFSHDSCMPVPICKSSSTKFKDYSSKLGNANTFLGNVSEADWLYTGDVLDYDDEESLILAMPKNSGGTVLSSTRAVWYGKVSARIKTSHLAGVVTGFILYSGAGDELDYEFVGADLETAQTNFYWESVLNYTNSANISTTDTFENYHTYELDWHEDYVTWSIDGVVGRTLYKNETYNATTQKYQYPQTPSKVDISIWPGGNSTNAPGTIAWSGGEINWDASDISNPGYYYAIVNEVNITCYDPPSDTKKNGTSAYVYTSSSEFLAKDIAITDDEVMMDSDEGSGLDPHKGATTSSTQKSSSSTATSSSKTSSDHSSSTKKSSKTSSTASSSSSSSSSSSSSSSTATKNGDKVVSSVSSSVTSQTQTTSSVSGSASSSTSSMSGNNAGANVAANWRLTVLCVILGYVL
Protein: Ribosomal protein S6 kinase (EC 2.7.11.1) (P91656)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADVSDPSELFDLELHDLELQDDKARDSDDDRIELDDVDLEPELCINLHQDTEGQETIQLCEENVNPGKIKLGPKDFELKKVLGKGGYGKVFQVRKTAGRDANKYFAMKVLKKASIVTNQKDTAHTRAERNILEAVKHPFIVELVYAFQTDGKLYLILEYLSGGELFMHLEREGIFLEDTTCFYLSEIIFALGHLHKLGIIYRDLKPENILLDAQGHVKLTDFGLCKEHIQEGIVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMFDMLTGVPPFTAENRKKTIETILKAKLNLPAYLTPEARDLVRRLMKRQEPQRLGSGPEDAAAVQIHPFFKHVNWDDVLARRLEPPIKPLLRSEDDVSQFDTRFTRQIPVDSPDDTTLSESANLIFQGFTYVAPSILEDMHRANRMPARSPRRTPRQLPDSSFRLQFPSANVGANAPAGHARSFAAIRDVCTSHAAASHADICAASIAGAGRDDGRAGSADGLKAGAIASQPTNPSHPVRSVATQQLHHKLPLPTPKKKKKKKKQQKITEIDSYYYDVCGVWTWLRIRNEQDDHQEVAEEEEEEEEEAEQHEEHMTSVREIVFVKEKRARIALFDVYDYENDYEYDYDYEADGEDDCATRRKAFVFGYT
Protein: Ubiquitin recognition factor in ER-associated degradation protein 1 (Ubiquitin fusion degradation protein 1 homolog) (UB fusion protein 1) (P70362)
Organism: Mus musculus (Mouse)
Function: Essential component of the ubiquitin-dependent proteolytic pathway which degrades ubiquitin fusion proteins. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. It may be involved in the development of some ectoderm-derived structures (By similarity). Acts as a negative regulator of type I interferon production via the complex formed with VCP and NPLOC4, which binds to RIGI and recruits RNF125 to promote ubiquitination and degradation of RIGI (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9ES53}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9ES53}.
Interaction partners:
- Nuclear protein localization protein 4 homolog
- UBX domain-containing protein 7
- Transitional endoplasmic reticulum ATPase
- FAS-associated factor 1
- FAS-associated factor 2
- Phospholipase A-2-activating protein
- Derlin-1
- Ubiquitin thioesterase OTU1
- NSFL1 cofactor p47
- Deubiquitinating protein VCPIP1
Sequence:
MFSFNMFDHPIPRVFQNRFSTQYRCFSVSMLAGPNDRSDVEKGGKIIMPPSALDQLSRLNITYPMLFKLTNKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLEEGGLVQVESVNLQVATYSKFQPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPDKAVSIIECDMNVDFDAPLGYKEPERPVQHEESIEGEADHSGYAGEVGFRAFSGSGNRLDGKKKGVEPSPSPIKPGDIKRGIPNYEFKLGKITFIRNSRPLVKKVEEDEAGGRFIAFSGEGQSLRKKGRKP
Protein: Myosin-7 (Myosin heavy chain 7) (Myosin heavy chain slow isoform) (MyHC-slow) (Myosin heavy chain, cardiac muscle beta isoform) (MyHC-beta) (P12883)
Organism: Homo sapiens (Human)
Function: Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle.
Subcellular location: Cytoplasm, myofibril {ECO:0000250|UniProtKB:P02564}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:P02564}. Note=Thick filaments of the myofibrils. {ECO:0000250|UniProtKB:P02564}.
Interaction partners:
- Myosin light chain 3
- Actin, alpha cardiac muscle 1
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin-binding protein C, cardiac-type
- Myosin-6
- Tropomyosin alpha-1 chain
- Myosin regulatory light chain 11
- Troponin I, slow skeletal muscle
- Alpha-actinin-2
Sequence:
MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNEE