wanglab/gogpt-training-data huggingface dataset:
Protein: Golgin subfamily A conserved domain-containing protein (F1RRA0)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
QNHDAENGPVPIDENTSFSSTESLRQLSQQLNGLVSESSPYINGEGLASPANIKKLEKQENQETLDQLEKEKKEFEQKLAKEQGALREQLQVHIQTIGILVSEKTELQTALAHTQQAARQKAGESENLASRLQSSRQRVGELERTLSAVSTQQKQADRYNKELTKERDTLKLELYKNNKSNEDLKQQKSELEEKLRLMATEKAAMQLGMEELQKKLEMSELLLQQFSTQPTPDSSQQLQQALEERAQLETCVGQLQDSLRQLQAERDQYVANLKEDSTVWQHKMQQMNEQLNKLRAEKEHSMSQVQELETSLAELRNQAAPPSGPSETEQRLQAEAEQLQKEVESLARQLQAQVKDNENLSLLNQEQEQRLMELERAAECWGEQAEERKQMLESMQSDRTTISRALTQNRKLKEQLAELQNGFVRLSNENMEITSALHSEQHVKKELAKKLGQLQENLGELKETVEVKSQEAQDLQQQRDQYLGHLQQYVAAYQQLAAEKELLHKQMVLQTQLVDQLQHEDMQGRMAVETARQELQEAQGRLEAANQHNQQLQAQLTLMAVPGEGTELDIEDEDKAGEAPRPKLSVPEELDSREAVVEFFNSALASAEEEQARLRRELKEQKLRCQRLAHLVAPAQDGVEKEAPAPGTEGDSVSAPGTGGDSVPVETHQALQVAMDKLQGRFTELMQEKVDLKERVEELEHRCIQLSGETDTIGEYIALYQSQRAVLKERHREKEEYISRLAQDKEEMKVKLLELQELVLHLVGERNEWQGKFLAAQNPAGEPTVAPPAPQELGAAENQGGLLEVSLSDNVEPTQGEALLGQTLTENPTAQQIMQLLREIQNPQERLGLGSNPCIPFFYRADDNDEVKIMVV
Protein: PTHB1 N-terminal domain-containing protein (Q381Z0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Bardet-Biedl syndrome 8 protein
- FG-GAP repeat protein, putative
- FG-GAP repeat protein, putative
- BBSome complex member BBS5 PH domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Anaphase-promoting complex subunit 5
- Uncharacterized protein
- Uncharacterized protein
- Dynein axonemal assembly factor 4
Sequence:
MGSLFKLRDHWYTRYGGEEFSHTQPLAVGNIDNHASGENKIIIGSFSGLLRIMQPMKKGAALPEDTLLEKDLGEPILQLACRPLELNSKGVAANLLAVLFPKRLALFRVRCGKTRSGEKENSGAFNASCSIHLCYKTSLEGHAYNFTCGAFGGAKHEMVCVQSMDGQLTIVDRNLVLLRFLLPEKEFLLPGCLTYCRNRDCFLTCNSSMKVLCYKFSALTNDQPQTETQGGALKSIKSEEHKETLTPLWAFPLGEDAIAIEVCRFSRGLAENDADIVILCQYALFVLKLNGQMRYSKRLDVAGLCLTSYDVPAAGASNVLVGTATGSVLVFSDTSLEWSAKMTEGVPLCMEVTQLMEMQGLVVSLNTEGTVAVNYLGTDPEEEPIQPLQSKEVDYAEAVDELRRVQQAIKRITNAEDGTSKTREAEKVLEVTWDVIGDEENSPAEVVVLLVIRNCSKDMTAFRVTALLQVVIPIEVDAHKHTIESITPGGSARITVRFSTPSSLNYVIPSSLDARVVILYTCGRTTGCSVGTTIHLPFTLVAQPIPYVDASNFVLQFDTNKSEPPSLIDVFTDFAQSEHISSNLLAIQYVNGAHAVLFVSRNAGRFRLQASTMEALWLFTFELHARLLTFYDSEVQFTFPNPIPLDDYFRVIDEHVETRKQLNTAKNTLARASQMFFAVQKRLLALFRTNSSTSVALTSTLLGACYGNLQRCTDTVCRLILQRKKAAASLCCCSRLVVMDLLIKCQKTLTDPEDIHLIESIFTCSIDADDELDWEESTDAALGRLVVGNKGSCDFIPADLSANDGMFVEPNVERLRKRITEFFDKLLSGALTSFLK
Protein: TGF-b1-induced anti-apoptotic factor 1 (A0A1I9GFB9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSSPSSPFREQSFLCAAGDAGEESRVQVLKNEVRRGSPVLLGWVEQAYADKCVCGPSAPPAPTPPSLSQRVMCNDLFKVNPFQLQQFRADPSTASLLLCPGGLDHKLNLRGKAWG
Protein: Ubiquitin carboxyl-terminal hydrolase 5 (EC 3.4.19.12) (Deubiquitinating enzyme 5) (Isopeptidase T) (Ubiquitin thioesterase 5) (Ubiquitin-specific-processing protease 5) (P56399)
Organism: Mus musculus (Mouse)
Function: Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity (By similarity).
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-C
- Polyubiquitin-B
- Ubiquitin carboxyl-terminal hydrolase 7
- Ubiquitin carboxyl-terminal hydrolase 14
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin carboxyl-terminal hydrolase 25
- Ubiquitin carboxyl-terminal hydrolase isozyme L5
- E3 ubiquitin-protein ligase CHIP
- Voltage-dependent T-type calcium channel subunit alpha-1H
Sequence:
MAELSEEALLSVLPTIRVPKAGDRVHKDECAFSFDTPESEGGLYICMNTFLGFGKQYVERHFNKTGQRVYLHLRRTRRPKEEDTSAGTGDPPRKKPTRLAIGVEGGFDLTEDKFEFDEDVKIVILPDYLEIARDGLGGLPDIVRDRVTSAVEALLSADSASRKQEVQAWDGEVRQVSKHAFNLKQLDNPARIPPCGWKCSKCDMRENLWLNLTDGSILCGRRYFDGSGGNNHAVEHYRETGYPLAVKLGTITPDGADVYSYDEDDMVLDPSLAEHLSHFGIDMLKMQKTDKTMTELEIDMNQRIGEWELIQESGVPLKPLFGPGYTGIRNLGNSCYLNSVVQVLFSIPDFQRKYVDKLEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPALESGDGEQVPEQKEVQDGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNCRSSENPNEVFRFLVEEKIKCLATEKVKYTQRVDYIMQLPVPMDAALNKEELLEYEEKKRQAEEEKVPLPELVRAQVPFSSCLEAYGAPEQVDDFWSTALQAKSVAVKTTRFASFPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELDISQLRGTGLQPGEEELPDIAPPLVTPDEPKGSLGFYGNEDEDSFCSPHFSSPTSPMLDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFANPLILPGSSGPGSTSAAADPPPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHIDDLDAEAAMDISEGRSAAESISESVPVGPKVRDGPGKYQLFAFISHMGTSTMCGHYVCHIKKEGRWVIYNDQKVCASEKPPKDLGYIYFYQRVVS
Protein: Alpha-lactalbumin (Lactose synthase B protein) (Lysozyme-like protein 7) (P00709)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
Subcellular location: Secreted.
Interaction partners:
- Lactotransferrin
- Beta-1,4-galactosyltransferase 1
- Albumin
- Kappa-casein
- Alpha-S1-casein
- Beta-casein
- Lactoperoxidase
- UDP-glucose 4-epimerase
- Beta-1,4-galactosyltransferase 2
- Myoglobin
Sequence:
MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL
Protein: PH-sensitive chloride channel 1, isoform K (M9PFD4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGCVFEAAKEQPHKPRSRQLRRNQCRGKAEKAAAGTRGKVAVRGNNDKPAEDIKIKDNYQQNHKTQTETQTEVAAVVAIATDAGAETETETEAEAQKEPATGPEHLKAAAQVLLTIRQARQENNKHSSSQVAETHKDEGEDALARQGSIVDTAAGRIGIDIAATTIQVAERHEDGQHWQQHNVRRRRRQPDPAAHPASITKLSAISLHFHALAALAKTLQKHEDLSPVQDRQPLAYRAWQEHPYAETQMPATMSAAIIANVGATAAATSAAAFQYLGQHYKHYSQSISFYAASSVLLMLCYLTTASTAAATQSETGALDKHPIFDESSSDKEILDLLLEKKRYDKRLLPPVNGTLTVNVNVLLLSLASPDESSLKYEVEFLLNQQWNDPRLQYGNKSHYDFLNALHHHDSIWTPDTYFIMHGDFKDPIIPMHFALRIFRNGTITYAMRRHLILSCQGSLHIFPFDDPKCSFSMESISYEEAQIKYVWKNDEDTLRKSPSLTTLNAYLIKNQTTACDQNSWRGNYSCLRVDLIFTRDRAFYFTTVFIPGIILVTSSFITFWLEWNAVPARSMIGVTTMLNFFTTSNGFRSTLPVVSNLTAMNVWDGVCMCFIYASLLEFVCVNYVGRKRPLHNVVYRPGENPVTQRLPAVLSRIGVILASPLGEKRQNAGAPNEIVACTTCGGSNSPCTHSANNGCATETCFVQVRKKEPPHPIRVAKTIDVIARITFPTAYAIFLIFFFVHYKGFS
Protein: Cytochrome c2 (Q2RVM4)
Organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
Function: Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
Interaction partners:
- Cytochrome c1
- Ubiquinol-cytochrome c reductase iron-sulfur subunit
- Ubiquinol-cytochrome c reductase iron-sulfur subunit
- Cytochrome b
- Cbb3-type cytochrome c oxidase subunit
- 4Fe-4S ferredoxin, iron-sulfur binding
- Protein-methionine-sulfoxide reductase catalytic subunit MsrP
- Molybdopterin oxidoreductase
- Dimethyl sulfoxide/trimethylamine N-oxide reductase
- Cytochrome c domain-containing protein
Sequence:
MKKGFLAAGVFAAVAFASGAALAEGDAAAGEKVSKKCLACHTFDQGGANKVGPNLFGVFENTAAHKDDYAYSESYTEMKAKGLTWTEANLAAYVKDPKAFVLEKSGDPKAKSKMTFKLTKDDEIENVIAYLKTLK
Protein: Polyubiquitin-A [Cleaved into: Ubiquitin; Ubiquitin-related] (P0CG71)
Organism: Caenorhabditis elegans
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-conjugating enzyme E2 2
- Ubiquitin-conjugating enzyme E2 13
- E3 ubiquitin-protein ligase parkin
- E1 ubiquitin-activating enzyme
- Ubiquitin carboxyl-terminal hydrolase
- Serine/threonine-protein kinase pink-1, mitochondrial
- Ubiquitin thioesterase otubain-like
- Ubiquitin carboxyl-terminal hydrolase 14
- Ubiquitin-conjugating enzyme E2 variant 1
Sequence:
MQIFVKTLTGKTITLEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLIGKTITLEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEASDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGDI
Protein: Dynamin-3 (EC 3.6.5.5) (Dynamin, testicular) (T-dynamin) (Q9UQ16)
Organism: Homo sapiens (Human)
Function: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305}. Note=Microtubule-associated. {ECO:0000305}.
Interaction partners:
- Dynamin-1
- Dynamin-2
- Hematopoietic lineage cell-specific protein
- Endophilin-A1
- Homer protein homolog 1
- Clathrin heavy chain 1
- Sorting nexin-9
- Amphiphysin
- Growth factor receptor-bound protein 2
Sequence:
MGNREMEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLHCKGKKFTDFDEVRLEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLPNFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSGDQVDTLELSGGAKINRIFHERFPFEIVKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCEETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQRSSQVHKKTTVGNQGTNLPPSRQIVIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKDYRFLELACDSQEDVDSWKASLLRAGVYPDKSVAENDENGQAENFSMDPQLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRPTRAPPSVPSRRPPPSPTRPTIIRPLESSLLD
Protein: Transmembrane protein 9 (B1ALM8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MKLLSLVAVVGCLLVPPAEANKSSEDIRCKCICPPYRNISGHIYNQNVSQKDCPVSLCCSNCLHVVEPMPVPGHDVEAYCLLCECRYEERSTTTIKVIIVIYLSVVGALLLYMAFLMLVDPLIRKPDAYTEQLHNEEENEDARSMAAAAAS
Protein: Purine-rich binding protein-alpha, isoform D (Q8IMC4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMASQDQGSSSRNDFDSSAKGGSGVEQELATKMLQIQSKRFYLDVKQNRRGRFIKVAEIGADGRRSQIYLALSTAAEFRDHLSSFSDYYASLGPPNTDNLPEDGKLKSEMMIKDYRRYYLDLKENARGRFLRVSQTITRGGPRSQIALPAQGMIEFRDALTDLLEEFGANDGGRFKGDLPEERHMKVDNKNFYFDIGQNNRGVYMRISEVKNNFRTSITIPEKCWIRFRDIFNDYCEKMKKSSDSITAEINLPTSSNSLK
Protein: creatine kinase (EC 2.7.3.2) (Q804Z1)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Interaction partners:
- Guanidinoacetate N-methyltransferase
Sequence:
MTKNCNNDYKMKFPMEEEYPDLSLHNNHMSKVLTKDIYNKLRGKSTPSGFTLDDCIQTGVDNPGHPFIMTVGCVAGDEESYEVFKDLFDPIISDRHSGYKPTDKHHTDLNWENLKGGDDLDPNYVVSSRVRTGRSIKGFTLPPTNSRGERRAVEKLSIEALTSLDGEFKGKYYPLKDMTDKEQEQLIADHFLFDKPVSPLLLAAGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISMQKGGNMKEVFKRFCVGLQKIEEIFKKHNHGFMWNEHLGFVLTCPSNLGTGLRGGVHVKLPKLSTHPKFEEILTRLRLQKRGTGGVDTASVGGVFDISNADRLGSSEVQQVQLVVDGVKLMVEMEKKLEKGESIDDMIPAQK
Protein: Tensin 1 (E9PF55)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}.
Interaction partners:
Sequence:
MSVSRTMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPVYTSGIYNIPGDSQTSVCITIEPGLLLKGDILLKCYHKKFRSPARDVIFRVQFHTCAIHDLGVVFGKEDLDDAFKDDRFPEYGKVEFVFSYGPEKIQGMEHLENGPSVSVDYNTSDPLIRWDSYDNFSGHRDDGMEEVVGHTQGPLDGSLYAKVKKKDSLHGSTGAVNATRPTLSATPNHVEHTLSVSSDSGNSTASTKTDKTDEPVPGASSATAALSPQEKRELDRLLSGFGLEREKQGAMYHTQHLRSRPAGGSAVPSSGRHVVPAQVHVNGGALASERETDILDDELPNQDGHSAGSMGTLSSLDGVTNTSEGGYPEALSPLTNGLDKSYPMEPMVNGGGYPYESASRAGPAHAGHTAPMRPSYSAQEGLAGYQREGPHPAWPQPVTTSHYAHDPSGMFRSQSFSEAEPQLPPAPVRGGSSREAVQRGLNSWQQQQQQQQQPRPPPRQQERAHLESLVASRPSPQPLAETPIPSLPEFPRAASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSRQSHPLTQSRSGYIPSGHSLGTPEPAPRASLESVPPGRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPPASLPGLTAQPLLSPKEATSDPSRTPEEEPLNLEGLVAHRVAGVQAREKQPAEPPAPLRRRAASDGQYENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLHSYKEAFEEMEGTSPSSPPPSGVRSPPGLAKTPLSALGLKPHNPADILLHPTGVTRRRIQPEPRSYVESVARTAVAGPRAQDSEPKSFSAPATQAYGHEIPLRNGTLGGSFVSPSPLSTSSPILSADSTSVGSFPSGESSDQGPRTPTQPLLESGFRSGSLGQPSPSAQRNYQSSSPLPTVGSSYSSPDYSLQHFSSSPESQARAQFSVAGVHTVPGSPQARHRTVGTNTPPSPGFGWRAINPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSPQSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSLGRHPGAHQGNLASGLHSNAIASPGSPSLGRHLGGSGSVVPGSPCLDRHVAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGSLPNYATINGKVSSPVASGMSSPSGGSTVSFSHTLPDFSKYSMPDNSPETRAKVKFVQDTSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTIMQQNKKDMTHELVRHFLIETGPRGVKLKGCPNEPNFGSLSALVYQHSIIPLALPCKLVIPNRDPTDESKDSSGPANSTADLLKQGAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQERKWMKTEGGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVMLNAGQKR
Protein: Tyrosine-protein kinase RYK (EC 2.7.10.1) (Kinase VIK) (Met-related kinase) (NYK-R) (Q01887)
Organism: Mus musculus (Mouse)
Function: May be a coreceptor along with FZD8 of Wnt proteins, such as WNT1, WNT3, WNT3A and WNT5A. Involved in neuron differentiation, axon guidance, corpus callosum establishment and neurite outgrowth. In response to WNT3 stimulation, receptor C-terminal cleavage occurs in its transmembrane region and allows the C-terminal intracellular product to translocate from the cytoplasm to the nucleus where it plays a crucial role in neuronal development.
Subcellular location: Membrane {ECO:0000269|PubMed:19000841}; Single-pass type I membrane protein {ECO:0000269|PubMed:19000841}. Nucleus {ECO:0000269|PubMed:19000841}. Cytoplasm {ECO:0000269|PubMed:19000841}. Note=In cells that have undergone neuronal differentiation, the C-terminal cleaved part is translocated from the cytoplasm to the nucleus.
Interaction partners:
- Protein Wnt-5a
- Protein Wnt-11
- Protein Wnt-5b
- Frizzled-1
- Protein Wnt-3a
- Frizzled-4
- Frizzled-8
- Frizzled-2
- Protein Wnt-7a
- Frizzled-5
Sequence:
MRAGRGGVPGSGGLRAPPPPLLLLLLAMLPAAAPRSPALAAAPAGPSVSLYLSEDEVRRLLGLDAELYYVRNDLISHYALSFNLLVPSETNFLHFTWHAKSKVEYKLGFQVDNFVAMGMPQVNISAQGEVPRTLSVFRVELSCTGKVDSEVMILMQLNLTVNSSKNFTVLNFKRRKMCYKKLEEVKTSALDKNTSRTIYDPVHAAPTTSTRVFYISVGVCCAVIFLVAIILAVLHLHSMKRIELDDSISASSSSQGLSQPSTQTTQYLRADTPNNATPITSSSGYPTLRIEKNDLRSVTLLEAKAKVKDIAISRERITLKDVLQEGTFGRIFHGILVDEKDPNKEKQTFVKTVKDQASEVQVTMMLTESCKLRGLHHRNLLPITHVCIEEGEKPMVVLPYMNWGNLKLFLRQCKLVEANNPQAISQQDLVHMAIQIACGMSYLARREVIHRDLAARNCVIDDTLQVKITDNALSRDLFPMDYHCLGDNENRPVRWMALESLVNNEFSSASDVWAFGVTLWELMTLGQTPYVDIDPFEMAAYLKDGYRIAQPINCPDELFAVMACCWALDPEERPKFQQLVQCLTEFHAALGAYV
Protein: Seminal fluid protein 24F (Seminal fluid protein 24F, isoform B) (B4ZJ93)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RT03039p
- GEO08953p1
- trypsin
- SCP domain-containing protein
- RE43153p
- FI01450p
- Uncharacterized protein, isoform C
Sequence:
MIVKLTGSTTFLVALFLFEVSRNVAGALEALQTTNDTFVRIGNSYYLIERKLQKNWFGAYEICRQQQAELISLETFDELRLVSEYLLANNIFERYWTSGTDLGTKGKHVWFSNGQPLSTDLWYGGEPNNKNNEEHCDELGSDFRPTKSPGMNDRNCNFESSFICEEVQPKYNVCP
Protein: Caspase recruitment domain-containing protein 11 (CARD-containing MAGUK protein 1) (Carma 1) (Q9BXL7)
Organism: Homo sapiens (Human)
Function: Adapter protein that plays a key role in adaptive immune response by transducing the activation of NF-kappa-B downstream of T-cell receptor (TCR) and B-cell receptor (BCR) engagement. Transduces signals downstream TCR or BCR activation via the formation of a multiprotein complex together with BCL10 and MALT1 that induces NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways. Upon activation in response to TCR or BCR triggering, CARD11 homooligomerizes to form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10 and subsequent recruitment of MALT1: this leads to I-kappa-B kinase (IKK) phosphorylation and degradation, and release of NF-kappa-B proteins for nuclear translocation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Promotes linear ubiquitination of BCL10 by promoting the targeting of BCL10 to RNF31/HOIP. Stimulates the phosphorylation of BCL10. Also activates the TORC1 signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17287217}. Membrane raft {ECO:0000269|PubMed:17287217}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000269|PubMed:17287217}.
Interaction partners:
- B-cell lymphoma/leukemia 10
- Mucosa-associated lymphoid tissue lymphoma translocation protein 1
- Protein kinase C theta type
- NF-kappa-B essential modulator
- Protein kinase C beta type
- TNF receptor-associated factor 6
- Caspase recruitment domain-containing protein 10
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Mitogen-activated protein kinase kinase kinase 7
- Caspase recruitment domain-containing protein 14
Sequence:
MPGGGPEMDDYMETLKDEEDALWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPELYKLVTGKEPTRRFSTIVVEEGHEGLTHFLMNEVIKLQQQMKAKDLQRCELLARLRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRPKKEQVLELERENEMLKTKNQELQSIIQAGKRSLPDSDKAILDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCEMYKHRMNTVMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQSLPRNLPVTIISQDFGDASPRTNGQEADDSSTSEESPEDSKYFLPYHPPQRRMNLKGIQLQRAKSPISLKRTSDFQAKGHEEEGTDASPSSCGSLPITNSFTKMQPPRSRSSIMSITAEPPGNDSIVRRYKEDAPHRSTVEEDNDSGGFDALDLDDDSHERYSFGPSSIHSSSSSHQSEGLDAYDLEQVNLMFRKFSLERPFRPSVTSVGHVRGPGPSVQHTTLNGDSLTSQLTLLGGNARGSFVHSVKPGSLAEKAGLREGHQLLLLEGCIRGERQSVPLDTCTKEEAHWTIQRCSGPVTLHYKVNHEGYRKLVKDMEDGLITSGDSFYIRLNLNISSQLDACTMSLKCDDVVHVRDTMYQDRHEWLCARVDPFTDHDLDMGTIPSYSRAQQLLLVKLQRLMHRGSREEVDGTHHTLRALRNTLQPEEALSTSDPRVSPRLSRASFLFGQLLQFVSRSENKYKRMNSNERVRIISGSPLGSLARSSLDATKLLTEKQEELDPESELGKNLSLIPYSLVRAFYCERRRPVLFTPTVLAKTLVQRLLNSGGAMEFTICKSDIVTRDEFLRRQKTETIIYSREKNPNAFECIAPANIEAVAAKNKHCLLEAGIGCTRDLIKSNIYPIVLFIRVCEKNIKRFRKLLPRPETEEEFLRVCRLKEKELEALPCLYATVEPDMWGSVEELLRVVKDKIGEEQRKTIWVDEDQL
Protein: Uncharacterized protein F9D24.20 (Q9M2K5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASSPPSDPTDRDAETLSQNPSLIEKPSVVEQGSLSVENVAEKALNLESTQDEETQNLQDLEESDGRDQQLEASLEESRNEEDDMDTTQAVSSSYYRRGGGPKRKKGNQKKRKQLEKSKEKLEVLLKTLKPIAFAPCKTLDFARHEKLLKTLGLWDFVHLDFDQNIREDLVANLVAYYNSERRCSYVNGARINVSRPDLARALKLPMKKDFVVTEEERELLENDESVRFIDEIVSTCVLLQRDDMWIMPVEIVEWTRDIKQKHLEKLDWPKLLWFMVEKELKAEPPLGDCFFASHLQLLIKSQKEDLLKEKCKADDEEDDDDDDDDVKEVDFLVKSPKEDCLEVKEEDVGAADSRKDDGAVDLKEDKYVEEHMLELNLGQETVSEMVSGEERGPVEGQPMDVEENKKEEDERWAWNGDSHAGSHFLRRCNHSSAREGDEDNHIEGSMEMGEDEPIEDVEEEETEEDTEKHEGGFPFFPNGDSLQGVGQGNLMLGDASPLGYNSGLQIHGNSIGGDFLASRGEMHMAMGSGSSSLFGNGNNKREIEHENGITYHSHNPINKRLRTEEPSWDEKPPPVDMCLDQMAYWAEKARLSFAEKDREREQSVINQQYLMNELQSKTAMIQELERTKFEEQQRKDIMIYKLESELRMMTSVVEGYRKALKITQKASREHRKRCPLRDDKQVYMDVKGSGGLVLSTTEIEKLRLKQEEEDRMQRVLAKRQIDDFEHNWLNKFEEHMEAVELLNERLIENEDEVKILRETLSESKNIETSEVAAAMEETATEET
Protein: Proton-coupled zinc antiporter SLC30A5 (Solute carrier family 30 member 5) (Zinc transporter 5) (Q8WQB6)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004557}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004557}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000256|ARBA:ARBA00004638}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004638}. Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00004205}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004205}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004166}.
Interaction partners:
- Zrt
- Zrt
- Zinc transporter ZIP3
- Zinc transporter zipt-7.1
Sequence:
MLAHDFVKKDDRNFTPTQSSRSASYFVVLVLTKILRCIGVFFVDILAKSSHIVNLLWLCKIICTCILFPLQKPLSAGKSLKRGIMPMVLKLSLMNSVIEVFWFYGITLCGPLRSVLVFELSSTVLLSAVVSFFKGGNMSTPSKTRGFFLLIVGFVALFLMDRDGTIEDPHHTTHAHHSGLNHLFYHLIGLFGMADHKGGLCILLISLLLRTGYETSFRHLAVEVGGAKRLHTLVTAGSAVCLTPVAVLSWALSSSSGASIGYFHYAALLVIIAVFVFVLDFYAESICFQHVADPVMAAARWSSVTMFSCAFGLAYLWYGSQNLGDHALTGGVSITVVCFILASISLTHSNQPKHRGGHFVGISNTGLPLFTYGEAFLQRTSKSLMLFMKETLNEILMNNDSRRIFWFLCVNLGFCGVEFLYGFWTNSLGLISDGFHMLFDCSALVMGLVASVMARWPPTRHFTFGFGRVEILSGFINALFLCVIALFILIEALERLFDPPNINTDRLLFVAISGLIVNLFGMYSLGEHGHSHGGGSSHGHSHGGGGSHGHSHGGGGNANMQGVFLHVLADTLGSVFVIISTLLIQWFGWVWVDPLCSLILSLLIIGSVYPLLVSSISTLLQDVPEEEEFEYHINEILEIEHVESYSNAHMWQHKSDINVASVHVQVKEEANAQMIRHRVSNILKSTGATHSTVQVEKKTFAHRIQQVCPGYKAGYTVVRGSVIREKKHDHSHHHGHSHDDHSGHHH
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (A6NLJ7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004628}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004628}.
Interaction partners:
Sequence:
MKQTIGNSCGTIGLIHAVANNQDKLGFEDGSVLKQFLSETEKMSPEDRAKCFEKNEAIQAAHDAVAQEGQCRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDTLLKDAAKVCREFTEREQGEVRFSAVALCKAA
Protein: Protein YhjR (P0ADJ3)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Cyclic di-GMP binding protein BcsE
- Cyclic di-GMP-binding protein
- Cellulose biosynthesis protein BcsF
- Cellulose synthase catalytic subunit
- Cellulose biosynthesis protein BcsG
- Endoglucanase
Sequence:
MNNNEPDTLPDPAIGYIFQNDIVALKQAFSLPDIDYADISQREQLAAALKRWPLLAEFAQQK
Protein: Acetyl-CoA acetyltransferase (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) (P76461)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Fatty acid oxidation complex subunit alpha
- Fatty acid oxidation complex subunit alpha
- Acetate CoA-transferase subunit beta
- 3-hydroxyadipyl-CoA dehydrogenase
- Acetate CoA-transferase subunit alpha
- Acyl-coenzyme A dehydrogenase
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Phosphate acetyltransferase
- Acetaldehyde dehydrogenase
- 3-ketoacyl-CoA thiolase FadA
Sequence:
MKNCVIVSAVRTAIGSFNGSLASTSAIDLGATVIKAAIERAKIDSQHVDEVIMGNVLQAGLGQNPARQALLKSGLAETVCGFTVNKVCGSGLKSVALAAQAIQAGQAQSIVAGGMENMSLAPYLLDAKARSGYRLGDGQVYDVILRDGLMCATHGYHMGITAENVAKEYGITREMQDELALHSQRKAAAAIESGAFTAEIVPVNVVTRKKTFVFSQDEFPKANSTAEALGALRPAFDKAGTVTAGNASGINDGAAALVIMEESAALAAGLTPLARIKSYASGGVPPALMGMGPVPATQKALQLAGLQLADIDLIEANEAFAAQFLAVGKNLGFDSEKVNVNGGAIALGHPIGASGARILVTLLHAMQARDKTLGLATLCIGGGQGIAMVIERLN