wanglab/gogpt-training-data huggingface dataset:
Protein: Fanconi anemia group G protein homolog (Protein FACG) (Q9EQR6)
Organism: Mus musculus (Mouse)
Function: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Candidate tumor suppressor gene (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11918676}.
Interaction partners:
- Fanconi anemia group C protein homolog
- Fanconi anemia group A protein homolog
- Fanconi anemia group M protein homolog
- Fanconi anemia group F protein
- Fanconi anemia core complex-associated protein 24
- E3 ubiquitin-protein ligase FANCL
- Fanconi anemia core complex-associated protein 100
- Fanconi anemia group B protein homolog
- Fanconi anemia, complementation group E
- Fanconi anemia group D2 protein homolog
Sequence:
MSSQVIPALPKTFSSSLDLWREKNDQLVRQAKQLTRDSRPSLRRQQSAQDTLEGLRELLLTLQGLPAAVPALPLELTVLCNCIILRASLVQAFTEDLTQDLQRGLERVLEAQHHLEPKSQQGLKELWHSVLSASSLPPELLPALHCLASLQAVFWMSTDHLEDLTLLLQTLNGSQTQSSEDLLLLLKSWSPPAEESPAPLILQDAESLRDVLLTAFACRQGFQELITGSLPHAQSNLHEAASGLCPPSVLVQVYTALGACLRKMGNPQRALLYLTEALKVGTTCALPLLEASRVYRQLGDRAAELESLELLVEALSATHSSETFKSLIEVELLLPQPDPASPLHCGTQSQAKHLLASRCLQTGRAEDAAEHYLDLLAMLLGGSETRFSPPTSSLGPCIPELCLEAAAALIQAGRALDALTVCEELLNRTSSLLPKMSSLWENARKRAKELPCCPVWVSATHLLQGQAWSQLKAQKEALSEFSQCLELLFRTLPEDKEQGSDCEQKCRSDVALKQLRVAALISRGLEWVASGQDTKALSDFLLSVQICPGNRDGSFYLLQTLKRLDRKNEASAFWREAHSQLPLEDAAGSLPLYLETCLSWIHPPNREAFLEEFGTSVLESCVL
Protein: F-box protein 11, isoform A (F-box protein 11, isoform B) (Q9VH60)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Partner of paired, isoform B
- Cullin homolog 1
- GEO01111p1
- F-box only protein 9
- Cullin 6
Sequence:
MPSASFTSSRTYVRRSRRKGANRIAMPNRPTGNIMDPMLQQNVTAAGAGASASGSNSNAASSSGAGGVGNNNASSSGSSGATSTSGSAAAAASAAGPTAAGASSSAEYFDSGQGASGSSGAASSGFSGSFYNALQMMDTTESSGAGTSQSTPPALGASSTTASKSTCATVGSSTASTSAAAAAAASASAGSSHQSPYDLRRKISASSHEQWPTSSSSAVAAAAAILVGPSSSSPPLVNPGASPSSSSSSSSSSSSSSSASSSSSSSNVQAPSTSATFPVNNAPTTGATLAQPPNVHSSVPQQHCGALPVGAAIEDNNYMLPARKRSRRLYTQGGEMGPSAGATGEAAGAGTAASGGAGCAPTAAQYLQYELPDEVLLAIFSYLMEQDLCRLALVCKRFNTIANDTELWKRLYQSVFEYDLPLFNPELCKFVFEKPEESEYANPWKESFRQLYRGVHVRPGYQERRSSGRSIVFFNTIQAALDYPEERAAAGVFVPAGAGAGNVVSAGLSNTSASAGVGGASVNALVNIYEEQVAPTEHPGPLIFLHAGHYKGEYLFIDSDVALVGAAPGNVAESVILEREAGSTVMFVEGAKYAYVGYLTLKFSPEVTSTVSHHKHYCLDIGENCSPTVDNCIIRSTSVVGAAVCVGGVNANPVIRNCDISDCENVGLYVTDYAQGTYEHNEISRNALAGIWVKNFASPIMRENHIHHGRDVGIFTFENGMGYFEKNDIHNNRIAGFEVKAGANPTVVKCEIHHGQTGGIYVHENGLGQFIENRIHSNNFAGVWITSNSNPTIRKNEIYNGHQGGVYIFGEGRGLIEHNNIYGNALAGIQIRTNSDPIVRHNKIHHGQHGGIYVHEKGQGLIEENEVYSNTLAGVWITTGSTPVLRRNRIHSGKQVGVYFYDNGHGKLEDNDIFNHLYSGVQIRTGSNPVIRGNKIWGGQNGGVLVYNGGLGLLEQNEIFDNAMAGVWIKTDSNPTLKRNKIYDGRDGGICIFNGGKGILEENDIFRNTQAGVLISTQSHPILRRNRIYDGQAAGVEITNNATATLEHNQIFKNKFGGLCLASGVQPITRGNNIFNNEDEVEKAVSSGQCLYKISSYTSFPMHDFYRCQTCNTTDRNAICVNCIKNCHAGHDVEFIRHDRFFCDCGAGTLSNQCQLQGEPTQDTDTLYDSAAPMESHTLMVN
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (Q62884)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MKPAARETRTPPRSPGLRWALLPLLLLLRQGQVVCTGAAPSPVFDVEAVTSPTSVVLTWKHNDSATSEYKINEGNTLRYTVKNQTSFNITGLSPATSYKFSITLGTVNETSGKPTYKNITTEPWPVSDLQVAYIGVTQALLAWSNANGTASYRMQIVELTTNSSGGISDLKPGTHKSLAVQGSNETQHDLWVTEGVSDPPSARDPSLTEVLLTELKPDTQYKVTIYSQAADGTEGQPGNKVFKTNPIQVSDIRAVNISDSNMTLTWKSNNNESHASFTYKIYVAGGSDSINETVNETQAVIRGLSSSTLYNITVLPFLGQTAGIPGFLQVYTSPRPVSDFRVTNVSLREIGLAWRSNDSESFEIFITQEGSEKRWNASTGDLSYIVVNLKPGTSYQFEIFPRGPNGTEGPSQTVVGRTDCSAVTDIRVVSVSTTEIQLEWQNTDSASGYTYHLVLESENGSIKTNSSQKWITVGGLTPGTLYNVTIFPEVDQMEGNSSSITQYTRPSNVSYIEVNTNTTVGAIQWKNLDAASASYSYSVLILKAGDGSNVTSRVRDIPSVTIPGLIPGVSSEVKIFTKIRNTEVGNEVPGQKLFCMEPAQVDSLHCEVVPKEPALVLKWACPPGMNSGFELGVRSDAWDNMTHLENCTLDNDTECRTEVTYLNFSTSYNISIATLSCGKMALPTQSTCTTGITDPPPPDGSPNITSVSHNSVKVKFSGFEASHGPIKAYAVLLTTGEAGQPSTDVLKYTYEDFKKGASDTYVTYLIRIEEKGQSQGLSEALNYEIDVGNQSTTLGYYNGRLEPLGSYRACVAGFTNITYNLQNDGLINGDESYVSFSPYSEAVSLPQDPGVICGAVFGCIFGALAIVAVGGFIFWRKKRKDAKNNEVSFSQIKPKKSKLIRVENFEAYFKKQQADSNCGFAEEYEDLKLIGISLPKYAAEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQSSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIRAQKDSKVDLIYQNTTAMTIYENLERVSMFGKANGYIA
Protein: single-stranded DNA cytosine deaminase (EC 3.5.4.38) (B7TQM3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MALLTAETFRLQFNNKRRLRRPYYPRKALLCYQLTPQNGSTPTRGYFENKKKCHAEICFINEIKSMGLDETQCYQVTCYLTWSPCSSCAWELVDFIKAHDHLNLGIFASRLYYHWCKPQQKGLRLLCGSQVPVEVMGFPEFADCWENFVDHEKPLSFNPYKMLEELDKNSRAIKRRLERIKQS
Protein: Transmembrane gamma-carboxyglutamic acid protein 4 (Proline-rich gamma-carboxyglutamic acid protein 4) (Proline-rich Gla protein 4) (Q9BZD6)
Organism: Homo sapiens (Human)
Function: May control axon guidance across the CNS. Prevents the delivery of ROBO1 at the cell surface and down-regulates its expression.
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:28859078}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:23873930}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Glutamine and serine-rich protein 1
Sequence:
MFTLLVLLSQLPTVTLGFPHCARGPKASKHAGEEVFTSKEEANFFIHRRLLYNRFDLELFTPGNLERECNEELCNYEEAREIFVDEDKTIAFWQEYSAKGPTTKSDGNREKIDVMGLLTGLIAAGVFLVIFGLLGYYLCITKCNRLQHPCSSAVYERGRHTPSIIFRRPEEAALSPLPPSVEDAGLPSYEQAVALTRKHSVSPPPPYPGHTKGFRVFKKSMSLPSH
Protein: Leukocyte immunoglobulin-like receptor subfamily B member 1 (LIR-1) (Leukocyte immunoglobulin-like receptor 1) (CD85 antigen-like family member J) (Immunoglobulin-like transcript 2) (ILT-2) (Monocyte/macrophage immunoglobulin-like receptor 7) (MIR-7) (CD antigen CD85j) (Q8NHL6)
Organism: Homo sapiens (Human)
Function: Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles. Receptor for H301/UL18, a human cytomegalovirus class I MHC homolog. Ligand binding results in inhibitory signals and down-regulation of the immune response. Engagement of LILRB1 present on natural killer cells or T-cells by class I MHC molecules protects the target cells from lysis. Interaction with HLA-B or HLA-E leads to inhibition of FCER1A signaling and serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions. Recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide. Upon interaction with peptide-bound HLA-G-B2M complex, triggers secretion of growth-promoting factors by decidual NK cells. Reprograms B cells toward an immune suppressive phenotype.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20448110, ECO:0000269|PubMed:24453251, ECO:0000269|PubMed:29262349, ECO:0000305|PubMed:19658091}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 5]: Secreted {ECO:0000269|PubMed:19658091}.
Interaction partners:
- HLA class I histocompatibility antigen, alpha chain F
- HLA class I histocompatibility antigen, A alpha chain
- HLA class I histocompatibility antigen, alpha chain G
- Beta-2-microglobulin
- HLA class I histocompatibility antigen, C alpha chain
- HLA class I histocompatibility antigen, alpha chain E
- Large ribosomal subunit protein uL18
- Tyrosine-protein phosphatase non-receptor type 6
- HLA class I histocompatibility antigen, B alpha chain
- CMRF35-like molecule 6
Sequence:
MTPILTVLICLGLSLGPRTHVQAGHLPKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRLYREKKTALWITRIPQELVKKGQFPIPSITWEHAGRYRCYYGSDTAGRSESSDPLELVVTGAYIKPTLSAQPSPVVNSGGNVILQCDSQVAFDGFSLCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPSRRWWYRCYAYDSNSPYEWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPEETLTLQCGSDAGYNRFVLYKDGERDFLQLAGAQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSEWSAPSDPLDILIAGQFYDRVSLSVQPGPTVASGENVTLLCQSQGWMQTFLLTKEGAADDPWRLRSTYQSQKYQAEFPMGPVTSAHAGTYRCYGSQSSKPYLLTHPSDPLELVVSGPSGGPSSPTTGPTSTSGPEDQPLTPTGSDPQSGLGRHLGVVIGILVAVILLLLLLLLLFLILRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKHTQPEDGVEMDTRSPHDEDPQAVTYAEVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMDTEAAASEAPQDVTYAQLHSLTLRREATEPPPSQEGPSPAVPSIYATLAIH
Protein: Ubiquitin-associated domain-containing protein 1 (Kip1 ubiquitination-promoting complex protein 2) (A0A140VK64)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MFVQEEKIFAGKVLRLHICASDGAEWLEEATEDTSVEKLKERCLKHCAHGSLEDPKSITHHKLIHAASERVLSDARTILEENIQDQDVLLLIKKRAPSPLPKMADVSAEEKKKQDQKAPDKEAILRATANLPSYNMDRAAVQTNMRDFQTELRKILVSLIEVAQKLLALNPDAVELFKKANAMLDEDEDERVDEAALRQLTEMGFPENRATKALQLNHMSVPQAMEWLIEHAEDPTIDTPLPGQAPPEAEGATAAASEAAAGASATDEEARDELTEIFKKIRRKREFRADARAVISLMEMGFDEKEVIDALRVNNNQQNAACEWLLGDRKPSPEELDKGIDPDSPLFQAILDNPVVQLGLTNPKTLLAFEDMLENPLNSTQWMNDPETGPVMLQISRIFQTLNRT
Protein: ADP-ribosylation factor-like protein 4A (P61213)
Organism: Mus musculus (Mouse)
Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in GDP-bound form (By similarity).
Subcellular location: Cell membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Localization in the nucleolus is dependent by nucleotide binding. {ECO:0000250}.
Interaction partners:
- GRIP and coiled-coil domain-containing protein 2
Sequence:
MGNGLSDQTSILSSLPSFQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIKVTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVDSVDVERMEEAKTELHKITRISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTPWHLQPTCAIIGDGLKEGLEKLHDMIIKRRKMLRQQKKKR
Protein: Protein transport protein sec23 (Q5BGR9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Protein transport protein sec31
- Protein transport protein sec24
- Protein transport protein sec13
- Vesicle coat complex COPII, subunit Sec24 family protein, putative
- Small COPII coat GTPase sar1
- COPII coat assembly protein sec16
- Uncharacterized protein
- ER-golgi SNARE complex subunit Bet1
- ER-Golgi SNARE complex subunit Sed5
- Guanine nucleotide-exchange factor SEC12
Sequence:
MDYEGLKDQWSDVEDRDGIRLSWNTFPSSRMEASRLVVPIGAIYTPLKERPDAPLLQYEPVTCKAPCRAVLNPYANVDVRARIWICPFCLMRNPLPPHYKDITESTIPPELHPLSTTIEYQLARPAPAPPIFVFVVDTCQEDDSLKAVKDSLILSLSLLPPNALVGLITFGTMAQVHELGYTECAKSYVFRGSKDYNAKQVQEMLGLASGIRPNMPNMPQQPVRPPLGAAARFLLPVQQAEFQITNMLEQLQRDPWPVANDKRPLRCTGVALNVAVGLLESSFQNAGAHIMLFTSGPATEGPGLVVSPELKEPIRSHHDIDRDNIKYYKKALKFYDALAKRAANNGHVVDLFAGCLDQVGLLEMKNLANYTGGHILLTDSFTSSQFKQSFIRVFDKDANDNLLMGFNASLEVLTTKELKVTGLIGHAVSLNKKSSSVGETECGIGNTCAWKMCGIDPSSSYGIYFEIANQGGPAAVQPGPQRGMMQFLTYYQHSSGHFHLRVTTVARNLSGPAGDPTLAQSFDQEAAAVLMARIGVFKAEVDDGPDVLRWVDRMLIRLCSRFADYRKDDPTSFRLEKNFTLYPQFMFHLRRSQFLQVFNNSPDETAFYRHVLNHEDVGDSLIMIQPTLDSYSLEHEGSLPVLLDSASIQPTHILLLDTFFHILIFHGETIAEWRKAGYQDQEGYENLKALLDLPKEDARELISERFPLPRFIVCDAGGSQARFLLSKLNPSTTHTTGGYGGGVSSQTIFTDDVSLQTFMDHLMKLAVSGTS
Protein: Protein JOKA2 (Protein NBR1 homolog) (M1BJF6)
Organism: Solanum tuberosum (Potato)
Function: Autophagic substrate that functions as host autophagy cargo receptor (Probable). Requires ATG8 protein expression to be recognized as an autophagic substrate (Probable). Activates ATG8CL-mediated selective autophagy, and contributes to defense against the fungal pathogen Phytophtora infestans.
Subcellular location: Vacuole {ECO:0000269|PubMed:29932422}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:29932422}.
Interaction partners:
- Autophagy-related protein 8C-like
- Autophagy-related protein
- Autophagy-related protein
- Autophagy-related protein
- Autophagy-related protein
- Autophagy-related protein
- Ubiquitin extension protein
- Ubiquitin extension protein
- Zinc ion binding protein
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MAMESSIVIKVKYEETLRRFNACVINEKLDLDIGGLRDKIIQLFNFAHDAELTLTYIDEDGDVVTLVDDEDLQDVMRQDLNPLRISARLNAGERSGRASARSSGNSTPLRSPRVQPPFLNLNSRVSDVLKYIPEPLRESVMKVCSDMTASASSSAPILAELVDAMSEMGLSYYQNQASGSQAVKEAGSCSGISKGNTKSADGGMPNVKIGESSPKKNRPLTALHGEPKPNASNEAVDASVKLVCKSETLEGDRTEDLSSSFKGSKAQTSLVNSLEKDKKFDVRSLDGRTIGYAYVRNSPIPPEKTSDEQPSKGHPVAKPVDLGGSASSSKVKQCNWDSPNADSSGSSINMPYDGFTPSGLVHLNTVNVNDSHNAGSSGSSMKMPYDGFRPAVRHLGPLIPVNACPFSGVPTVNNPIPPQNFSFEVPLKRSHNHSDGTGTIFHKGVRCDGCGVHPITGPRFISKVKENYDLCSICFAEMGNDADYIRMDRPLTYPNPWSFKSLHDLHGRLRPRPPTVPQVIRGFGLKAGRPKLDSRFIQDVNVLDGTIMAPLTRFTKIWRMKNNGNLVWPQGTQLVWIGGDKLSDRFSVELEITTAGLAVDQELDVAVDFTAPEHPGRYISYWRLASASGQKFGQRVWVLIQVDALLSVPKKGLVHEAFQGLNLNLPPAGSGVSGPDIINVNSEPQNVLPEPKSSSTMELVDSVAEVNQNKEQEAKFPINDSLLVGFGDKSSSPSASGSPISYPVIDLTEKPSADSSMQPSAAVAMQAPLQDARGNFEVEMSLLQELEEMGFKQVDLNKEILRKNEYDLEQSVDDLCGVAEWDPILEELKEMGFCDKEMNKKLLKKNNGSIKRVVMDLIAGEQ
Protein: Tubulin alpha 4a (C9JDL2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MKVRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDP
Protein: Peroxisome biogenesis factor 10 (EC 2.3.2.27) (E3 ubiquitin-protein ligase PEX10) (Peroxin-10) (Peroxisomal biogenesis factor 10) (Peroxisome assembly protein 10) (Peroxisome assembly protein PAS7) (Q92265)
Organism: Komagataella pastoris (Yeast) (Pichia pastoris)
Function: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 and/or PEX20 receptors from peroxisomes to the cytosol, thereby promoting PEX5 and PEX20 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 and/or PEX20 through the peroxisomal membrane (By similarity). PEX10 also regulates PEX5 and/or PEX20 recycling by acting as a E3 ubiquitin-protein ligase (By similarity). When PEX5 or PEX20 recycling is compromised, PEX10 catalyzes polyubiquitination of PEX5 and/or PEX20 during their passage through the retrotranslocation channel, leading to its degradation (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:7565793}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPPSEEIKLRAVSPRPDFKANYLEFANAPAIVRANQKDSYFETVLRDKLQNVIQIFKGQRFTHTHPEEIGVAAKALYLSLTTLLGTKTLGEEYVDLIYVSRDGKRIPRYLARAGFIFAYAILPYFLTRLFRRLKSSSTPKDEVTEEKINKELPISLRIEKYLSNMSYSKVLDTIMNLHIAVFYFSGQFYNISKRFFSMRYAFGHKINKERTPNGNYELLGGLIVLQLVMKSLGGFKGLIGSFTGNDEHDESNLRANNKDIMYGIPSEEEQEEAKQQLGIIDLSDPGQLPYIPESSRQCMLCLSYMTNPTAANCGHCFCWSCIIDWCKERQTVLCVGKKCWNSNCYHCIRLFYIPTLNKICFFFLLSFLSVRAASKEFKSTKEEFAELFNEELADIAGEDPHCPGPFPTGRTLGYFLVVF
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (A0A3B3IRY8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MALDYLLLLLLASAVAAMEETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWSEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKKCPSIVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKPGYEPENSVACKACPAGTFKASQEAEGCSHCPSNSRSPAEASPICTCRTGYYRADFDPPEVACTSVPSGPRNVISIVNETSIILEWHPPRETGGRDDVTYNIICKKCRADRRSCSRCDDNVEFVPRQLGLTECRVSISSLWAHTPYTFDIQAINGVSSKSPFPPQHVSVNITTNQAAPSTVPIMHQVSATMRSITLSWPQPEQPNGIILDYEIRYYEKEHNEFNSSMARSQTNTARIDGLRPGMVYVVQVRARTVAGYGKFSGKMCFQTLTDDDYKSELREQLPLIAGSAAAGVVFVVSLVAISIVCSRKRAYSKEAVYSDKLQHYSTGRGSPGMKIYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVYKGRLKLPGKREIYVAIKTLKAGYSEKQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLAEMNYVHRDLAARNILVNSNLVCKVSDFGLSRYLQDDTSDPTYTSSLGGKIPVRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPMDCPAALHQLMLDCWQKDRNSRPRFAEIVNTLDKMIRNPASLKTVATITAVPSQPLLDRSIPDFTAFTTVDDWLSAIKMVQYRDSFLTAGFTSLQLVTQMTSEHHLGRPSEEDPEQHSFYEGPDKSVTNGNGMRTLVSWGRRGGKRTRVKGDQRLTTVECTGETGFSAEECISISEESTGPVASRQSPFLSDRSMFEMPWETKYIIIKI
Protein: Tail tube protein gp19 (Gene product 19) (gp19) (P13333)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Forms the central cylindrical rigid tube, which is surrounded by the outer contractile sheath assembled from gp18 subunits. The tail tube first 2 annuli are formed by gp48 and gp54, which are in continuation of the spike complex. During infection, contraction of the sheath drives the central tube through the host outer membrane, creating a channel for DNA ejection from the capsid into the host cell.
Subcellular location: Virion {ECO:0000269|PubMed:15315755, ECO:0000269|PubMed:27193680}.
Interaction partners:
Sequence:
MFVDDVTRAFESGDFARPNLFQVEISYLGQNFTFQCKATALPAGIVEKIPVGFMNRKINVAGDRTFDDWTVTVMNDEAHDARQKFVDWQSIAAGQGNEITGGKPAEYKKSAIVRQYARDAKTVTKEIEIKGLWPTNVGELQLDWDSNNEIQTFEVTLALDYWE
Protein: Ribosomal silencing factor RsfS (Large ribosomal subunit assembly factor RsfS) (P0AAT6)
Organism: Escherichia coli (strain K12)
Function: Functions as a ribosomal silencing factor. Addition to isolated ribosomal subunits partially inhibits their association, preventing translation. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8, preventing association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01477, ECO:0000269|PubMed:16980477, ECO:0000269|PubMed:22829778, ECO:0000269|PubMed:33639093}. Note=Comigrates with the 50S ribosomal subunit in sucrose gradients (PubMed:16980477), specifically with ribosomal protein uL14 (rplN) (PubMed:22829778). In pre-50S ribosomal subunits interacts with uL14 (rplN), bL19 (rplS) and ObgE (PubMed:33639093). {ECO:0000269|PubMed:22829778, ECO:0000269|PubMed:33639093}.
Interaction partners:
- GTPase ObgE/CgtA
- Ribosomal RNA large subunit methyltransferase H-methyltransferase)
- Large ribosomal subunit protein uL14
- Nicotinate-nucleotide adenylyltransferase
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein uL24
- Ribosomal large subunit pseudouridine synthase D synthase)
- Large ribosomal subunit protein bL32
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL2
Sequence:
MQGKALQDFVIDKIDDLKGQDIIALDVQGKSSITDCMIICTGTSSRHVMSIADHVVQESRAAGLLPLGVEGENSADWIVVDLGDVIVHVMQEESRRLYELEKLWS
Protein: Uncharacterized protein, isoform B (A0A0B4JCT2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Uncharacterized protein, isoform A
- Accessory gland protein Acp36DE
- AT03573p
- Lectin-46Ca
- ACP24A4
- Seminase
- FI08238p
- Glycerol-3-phosphate dehydrogenase
- Aquarius
- IP12902p
Sequence:
MLDTKWPPLLLLLMLLGQQLQAFDYCDPTLCPGPERHIACNNFGALADICSPDAHIVRITTARRTMILNELNEYRDRIARGDLMGFSPATRMATLQWDQELASFAELNVKRCALVNDHCRNSEQFRNVAQVVAEGGWQGDPLPPSSPSDPPNPEAPIPVEYHTEDEVIKATLEQMFAEYKECSMRDIIAFSPPNNRILRLRVSKCIAYFTQLVRDSTTHVGCGILRQTKNTTNEAGQSLSSVHQYMTCNFVRTNDVNAPVYQSGDRPATECRSGRNPVFINLCSVNEIYDSSNLAGLF
Protein: Prefoldin subunit 2, putative (Q382R3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Prefoldin subunit 3
- Prefoldin subunit 4
- Prefoldin subunit, putative
- Prefoldin, putative
- Prefoldin subunit
- Prefoldin subunit
- CCT-beta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit eta
- Translation elongation factor 1-beta, putative
Sequence:
MAATNSPTEEEVVMRYQQLRQECLAMDSRISELENELHEHQLVADTLKPLNGDRRCHRLVGGALIERTVADILPELVENIKGIEEALAQLNKMLTEKQAAMDEYARKHGVTVAQRQGQTPAGGGGANNDEGEKKPMGADSRGVLV
Protein: Secretin/TonB short N-terminal domain-containing protein (Q9I226)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}.
Interaction partners:
- Luciferase-like domain-containing protein
- Major facilitator superfamily
- Probable major facilitator superfamily
- Probable sigma-70 factor, ECF subfamily
- Probable transmembrane sensor
- asparagine synthase
- Probable transcriptional regulator
- Probable TonB-dependent receptor
- L-2-amino-thiazoline-4-carboxylic acid hydrolase
- Peptidase C13
Sequence:
MSNPRSPRLRLVPVLCAVGLACLGQPGESAAEEVRATSSAEIQRFDIPAGELAQVLLSIVRQSRTPIAFDQHLVEGLPAPAIQGSYSVEQALQRALQGSGLEYSRSAAGVLSLQRATAPDAALPAAKPAGTLATVVVTGTRKADVKAGESLAPIDVVSAEQLRDSGSGDLRDALVRLLPSLSRQAQAYNASALTNAQSLRGLSPNHVLVLVNGKRRHETANINVSGGLQSGSTGVDLDTIPLAAIERIEVLRDGASAQYGSDAIAGVINVILKSADHGGRLAYDNGRYGDGDGLTQNGGVNGGLRFGESGFLNLSAQFREQARTIRAGIDQRTGHYGNPSIGDPSLHRQALAYNAGVALDDNVELYSFATYTHRSVSSAQIYQLPSLAPRLYPNGFTPRITSDEDDYSLTLGARGGELFGAWDWDLSSTYGADRPEIGMDHSINLALYGETGDSPRSFDLARYKATQWTNNLDLRRDFDLAWLPAPLNFSWGLEQRRELYEVEAGDPWSYYNGGSKALPGQAPATAGQWSRDVLGAYLDLSIALDERWQLETAARYEHYSDFGSTTNGKLASRYRFSPEVSARASLSSGFRAPSLAQENYTSLGVSPTIASGLLAVNSPAARLLGAEDLEPEKSISYNLGLVLDPLPDLNLAIDAYRIEIRDRIVDGATYSGQPAIDALRAGGISIPAGLTQVSTHYMTNGADTRTHGLDLTASYLTRLGEWGRIDWRLGANVNRTKLVRNHRGRNGQPLLNDQQQAWITSSTPRSQVSLQADWSYRRWGLTLRETRYSKTVSELDYYTGEHAYSTTVFNRFENSPKYITDVALRYAASRNLTLSAGANNLFDVKPDKLPAESAYLGFNQYDTYASQISFNGAFYYLGAAYTF
Protein: Cuticle collagen sqt-1 (Protein roller-5) (Protein squat-1) (P12114)
Organism: Caenorhabditis elegans
Function: Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment. This is a collagen critical for organismal morphogenesis. Mutations in sqt-1 can lengthen, shorten, or helically twist the entire animal.
Interaction partners:
- Cuticle collagen rol-6
- Cuticle collagen 6
- COLlagen
- Cuticle collagen lon-3
- Cuticle collagen dpy-5
- Nematode cuticle collagen N-terminal domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
Sequence:
MSVKLACYVTASVTVATLMVCFMTMSTIYSEVDGFREKLDTEMNVFRQSTNGLWKDIVVIGRSSKRVRRQYEETNATPTPHADGSPSAPPGQPPAVPPVFNQPKTPNGANGNGPTCNCNADNKCPAGPSGPKGVPGVPGLDGVPGLDGVPGVGADDIAPQRESVGCFTCPQGPVGPPGALGRPGPRGLPGPRGQNGNPGRDGQPGHPGEQGSSGQIGKIGEPGPPGEKGRDAEHPIGRPGPKGPRGDQGPTGPAGQNGLHGPPGEPGTVGPEGPSGKQGRQGPDGTQGETGPDGRPGKDAEYCQCPDKSPPSEAVNANRGYRNI