wanglab/gogpt-training-data huggingface dataset:
Protein: Hedgehog-interacting protein (HHIP) (HIP) (Q7TN16)
Organism: Mus musculus (Mouse)
Function: Modulates hedgehog signaling in several cell types, including brain and lung through direct interaction with members of the hedgehog family. Soluble forms inhibit Shh-induced differentiation in the fibroblast cell line C3H/10T1/2.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10050855}; Peripheral membrane protein {ECO:0000269|PubMed:10050855}. Secreted {ECO:0000269|PubMed:10050855}. Note=The last 22 C-terminal amino acids may participate in cell membrane attachment.
Interaction partners:
- Sonic hedgehog protein
- Desert hedgehog protein
- Indian hedgehog protein
- Protein patched homolog 1
- Zinc finger protein GLI1
- Protein FAM13A
- Protein smoothened
- Zinc finger protein GLI2
- Protein patched homolog 2
- Transcriptional activator GLI3
Sequence:
MLKMLSFKLLLLAVALGFFEGDAKFGERNEGSGARRRRCLNGNPPKRLKRRDRRVMSQLELLSGGEILCGGFYPRVSCCLQSDSPGLGRLENKIFSATNNSECSRLLEEIQCAPCSPHSQSLFYTPERDVLDGDLALPLLCKDYCKEFFYTCRGHIPGLLQTTADEFCFYYARKDAGLCFPDFPRKQVRGPASNYLGQMEDYEKVGGISRKHKHNCLCVQEVMSGLRQPVSAVHSGDGSHRLFILEKEGYVKILTPEGELFKEPYLDIHKLVQSGIKGGDERGLLSLAFHPNYKKNGKLYVSYTTNQERWAIGPHDHILRVVEYTVSRKNPHQVDVRTARVFLEVAELHRKHLGGQLLFGPDGFLYIILGDGMITLDDMEEMDGLSDFTGSVLRLDVDTDMCNVPYSIPRSNPHFNSTNQPPEVFAHGLHDPGRCAVDRHPTDININLTILCSDSNGKNRSSARILQIIKGRDYESEPSLLEFKPFSNGPLVGGFVYRGCQSERLYGSYVFGDRNGNFLTLQQSPVTKQWQEKPLCLGASSSCRGYFSGHILGFGEDELGEVYILSSSKSMTQTHNGKLYKIVDPKRPLMPEECRVTVQPAQPLTSDCSRLCRNGYYTPTGKCCCSPGWEGDFCRIAKCEPACRHGGVCVRPNKCLCKKGYLGPQCEQVDRNVRRVTRAGILDQIIDMTSYLLDLTSYIV
Protein: Actin-related protein 2/3 complex subunit 1A-A (Q8AVT9)
Organism: Xenopus laevis (African clawed frog)
Function: Probably functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks (By similarity). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (Probable).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q92747}. Nucleus {ECO:0000269|PubMed:29925947}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 3-A
- Actin-related protein 3-B
- Actin-related protein 2/3 complex subunit 2-A
- Actin-related protein 2/3 complex subunit 2-B
- Actin-related protein 2/3 complex subunit 3-A
- Actin-related protein 2/3 complex subunit 3-B
- Actin-related protein 2/3 complex subunit 5-B
- Actin-related protein 2/3 complex subunit 5-A
- Actin-related protein 2
Sequence:
MSLHQFLLEPISCHAWNKDLTQIAISPNNHEVHIYKKSGDQWVKGHELKEHNGHITGIDWAPKSDRIVTCGADRNAYVWSQKDGVWKPTLVILRINRAATFVKWSPLENKFAVGSGARLISVCYFESENDWWVSKHIKKPIRSTVLSLDWHPNNVLLAAGSCDFKTRVFSAYIKEVDEKPASTPWGSKMPFGQMMAEFGGVSSGGWVHSVSFSASGNKLAWVSHDSTVSVADASKNMSVSQLKTEFLPLLSVIFVSENSLIAAGHDCCPMLFTYDEHGSLTFVSKLDIPKQSTQRNISAMERFRNMDKRATTEDRNTTLETLHQNSITQVSIYDGDKTECRKFCTTGIDGAMTIWDFKTLESYIQGLKIM
Protein: Large ribosomal subunit protein uL23 (60S ribosomal protein L23a) (F1QGI3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Ribosomal protein L4
- Ribosomal protein L3
- Mitochondrial ribosomal protein L27.
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein eL27
- Large ribosomal subunit protein uL30
- Small ribosomal subunit protein RACK1
- Elongation factor Tu
- Large ribosomal subunit protein eL6
- Small ribosomal subunit protein uS14
Sequence:
MAPKAKKEAVPAKTEAKSKALKAKKAVLKGVHSQKKKKIRTTPTFHRPKTLRLRRQPKYPRKSAPRRNKLDHYAIIKFPLTTESAMKKIEDNNTLVFIVDVKANKHQIKHAVKKLYDIDVAKVNTLIRPDGEKKAYVRLAPDYDALDVANKIGII
Protein: RNA helicase (EC 3.6.4.13) (Q5SQH4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATPAGLERWVQDELHSVLGLSERHVAQFLIGTAQRCTSAEEFVQRLRDTDTLDLSGPARDFALRLWNKVPRKAVVEKPARAAEREARALLEKNRSYRLLEDSEESSEETVSRAGSSLQKKRKKRKHLRKKREEEEEEEASEKGKKKTGGSKQQTEKPESEDEWERTERERLQDLEERDAFAERVRQRDKDRTRNVLERSDKKAYEEAQKRLKMAEEDRKAMVPELRKKSRREYLAKREREKLEDLEAELADEEFLFGDVELSRHERQELKYKRRVRDLAREYRAAGEQEKLEATNRYHMPKETRGQPARAVDLVEEESGAPGEEQRRWEEARLGAASLKFGARDAASQEPKYQLVLEEEETIEFVRATQLQGDEEPSAPPTSTQAQQKESIQAVRRSLPVFPFREELLAAIANHQVLIIEGETGSGKTTQIPQYLFEEGYTNKGMKIACTQPRRVAAMSVAARVAREMGVKLGNEVGYSIRFEDCTSERTVLRYMTDGMLLREFLSEPDLASYSVVMVDEAHERTLHTDILFGLIKDVARFRPELKVLVASATMDTARFSTFFDDAPVFRIPGRRFPVDIFYTKAPEADYLEACVVSVLQIHVTQPPGDILVFLTGQEEIEAACEMLQDRCRRLGSKIRELLVLPIYANLPSDMQARIFQPTPPGARKVVVATNIAETSLTIEGIIYVLDPGFCKQKSYNPRTGMESLTVTPCSKASANQRAGRAGRVAAGKCFRLYTAWAYQHELEETTVPEIQRTSLGNVVLLLKSLGIHDLMHFDFLDPPPYETLLLALEQLYALGALNHLGELTTSGRKMAELPVDPMLSKMILASEKYSCSEEILTVAAMLSVNNSIFYRPKDKVVHADNARVNFFLPGGDHLVLLNVYTQWAESGYSSQWCYENFVQFRSMRRARDVREQLEGLLERVEVGLSSCQGDYIRVRKAITAGYFYHTARLTRSGYRTVKQQQTVFIHPNSSLFEQQPRWLLYHELVLTTKEFMRQVLEIESSWLLEVAPHYYKAKELEDPHAKKMPKKIGKTREELG
Protein: RNA-binding protein 5 variant (E1CJT4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSDKRVSRTERSGRYGSIIDRDDRDERESRSRRRDSDYKRSSDDRRGDRYDDYRDYDSPERERERRNSDRSEDGYHSDGDYGEHDYRHDISDERESKTIMLRGLPITITESDIREMMESFEGPQPADVRLMKRKTGESLLSS
Protein: TATA box-binding protein-associated factor, RNA polymerase III, subunit 2 (Q54U85)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- TATA-box-binding protein
- Myb domain-containing protein
- Transcription factor IIIC-gamma subunit
- DNA-directed RNA polymerase III subunit rpc6
- DNA-directed RNA polymerase III subunit rpc1
- DNA-directed RNA polymerase III subunit rpc2
- DNA-directed RNA polymerases I, II, and III subunit rpabc4
- DNA-directed RNA polymerases I and III subunit rpac1
- DNA-directed RNA polymerase III subunit rpc9
- DNA-directed RNA polymerase III subunit rpc3
Sequence:
MSKNCGNCGNDSFASSNEGSVVCTACGTVKESANIVSEVQFGGDSSIVGTFVSATRKPSSYRSLGGRDSRAMSVENARKKLDQIGNSLRIRSHLIDSAQRTFELAMENNFTKGRQTRLVAAACLYIVCRRERTPHLLIDFSENLQVNVFIVAGTFLQLIKLLNIQLPIVDPSFFIQRFASALEFGDQTKDVIATANKLVARMKRDWMSIGRKPSGICGASLYIASKIHGFKRSMKEIVHVVKIGEQTLINRLDEFRKTPTATLRFDEFNGMDLEDQCDPPSFTRARLKEKKEEEKLKLLEEKKERKRLKKEKKKLLELENNKDNKEIIIKENKEEIEKKLEKKQDLKKDKKDKIKGGEGEEEEEEEEDDDDDDEEEEEDNLNEETKGDNKKNKKRKRELLKDDDDIEKESNDIVKGSQNVQSIKDITNVDSIPTTLLENIEKFEKIQSDIKTLAQKVKNEMDEKIKESQSQEPDTTPPPSSTTTTQTTTTTTTSQNNESSAPIDLPTPINKTMDSVVSYPTITSTIDQSVFAPNDELENLSDEELDFYLEHDKDTVKKKEEIWVELNKEWIEKNEERQREIEEDIKAGRPPRKRKAPVSKKSAENAQAAAEEELKKRTRNAKLVEKLGLFKPNFVTMGLFGGAGASNNQAAVGAMLSTDGTSKNTSINPKETNKEDDDDDDYEPIQPIQSGSLLSRNFNNYEEDDY
Protein: H-2 class II histocompatibility antigen, I-A beta chain (P18468)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVWLPRVPCVAAVILLLTVLSPPVALVRDSRPWFLEYCKSECHFYNGTQRVRFLKRYFYNLEENLRFDSDVGEFRAVTELGRPDAENWNSQPEILDEKRAAVDTYCRHNYEIFDNFLVPRRVEPTVTVYPTKTQPLEHHNLLVCSVSDFYPGNIEVRWFRNGKEEKTGIVSTGLVRNGDWTFQTLVMLETVPQSGEVYTCQVEHPSLTDPVTVEWKAQSTSAQNKMLSGVGGFVLGLLFLRAGLFIYFRNQKGQSGLQPTGLLS
Protein: Protein FAM53C (Q9NYF3)
Organism: Homo sapiens (Human)
Interaction partners:
- Dual specificity tyrosine-phosphorylation-regulated kinase 1A
- Dual specificity tyrosine-phosphorylation-regulated kinase 1B
- DDB1- and CUL4-associated factor 7
Sequence:
MITLITEQLQKQTLDELKCTRFSISLPLPDHADISNCGNSFQLVSEGASWRGLPHCSCAEFQDSLNFSYHPSGLSLHLRPPSRGNSPKEQPFSQVLRPEPPDPEKLPVPPAPPSKRHCRSLSVPVDLSRWQPVWRPAPSKLWTPIKHRGSGGGGGPQVPHQSPPKRVSSLRFLQAPSASSQCAPAHRPYSPPFFSLALAQDSSRPCAASPQSGSWESDAESLSPCPPQRRFSLSPSLGPQASRFLPSARSSPASSPELPWRPRGLRNLPRSRSQPCDLDARKTGVKRRHEEDPRRLRPSLDFDKMNQKPYSGGLCLQETAREGSSISPPWFMACSPPPLSASCSPTGGSSQVLSESEEEEEGAVRWGRQALSKRTLCQRDFGDLDLNLIEEN
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q38DM0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase
- Pre-mRNA-splicing factor SLU7
- RNA helicase
- MI domain-containing protein
- ATP-dependent DEAD/H RNA helicase, putative
- peptidylprolyl isomerase
- RNA-binding protein, putative
- Peptidyl-prolyl cis-trans isomerase
- Pre-mRNA splicing factor, putative
- Splicing factor YJU2
Sequence:
MSVVISTSLGSLLINLRFVDCPKASFNFLALCASSYYDGCRFHRLVPETFVLTGDPTGTGKGGESVFVHHQDIKQRYFEDEGMGNALHDRRGVVSMAHKGNKPDTNASQFFILFKPCPSLDSKHTAFGVVDFGWNDGESERTLKRVEELEADGSYNVLDVEARILSTTVLYNPFAEGHIKLNV
Protein: Dynein axonemal assembly factor 5 (HEAT repeat-containing protein 2 homolog) (Q8INF7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cytoplasmic protein involved in the delivery of the dynein machinery to the motile cilium. It is required for the assembly of the axonemal dynein inner and outer arms, two structures attached to the peripheral outer doublet A microtubule of the axoneme, that play a crucial role in cilium motility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25232951}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q86Y56}. Note=Observed only in the cytoplasm of ciliated cells and absent from cilia. {ECO:0000269|PubMed:25232951}.
Interaction partners:
- Zinc finger MYND domain-containing protein 10 homolog
- Spag1 axonemal dynein assembly factor
- Dynein, axonemal, intermediate chain 2, isoform C
- GH13165p
- Putative inner dynein arm light chain, axonemal
- Radial spoke head protein 9 homolog
- Dynein axonemal assembly factor 3 homolog
- Forkhead domain 3F, isoform D
- Cilia- and flagella-associated protein 298
- Protein tilB
Sequence:
MGFDIDSQKICSDLESSDRRLKTTVLDELLDKCKEATNSESADKIADVFDKLYLHLLKCYEDRFESVRSKAIQVVSAFLSSLPPTDFHLMNVVSTLAERMGKAETVEPSEEIRLLYIAQLNLMICLYEKMENVGVFRECYPLVVKILIKSIKDDYPVVQREGCSAVVTLSRLADTQEFRPFTESILLPLYTMLNHKHAQARISAIQAIARLSLHMDASGDAMRRLFNEVSPLLMDTMPLVRREVGQMGILMLMELLDRYSFFERILPLVLCCLKDESPEVLNHIYPQWLKCGIQYFNENEAELSQQEISDLPVENYPKDVKRPTIGCRGLVQRSLRLLQLITRETSDWKDNVRLHALKLLYQFVLHAEAAMTAKFFEIYGDLAHACIDHVAEVNAEAAKVADLMGRLLSYDAWIDHGFDGLERNARESYMRCFYHMFTASLGGTYEQLMRLAKLLRCTDYSHTLKPGFQHYILKLLNTIVDKTLKINAGQNELEDLYESVYVCAIKVMALSSSLENVGDEDVNFGQTLIEKMVKLLNTSVPKIHERWFHLALQDVINLDAALEDNAEPVMLLNGLINMCHIRATYVHDLIEKVKIVFQHCCDSAQVKIFSSLSLATLFWSKTMNVERESSTQMLSEFVSQIVEPYLTWKAGSNAEAMRSLAMATLCALAQGAESESVEVLPSLAKYMPSLLEDRNVTTRHYAIKAVVYFREMSVEDLKPLAYATMQRMDDPSAGIRILAALAMGKLKPKFAETDTEENYEKEVWDAIVKRAMDLLLLYHESPEKDMRAAVAVTLKVLAKSHPEAWEERYQRALPMAQKKDLLTELYDKLTINEDSHTEVTSASQD
Protein: F-box/WD repeat-containing protein 2 (F-box and WD-40 domain-containing protein 2) (Protein MD6) (Q9UKT8)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- Sperm protein associated with the nucleus on the X chromosome N3
- Dynactin subunit 5
- F-box/WD repeat-containing protein 4
- F-box/WD repeat-containing protein 1A
- F-box/WD repeat-containing protein 7
- F-box only protein 17
- Chorion-specific transcription factor GCMa
Sequence:
MERKDFETWLDNISVTFLSLTDLQKNETLDHLISLSGAVQLRHLSNNLETLLKRDFLKLLPLELSFYLLKWLDPQTLLTCCLVSKQWNKVISACTEVWQTACKNLGWQIDDSVQDALHWKKVYLKAILRMKQLEDHEAFETSSLIGHSARVYALYYKDGLLCTGSDDLSAKLWDVSTGQCVYGIQTHTCAAVKFDEQKLVTGSFDNTVACWEWSSGARTQHFRGHTGAVFSVDYNDELDILVSGSADFTVKVWALSAGTCLNTLTGHTEWVTKVVLQKCKVKSLLHSPGDYILLSADKYEIKIWPIGREINCKCLKTLSVSEDRSICLQPRLHFDGKYIVCSSALGLYQWDFASYDILRVIKTPEIANLALLGFGDIFALLFDNRYLYIMDLRTESLISRWPLPEYRKSKRGSSFLAGEASWLNGLDGHNDTGLVFATSMPDHSIHLVLWKEHG
Protein: Retinal dehydrogenase 2 (EC 1.2.1.36) (Retinaldehyde dehydrogenase type 2) (Q90XS8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTSSEVELPGEVKNDPAALMASLHLMPSPVPNPEIKYTKIFINNEWHDSVSGKVFPTYNPATGEKICDVQEADKADVDKAVQAARSAFSLGSVWRKMDASERGKLLFKLADLVERDSAYLATLESLDSGKPFLPCFFVDLQGIIKTFRYYAGWADKIHGSTIPIDGEFFTLTRHEPIGVCGQIIPWNFPLVMTAWKLGPALSCGNTVVLKPAEQTPLTCLYLGALIKEAGFPPGVVNILPGYGPTAGAAISSHMGIDKVAFTGSTEVGKLIQEAAGKSNLKRVTLELGGKSPNIIFADADFELALEQAHQGVFFNNGQCCTAGSRIFVEEPIYDEFVRRSVERAQRRKVGNPFDPTTEHGPQVSEEQQRRVLELIQSGITEGAKLECGGKAPATKGFFVEPTVFSNVKDHMRIAKEEIFGPVQQIMKFKTIEEVIERANNTEYGLAAAVFTRDISKAMTISAAVQAGTVWINCYNAMSCQCPFGGFKMSGNGRELGEIGLKEYTELKTITMKMSGKTS
Protein: Peroxisomal biogenesis factor 19 (Peroxin-19) (Peroxisomal farnesylated protein) (Q9QYU1)
Organism: Rattus norvegicus (Rat)
Function: Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P40855}. Peroxisome membrane {ECO:0000250|UniProtKB:P40855}; Lipid-anchor {ECO:0000250|UniProtKB:P40855}; Cytoplasmic side {ECO:0000250|UniProtKB:P40855}. Note=Mainly cytoplasmic, some fraction membrane-associated to the outer surface of peroxisomes. {ECO:0000250|UniProtKB:P40855}.
Interaction partners:
- Peroxisomal biogenesis factor 3
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein PEX16
- Peroxisomal membrane protein PEX14
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Peroxisomal biogenesis factor 11 beta
- ATP-binding cassette sub-family D member 3
- Peroxisomal membrane protein 11A
- Similar to peroxisome biogenesis factor 26.
Sequence:
MAAAEGGCGAGVEADRELEELLESALDDFDKAKPSPAPSPTISAPDASGPQKRSPGDTAKDALFASQEKFFQELFDSELASQATAEFEKAMKELAEEEPHLVEQFQKLSEAAGRVGSDASSQQEFTSCLKETLSGLAKNATDLQNSGMSEEELTKAMEGLGMDEGDGEGNILPIMQSLMQNLLSKDVLYPSLKEITEKYPEWLQSHQESIPPEQFEKYQQQHSVMGKICEQFEAETPTDSEATHRARFEAVLDLMQQLQDLGHPPKELAGEMPPGLNFDLDALNLSGPPGANGEQCLIM
Protein: Immunoglobulin kappa variable 3-11 (Ig kappa chain V-III region VG) (P04433)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MEAPAQLLFLLLLWLPDTTGEIVLTQSPATLSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWP
Protein: Snaclec jerdonibitin subunit beta (TJ-GPIb-bp subunit beta) (D1MGU1)
Organism: Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii)
Function: Snaclec that dose-dependently inhibits platelet aggregation induced by ristocetin or low-dose thrombin, but not by high-dose thrombin. Binds to GPIbalpha (GP1BA). In vivo, also dose-dependently induces thrombocytopenia of mice and platelet counts remains at very low level even after 18 hours intravenous injection.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MGRFIFVSFGLLVVFLSLSGTGADCPSDWSSYEGHCYRVFQQQMNWADAEKFCTQQRKESHLVSFESSEEVDFVVSKTFPILKENFVWIGLSNVWNGCRLQWSDGTELKYNAWSAESECIASKTTDNQWWSMDCSKTYPFVCKLIV
Protein: Probable chromatin modification-related protein eaf7 (O42924)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Chromatin modification-related protein eaf3
- SWR1-complex protein 4
- Enhancer of polycomb-like protein 1
- Protein AF-9 homolog
- NuA4 acetyltransferase complex subunit Tra2
- Chromatin modification-related protein eaf6
- Chromatin modification-related protein png1
- Histone acetyltransferase mst1
- Actin-related protein 4
- Chromatin modification-related protein vid21
Sequence:
MSSRGTRSSTAAEQKRQEDVNKESNMNDSVTEWSVLEETLLLKAICRGLRPVGIEKNFYMIGILREIRDGCKRSTIKAQDVWNKLGTLYNLKEFEELEAPGNEEVKAKEKRIKSPDVKDFKLPKDILKVKEKSEKPLETSQKVEIETVETKPGEPEVKQETNLQKEKKESKVKLESKEEKISRNLRSSSRSISPVTEQPQSPKIQPVIPEKKEKSEKKESSMTLRKRSVSPSSQNTARSPKRMATEPIEPASSPAASNQAIRRSSRSRRPPT
Protein: Transforming acidic coiled-coil-containing protein 3 (Cytoplasmic polyadenylation element-binding protein-associated factor Maskin) (CPEB-associated factor Maskin) (Q9PTG8)
Organism: Xenopus laevis (African clawed frog)
Function: Maternal RNA in oocytes remains in a dormant state as masking outcompetes eif4g to bind eif4e, thereby preventing translation. During oocyte maturation this complex dissolves and eif4g binds eif4e to allow translation of maternal RNAs. Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome (By similarity). Involved in microtubule assembly during M-phase. Involved in spindle pole assembly by recruiting and regulating ckap5 at the spindle pole leading to microtubule elongation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10635326}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:25262927}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:25262927}.
Interaction partners:
Sequence:
MSLQIINDENAGNDITAEKFDLLLNPQTTGRPSILRPSQKDNLPPKPALKSTKVTFQTPMRDPQTLRIMTPSVANKPENVFLLEDCTQALEQLHLSLPSSCGPNPVEINVSVSNNQPDSEELPVRTTGAYSIDFDNFDDINPFKSKTQMLNSPIKADLPSLTENIETTTPVVPADEASKQMVSLNLSAANLDSPVTVQFSSESGSIGVSEKTALDDTLPLSESGIKDLQGLNASSNNIEEPVPLDKDICSNNEKDDATMADSTCEGTSDAHTSSNNIEEPVTLDKDICSSNEKDNAAVADSTCEGTSDAQSPLPIPKSSYSFDPDQFDMMNPFKTGGSKLQNSPAGKKQTPPSADLNTAKTEPVKLEFNFGDGDVSERKPPPKKLGKRPLLKTAAKKPSPKPEIASEKQEQQTAKPSEDEAIVPKASYKFDWEKFDDPNFNPFGCGGSKISSSPKGQKIANEQPSACTQGSKPEAECTASDMAPAENADEKDHGEIEPSQDSGAAEDRSQAEDQSVALSKVEVPHEQTTDCSPVENETQPEVSLINEEPSQKEVEHTSSDMTPPEINGTDSEFKLATEADFLLAADMDFKPASEIFSEGFRQPVEIDYLENFGTNSFKESVLRKQSLYLKFDPLLRESPKKSAAGINLLPSVPLKCSSDLFGAIPEANFPLIPSIENEEKPKGLDLLGTFTVADTALLIVDAPSSVAVPNPFLSTSDAIVEMLKYSQKDMDAAIEAVRLEVQEKDLEVLEWKTKHEKLYLEYVEMGKIIAEFEGTITQILEDSQRQKETAKLELNKVLQEKQQVQVDLNSMETSFSELFKRLEKQKEALEGYRKNEEALKKCVEDYLVRIKKEEQRYQALKAHAEEKLNRANEEIAHVRSKAKSEATALQATLRKEQMKIQSLERSLEQKSKENDELTKICDDFILKMEKI
Protein: Zinc transporter ZIP10 (Solute carrier family 39 member 10) (Zrt- and Irt-like protein 10) (ZIP-10) (Q6PEH9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May act as a zinc-influx transporter.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9ULF5}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q9ULF5}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Solute carrier family 30
- Solute carrier family 30 member 1b
- Zinc transporter ZIP1
- Zinc transporter ZIP9
- Proton-coupled zinc antiporter SLC30A5
- Solute carrier family 30
- Probable proton-coupled zinc antiporter SLC30A3
- Zinc transporter 6
- Prion protein a.
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
Sequence:
MMRVHTHTRLCFLCVLTLLYHQCSHCHEGGSHHHHGHNHGDHDHIHSDLQISEMSCNGLSDRLVHGSQGEPAENEQRYYIHQLFCRYGQKDRLDFKGFQSLLLSLGLGEVRVVGLEHEDLGHDHVAHLDILEVQDGRHSHSAGHPHSHQNPNISHKTHQHSHHENEEHTLAEDVPCSKTLGTGATPPSVSEEHDHDHEHDHDHDKDSDHEHNHRHVTDSPQTQDHEHDHIHLHTHSHKQDSDVTQRLELDHDQKSREHAQEHNDLSDQNHHHHDHHHHKHPHPHLHAPESVVHTTSAMPKIQPSVPPELPANQTRRHRRPSKVKAHRGRNRTSVTVTQAVELETSGDDHEHSLQDHSPAQQQRGRREVPGSPAHGVLHQHEECLNLTQLLHQYGLSSDSLISPVQFTYLCPALLYQIDRRFCILHYHHVEAEEQVAPSSGWVWMWGFVSITIISLLSLLGVVLVPILNQSCFKFLLTFLVALAVGTLSGDALLHLLPHSQGDHDHNHGEQMEEEPEVDFLIKFDGVWKGLTALAGIYLLFIIEHCIGMFKHYSDQRGGLCHKKKKGEQAKIGRKLSDHKLNRRSDAEWLHLKPLTEGDGTTCEAGHNDTQMTELQPLDSPSKMPLNISDSDHPYEAPVKTEEDNVPKAKSKKHGHGHGHGHGHGHGHSHHGHCHSDQEMKDAGIASIAWMVIMGDGMHNFSDGLAIGAAFSANITGGISTSVAVFCHELPHELGDFAVLLKAGMSVKQAIVYNLLSALMAYAGMVIGTAVGQYTHNVTSWIFAVTAGMFLYVALVDMLPEMLHGDSEEHKRCEMGHFVLQNFGMLTGFGIMLLIAIFEDHIVLDFGF
Protein: Carabin (TBC1 domain family member 10C) (Q8C9V1)
Organism: Mus musculus (Mouse)
Function: Inhibits the Ras signaling pathway through its intrinsic Ras GTPase-activating protein (GAP) activity. Acts as a negative feedback inhibitor of the calcineurin signaling pathway that also mediates crosstalk between calcineurin and Ras (By similarity).
Interaction partners:
- TBC1 domain family member 21
- TBC1 domain family member 13
Sequence:
MAQALGEDLLSELQDDSSSLGSDSELSGPSPYRQADRYGFIGGNSGELRLCQPSADLIRQREMKWVEMTLHWEKTMSRRYKKVKIQCRKGIPSALRARCWPLLCGARMCQKNNPGTYQELAAAPGDPQWMETIGRDLHRQFPLHEMFVSPQGHGQQGLLQVLKAYTLYRPEQGYCQAQGPVAAVLLMHLPPEEAFWCLVQICEVYLPGYYGPHMEAVQLDAEVFMALLRRQLPRVYKHLQQVGVGPLLYLPEWFLCLFTRSLPFPTVLRIWDAFLSEGAKVLFRVGLTLMRLALGTVEQRTACPGLLETLGALRAIPPTQLQEEVFMSQVHSVTLSERVLQQEIRIQLAQLSKSLPGPAPLPQARLPGAQAIFESQQLAGVRESTKPEIPRIVVQPPEEPKPPRRKPQTRGKTFHGLLIRARGPPIEGPSRSQRGSASFLDTRF
Protein: Fatty acid-binding protein 9 (Testis lipid-binding protein) (TLBP) (Testis-type fatty acid-binding protein) (T-FABP) (Q0Z7S8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MVEPFLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVKSTITLENGSMIHVQKWLGKETTIKRKIVDEKMVVECKMNNIVSTRIYEKV
Protein: Integrin beta (A0A087WXP3)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}.
Interaction partners:
Sequence:
MGIELLCLFFLFLGRNDHVQGGAQTLQVHVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVIPNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNNGTLFQHQKKCSHMKVGDTASFSVTVNIPHCERRSRHIIIKPVGLGDALELLVSPECNCDCQKEVEVNSSKCHHGNGSFQCGVCACHPGHMGPRCECGEDMLSTDSCKEAPDHPSCSGRGDCYCGQCICHLSPYGNIYGPYCQCDNFSCVRHKGLLCGGNGDCDCGECVCRSGWTGEYCNCTTSTDSCVSEDGVLCSGRGDCVCGKCVCTNPGASGPTCERCPTCGDPCNSKRSCIECHLSAAGQAREECVDKCKLAGATISEEEDFSKDGSVSCSLQGENECLITFLITTDNEGKTIIHSINEKDCPKPPNIPMIMLGVSLAILLIGVVLLCIWKLLVSFHDRKEVAKFEAERSKAKWQTGTNPLYRGSTSTFKNVTYKHREKQKVDLSTDC
Protein: 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) (Q6FIM1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Gluconokinase
- Glucose-6-phosphate 1-dehydrogenase
- Ribulose-phosphate 3-epimerase
- Ribose-5-phosphate isomerase
- 6-phosphogluconolactonase-like protein
- 6-phosphogluconolactonase-like protein
- 6-phosphogluconolactonase-like protein
- Transketolase
- Transaldolase
- Transaldolase
Sequence:
MSADFGLIGLAVMGQNLILNIADHGYTVVAYNRSVDKVHQFLDNEAKGKSIIGAESIEDLVAKLKRPRKIMMLVKAGAPVDGLIAQLVPHLEKGDIIIDGGNSHFPDSNRRYEELKAKGILFVGSGVSGGEDGARYGPSLMPGGAEEAWPHIKEIFQSISAKSDGEPCCDWVGPAGSGHYVKMVHNGIEYGDMQLICEAYDIMKRIGGFTDKEISEVFGKWDTGVLDSFLVEITTNILKKDDVDGKPLVEKIMDSAGQKGTGKWTAINALDLGMPVSLIGEAVFARCLSALKCERVKASKTLPGPEIPKDLIKDRQQFIDDLEQALYASKIISYAQGFMLIREAAKTYGWKLNNPAIALMWRGGCIIRSVFLGEITKAYRENPDLENLLFHKFFKDAVTKAQGGWRRSLALAATYGIPSPAFATALSFYDGYRSERLPANLLQAQRDYFGAHTFRVLPECASDSLPKDKDIHINWTGHGGNVSSTTYDA