wanglab/gogpt-training-data huggingface dataset:
Protein: kinetoplast-associated protein 2-2 (Histone H1-like protein p18-2) (Q9TY84)
Organism: Crithidia fasciculata
Function: Histone H1-like DNA-binding protein involved in the organization and segregation of kinetoplast DNA (kDNA). The mitochondrial DNA of kinetoplastid protozoa consists of about 5,000 minicircles and 20 to 30 maxicircles. These circular DNAs are held together by catenation into a highly organized compact disk structure referred to as a kinetoplast DNA (kDNA) network. Binds preferentially to a specific fragment of minicircle DNA and is able to compact kDNA networks through DNA charge neutralization and condensation.
Subcellular location: Mitochondrion matrix, kinetoplast {ECO:0000269|PubMed:8446592, ECO:0000269|PubMed:8552084}.
Interaction partners:
Sequence:
MLRRTVSNFAMSPYMLFISDLAKTGKLKGIRTPGKFVGKKYRQLSAKEKAALQQRAKQASTPAMTAYRRMAHREMSNKSVPIEQRRANLTKKWNETKQAQRAKAQKAQKKPKSAKSKVKKAAKKAKKSKK
Protein: Translin associated factor X (Q5VVQ1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSNKEGSGGFRKRKHDNFPHNQRREGKDVNSSSPVMLAFKSFQQELDARHDKYERLVKLSRDITVESKRTIFLLHRITSSQYLDHSAPDMEDILTESEIKLDGVRQKIFQVAQELSGEDMHQFHRAITTGLQEYVEAVSFQHFIKTRSLISMDEINKQLIFTT
Protein: Nuclear pore complex interacting protein family member B6 (E9PS57)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRLRFWLLIWLLLGFISHQPTPVINSLAVYRHRETDFGVGVRDHPGQHGKTPSPQKLDNLIIIIIGFLRRYTFNILFCTSCLCVSFLKTIFWSRNGHDGSMDVQQRAWRSNRSRQKGLRSICMHTKKRVSSFRGNKIGLKDVITLRRHVETKVRAKIRKRKVTTKINRHDKINGKRKTARKQKMFQRAQELRRRAEDYHKCKIPPSARKPLCNWVRMVAAEHRHSSGLPYWPYLTAETLKNRMGRQPPPPTQQHSITDNSLSLKTPTECLLTPLPPSVDDNIKECPLAPLPPSPLPPSVDDNLKECLFVPLPPSPLPPSVDDNLKTPPLATQEAEVEKPPKPKRWRVDEVEQSPKPKRRRVDEVEQSPKPKRQREAEAQQLPKPKRRRLSKLRTRHCTQAWAIRINP
Protein: Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing] (pDCR) (EC 1.3.1.124) (2,4-dienoyl-CoA reductase 2) (Short chain dehydrogenase/reductase family 17C member 1) (Q9NUI1)
Organism: Homo sapiens (Human)
Function: Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid.
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:Q9Z2M4}.
Interaction partners:
- Peroxisomal multifunctional enzyme type 2
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal targeting signal 1 receptor
- Sterol carrier protein 2
Sequence:
MAQPPPDVEGDDCLPAYRHLFCPDLLRDKVAFITGGGSGIGFRIAEIFMRHGCHTVIASRSLPRVLTAARKLAGATGRRCLPLSMDVRAPPAVMAAVDQALKEFGRIDILINCAAGNFLCPAGALSFNAFKTVMDIDTSGTFNVSRVLYEKFFRDHGGVIVNITATLGNRGQALQVHAGSAKAAVDAMTRHLAVEWGPQNIRVNSLAPGPISGTEGLRRLGGPQASLSTKVTASPLQRLGNKTEIAHSVLYLASPLASYVTGAVLVADGGAWLTFPNGVKGLPDFASFSAKL
Protein: Uncharacterized protein C15F9.01c (Q10098)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MEQIRPFSDNYLDRLRTVEEDDYNDWEGSSDTKTLYSSVSDSKIGHKKSFHKDGKGLFKTLRNFLSLKTNKVPKNRKFSLLKGSKCNNVEIKVFIRNNDKQSNVHNFKGKDSIHEAWSQYLIFDSMGLSPLIHISGEDKYKVLCLFSIWRRKLGKCSIFTVHDPDIQKKIKSILSYLWELSNTNDPPHVIVWHTAKGTNVMTMGPLGLKDEDLWNYANERSNLNGTT
Protein: Spermatogenesis-associated protein 19, mitochondrial (Spermatogenic cell-specific gene 1 protein) (Spergen-1) (Q9DAQ9)
Organism: Mus musculus (Mouse)
Function: Essential for sperm motility and male fertility. Plays an important role in sperm motility by regulating the organization and function of the mitochondria and is also required for correct sperm midpiece assembly.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:15139970}. Mitochondrion {ECO:0000269|PubMed:15139970}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:26265198}. Note=Localizes to the midpiece of the sperm flagellum. {ECO:0000269|PubMed:26265198}.
Interaction partners:
- Outer dense fiber protein 1
- Ornithine decarboxylase antizyme 3
Sequence:
MIITTWIMYIFARKTVGLPFPPRVNSDIEVEESEAVSVVQHWLNKTEEEASRSIREKMSINDSPTHGHDIHVTRDLVKHHLSKSDMLTDPSQEVLEERTRIQFIRWSHTRIFQVPSEVMDDVMQERIDQVRRSVSHLMCDSYNDPSFRTSCSEC
Protein: Transcription termination factor 2, mitochondrial (Mitochondrial transcription termination factor 2) (mTERF2) (Mitochondrial transcription termination factor-like protein) (mTERF-like) (mTERFL) (mTERF domain-containing protein 3, mitochondrial) (Q49AM1)
Organism: Homo sapiens (Human)
Function: Binds mitochondrial DNA and plays a role in the regulation of transcription of mitochondrial mRNA and rRNA species.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16226716}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q8BKY8}.
Interaction partners:
- Transcription termination factor 3, mitochondrial
- Transcription termination factor 4, mitochondrial
Sequence:
MLWKLLLRSQSCRLCSFRKMRSPPKYRPFLACFTYTTDKQSSKENTRTVEKLYKCSVDIRKIRRLKGWVLLEDETYVEEIANILQELGADETAVASILERCPEAIVCSPTAVNTQRKLWQLVCKNEEELIKLIEQFPESFFTIKDQENQKLNVQFFQELGLKNVVISRLLTAAPNVFHNPVEKNKQMVRILQESYLDVGGSEANMKVWLLKLLSQNPFILLNSPTAIKETLEFLQEQGFTSFEILQLLSKLKGFLFQLCPRSIQNSISFSKNAFKCTDHDLKQLVLKCPALLYYSVPVLEERMQGLLREGISIAQIRETPMVLELTPQIVQYRIRKLNSSGYRIKDGHLANLNGSKKEFEANFGKIQAKKVRPLFNPVAPLNVEE
Protein: Cell adhesion molecule 1 (Synaptic cell adhesion molecule) (SynCAM) (Tumor suppressor in lung cancer 1 homolog) (TSLC-1) (Q6AYP5)
Organism: Rattus norvegicus (Rat)
Function: Mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and NECTIN3 in a Ca(2+)-independent manner. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ T-cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM1 in vivo (By similarity). In mast cells, may mediate attachment to and promote communication with nerves (By similarity). CADM1, together with MITF, is essential for development and survival of mast cells in vivo. By interacting with CRTAM and thus promoting the adhesion between CD8+ T-cells and CD8+ dendritic cells, regulates the retention of activated CD8+ T-cell within the draining lymph node. Required for the intestinal retention of intraepithelial CD4+ CD8+ T-cells and, to a lesser extent, intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells. Interaction with CRTAM promotes the adhesion to gut-associated CD103+ dendritic cells, which may facilitate the expression of gut-homing and adhesion molecules on T-cells and the conversion of CD4+ T-cells into CD4+ CD8+ T-cells. Acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly. May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8R5M8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8R5M8}. Synapse {ECO:0000250|UniProtKB:Q8R5M8}. Postsynaptic cell membrane {ECO:0000269|PubMed:27756895}. Note=Localized to the basolateral plasma membrane of epithelial cells in gall bladder. {ECO:0000250|UniProtKB:Q8R5M8}.
Interaction partners:
- Nectin-3
- Cell adhesion molecule 3
- Intercellular adhesion molecule 1
- Cytotoxic and regulatory T cell molecule
- Interleukin-6
- Vascular cell adhesion protein 1
- Neuroligin-1
- Neuroligin-3
- Neuroligin-2
Sequence:
MASPVLPSGSQCAAAAAVAAAAAPPGLRLRLLLLLLSAAALIPTGDGQNLFTKDVTVIEGEVATISCQVNKSDDSVIQLLNPNRQTIYFRDFRPLKDSRFQLLNFSSSELKVSLTNVSISDEGRYFCQLYTDPPQESYTTITVLVPPRNLMIDIQKDTAVEGEEIEVNCTAMASKPATTIRWFKGNKELKGKSEVEEWSDMYTVTSQLMLKVHKEDDGVPVICQVEHPAVTGNLQTQRYLEVQYKPQVQIQMTYPLQGLTREGDAFELTCEATGKPQPVMVTWVRVDDEMPQHAVLSGPNLFINNLNKTDNGTYRCEASNTVGKAHSDYMLYVYDPPTTIPPPTTTTTTTTTTTTTTTILTIITDTTATTEPAVHGLTQLPNSAEELDSEDLSDSRAGEEGAIGAVDHAVIGGVVAVVVFAMLCLLIILGRYFARHKGTYFTHEAKGADDAADADTAIINAEGGQNNSEEKKEYFI
Protein: MICOS complex subunit mic60 (Mitofilin) (O59725)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- MICOS complex subunit mic10
- SAM50-like protein SPAC17C9.06
- Uncharacterized protein C1442.05c
- MICOS complex subunit mic19
- Probable mitochondrial import receptor subunit tom40
- Uncharacterized protein C29A4.17c
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Elongation factor Tu
- Probable mitochondrial import receptor subunit tom70
- Mitophagy receptor atg43
Sequence:
MNRQLRTVKSCFSLQKTHQYRSFWIQSSLRALPPDVKQNKTEPIPFVPKPEEGSSNKSNSSKFRKRFLLLFLLGITGYSCSVVYCFKDPNFYDYFAEHTPFGKQVLYNVEQSWIGYKYLGGNRIKVDDSSPKLKQNSNNISKKQNSSRNDDTKVKKDTTIERPESLVVEIVDLPSEVTKDTAEESVWKDIGLDQETGLSVTAIPIITETLDHAHEQEIKDQSLRFESSLNEANELHGKLSKIQQEQEHLFEQRLREKVSEMESKLEALLIARDEKWQSAFESEKLRLQKLHEARLQQELFKLASVFESKLKNELTEQAITLEKLHLQSIKAQVEQERGSRLGRLQELRNSFQQLQELVRVVLHENGRVTRLVDVSNTLDDLNKDMRFHKLSEVRQHVNTLKEATKDDELAALASRVIEKIVDSGPILDKEELQTKFDTLSKEIYKTCFLTTESGFFGHLKSIILSQLPAAVFKSPDIVSVKKTLEDARSHLLKDDLDGSVRALLSLSQWPRALSRDWINACRRRMELQQAIEIIKASATLSSQLEDAQQA
Protein: Actin-binding LIM protein 1 (A0A8I5Y6A1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPSFLGLRCLEKLCSSEKGKGPSPERASLRGSHGRRLVIEDLSVPETPHPARHRHGTVTYLFYLYSSNRGPPELRFSSCDSSVAHPQDPHHSSEKPVIHCHKCGEPCKGEVLRVQTKHFHIKCFTCKVCGCDLAQGGFFIKNGDYLCTLDYQRMYGTRCHGCGEFVEGEVVTALGKTYHPNCFACTICKRPFPPGDRVTFNGRDCLCQLCAQPMSSSPKEATCSSNCAGCGRDIKNGQALLALDKQWHLGCFKCKSCGKVLTGEYISKDGSPYCEKDYQGLFGVKCEACHQFITGKVLEAGDKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTEEKLRPPNIPRSSSDFFYPKSLIRRTGRSPALQHLSPPCLVNSNQNPRQPTRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYEDKQDRQSLGESPRTLSPTPSAEGFQDGRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPELLSPGVHRWSPLRTSSFSSTHSDTRPNPPFRHHFLPHVKGNEPSSGRNSPLPYRPDSRPLTPTYAQAPKHFHVPDQGINIYRKPPIYKQHAALAAQNKASEDIIKFSKFPAAQAPDPNEIPKIETDHWPGPPSLAAIGTDPRRRSSGREEDEEELLRRRQLQEEQLMKLNSGLGQLILKEEMEKENRERASLLASRYDSPLHSASHAPSSKTSSLPGYGKSGLHRPVSTDFAQYNSYGDVSGGVRDYQTLPDGHMPAMRMDRGVSMPNMLEPKIFPYEMLMVTNRGRNKILRDVDRTRLERHLAPEVFWEIFGMSIQEFDKLPLWRRNDMKKKAKLF
Protein: oxoglutarate dehydrogenase (succinyl-transferring) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase) (C9J4G7)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFHLRTCAAKLRPLTASQTVKTFSQNRPAAARTFQQIRCYSAPVAAEPFLSGTSSNYVEEMYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNVDKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDESDLDKVFHLPTTTFIGGQESALPLREIIRRLE
Protein: Small ubiquitin-related modifier 1 (SUMO-1) (GAP-modifying protein 1) (GMP1) (SMT3 homolog 3) (Sentrin) (Ubiquitin-homology domain protein PIC1) (Ubiquitin-like protein SMT3C) (Smt3C) (Ubiquitin-like protein UBL1) (P63165)
Organism: Homo sapiens (Human)
Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:10574707, ECO:0000269|PubMed:12383504}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000269|PubMed:12383504, ECO:0000269|PubMed:9162015}. Nucleus, PML body {ECO:0000269|PubMed:10574707, ECO:0000269|PubMed:12383504, ECO:0000269|PubMed:22406621}. Cell membrane {ECO:0000269|PubMed:19223394}. Nucleus {ECO:0000269|PubMed:24651376, ECO:0000269|PubMed:9162015}. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (PubMed:24651376). {ECO:0000250|UniProtKB:P63166, ECO:0000269|PubMed:24651376}.
Interaction partners:
- Protein PML
- SUMO-activating enzyme subunit 1
- E3 SUMO-protein ligase RanBP2
- Sentrin-specific protease 1
- E3 SUMO-protein ligase PIAS2
- SUMO-activating enzyme subunit 2
- Death domain-associated protein 6
- SUMO-conjugating enzyme UBC9
- Ran GTPase-activating protein 1
- E3 SUMO-protein ligase PIAS1
Sequence:
MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV
Protein: Undecaprenyl-diphosphatase (EC 3.6.1.27) (Bacitracin resistance protein) (Undecaprenyl pyrophosphate phosphatase) (P9WFF9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01006}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01006}.
Interaction partners:
- Conserved protein
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- Uncharacterized protein
- Conserved protein
- Protein Rv2133c
Sequence:
MTAAPAMSWWQVIVLAAAQGLTEFLPVSSSGHLAIVSRIFFSGDAGASFTAVSQLGTEAAVVIYFARDIVRILSAWLHGLVVKAHRNTDYRLGWYVIIGTIPICILGLFFKDDIRSGVRNLWVVVTALVVFSGVIALAEYVGRQSRHIERLTWRDAVVVGIAQTLALVPGVSRSGSTISAGLFLGLDRELAARFGFLLAIPAVFASGLFSLPDAFHPVTEGMSATGPQLLVATLIAFVLGLTAVAWLLRFLVRHNMYWFVGYRVLVGTGMLVLLATGTVAAT
Protein: Adipocyte enhancer-binding protein 1 (AE-binding protein 1) (Aortic carboxypeptidase-like protein) (Q640N1)
Organism: Mus musculus (Mouse)
Function: As a positive regulator of collagen fibrillogenesis, it is probably involved in the organization and remodeling of the extracellular matrix.
Subcellular location: [Isoform 1]: Secreted {ECO:0000269|PubMed:11438679, ECO:0000269|PubMed:15927179}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:17202411, ECO:0000269|PubMed:9624159}. Nucleus {ECO:0000269|PubMed:17202411}.
Interaction partners:
- Procollagen C-endopeptidase enhancer 1
- Fibromodulin
- Matrix remodeling-associated protein 8
Sequence:
MAPVRTASLLCGLLALLTLCPEGNPQTVLTDDEIEEFLEGFLSELETQSPPREDDVEVQPLPEPTQRPRKSKAGGKQRADVEVPPEKNKDKEKKGKKDKGPKATKPLEGSTRPTKKPKEKPPKATKKPKEKPPKATKKPKEKPPKATKKPKEKPPKATKRPSAGKKFSTVAPLETLDRLLPSPSNPSAQELPQKRDTPFPNAWQGQGEETQVEAKQPRPEPEEETEMPTLDYNDQIEKEDYEDFEYIRRQKQPRPTPSRRRLWPERPEEKTEEPEERKEVEPPLKPLLPPDYGDSYVIPNYDDLDYYFPHPPPQKPDVGQEVDEEKEEMKKPKKEGSSPKEDTEDKWTVEKNKDHKGPRKGEELEEEWAPVEKIKCPPIGMESHRIEDNQIRASSMLRHGLGAQRGRLNMQAGANEDDYYDGAWCAEDESQTQWIEVDTRRTTRFTGVITQGRDSSIHDDFVTTFFVGFSNDSQTWVMYTNGYEEMTFYGNVDKDTPVLSELPEPVVARFIRIYPLTWNGSLCMRLEVLGCPVTPVYSYYAQNEVVTTDSLDFRHHSYKDMRQLMKAVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGDHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLCQEYRDGNPRVRNLVQDTRIHLVPSLNPDGYEVAAQMGSEFGNWALGLWTEEGFDIFEDFPDLNSVLWAAEEKKWVPYRVPNNNLPIPERYLSPDATVSTEVRAIISWMEKNPFVLGANLNGGERLVSYPYDMARTPSQEQLLAEALAAARGEDDDGVSEAQETPDHAIFRWLAISFASAHLTMTEPYRGGCQAQDYTSGMGIVNGAKWNPRSGTFNDFSYLHTNCLELSVYLGCDKFPHESELPREWENNKEALLTFMEQVHRGIKGVVTDEQGIPIANATISVSGINHGVKTASGGDYWRILNPGEYRVTAHAEGYTSSAKICNVDYDIGATQCNFILARSNWKRIREILAMNGNRPILRVDPSRPMTPQQRRMQQRRLQYRLRMREQMRLRRLNSTAGPATSPTPALMPPPSPTPAITLRPWEVLPTTTAGWEESETETYTEVVTEFETEYGTDLEVEEIEEEEEEEEEEMDTGLTFPLTTVETYTVNFGDF
Protein: Interferon gamma (Q30DS9)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
GGPLFSEILKNWKEESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKRLIQIPVD
Protein: Vitellogenin-3 (Vitellogenin III) (Yolk protein 3) (P06607)
Organism: Drosophila melanogaster (Fruit fly)
Function: Vitellogenin is the major yolk protein of eggs where it is used as a food source during embryogenesis.
Subcellular location: Secreted.
Interaction partners:
- Vitellogenin-2
- Vitellogenin-1
- Vitelline membrane protein Vm26Aa
- Vitelline membrane protein Vm34Ca
- MIP10846p1
Sequence:
MMSLRICLLATCLLVAAHASKDASNDRLKPTKWLTATELENVPSLNDITWERLENQPLEQGAKVIEKIYHVGQIKHDLTPSFVPSPSNVPVWIIKSNGQKVECKLNNYVETAKAQPGFGEDEVTIVLTGLPKTSPAQQKAMRRLIQAYVQKYNLQQLQKNAQEQQQQLKSSDYDYTSSEEAADQWKSAKAASGDLIIIDLGSTLTNFKRYAMLDVLNTGAMIGQTLIDLTNKGVPQEIIHLIGQGISAHVAGAAGNKYTAQTGHKLRRITGLDPAKVLSKRPQILGGLSRGDADFVDAIHTSTFAMGTPIRCGDVDFYPNGPSTGVPGSENVIEAVARATRYFAESVRPGSERNFPAVPANSLKQYKEQDGFGKRAYMGLQIDYDLRGDYILEVNAKSPFGQRSPAHKQAAYHGMHHAQN
Protein: Heat shock protein 90-4 (AtHSP90.4) (AtHsp90-4) (Heat shock protein 81-4) (Hsp81-4) (O03986)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Molecular chaperone which stabilizes unfolding protein intermediates and functions as a folding molecular chaperone that assists the non-covalent folding of proteins in an ATP-dependent manner.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Protein SGT1 homolog B
- Protein SGT1 homolog A
- Heat shock 70 kDa protein 1
- Cysteine and histidine-rich domain-containing protein RAR1
- Peptidyl-prolyl cis-trans isomerase CYP40
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 10, mitochondrial
- Co-chaperone protein p23-2
- Co-chaperone protein p23-1
- Heat shock 70 kDa protein 15
Sequence:
MADAETFAFQAEINQLLSLIINTFYSNKEIFLRELISNSSDALDKIRFESLTDKSKLDGQPELFIHIIPDKTNNTLTIIDSGIGMTKADLVNNLGTIARSGTKEFMEALAAGADVSMIGQFGVGFYSAYLVADKVVVTTKHNDDEQYVWESQAGGSFTVTRDTSGEALGRGTKMILYLKEDQMEYIEERRLKDLVKKHSEFISYPISLWIEKTIEKEISDDEEEEEKKDEEGKVEEIDEEKEKEEKKKKKIKEVTHEWDLVNKQKPIWMRKPEEINKEEYAAFYKSLSNDWEEHLAVKHFSVEGQLEFKAILFVPKRAPFDLFDTKKKPNNIKLYVRRVFIMDNCEDIIPDYLGFVKGIVDSEDLPLNISRETLQQNKILKVIRKNLVKKCLELFFEIAENKEDYNKFYEAFSKNLKLGIHEDSQNRTKIAELLRYHSTKSGDELTSLKDYVTRMKEGQNEIFYITGESKKAVENSPFLEKLKKKGYEVLYMVDAIDEYAIGQLKEFEGKKLVSATKEGLKLEETDDEKKKKEELKEKFEGLCKVIKDVLGDKVEKVIVSDRVVDSPCCLVTGEYGWTANMERIMKAQALKDSNTGGYMSSKKTMEINPENSIMDELRKRAEADKNDKSVKDLVLLLFETALLTSGFSLDEPNTFGSRIHRMLKLGLSIEEDDAVEADAEMPPLEDDADAEGSKMEEVD
Protein: SSD domain-containing protein (H2KZH1)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Uncharacterized protein C16C10.8
- Nuclear hormone receptor family member nhr-19
Sequence:
MTAESHIQTKSASHEAVKTTRLVRGISWFFEKWSHFVADHAVALIVICVVLTLIGTFKVATTPNDNDITGYTPYGARARDEFDVMTDFFAHNGNGIAMFVLILPTRHESVLHPDVLREALRLEDILSTNFSMLSADGKPENYQEFCTNFCQINEPFVQFARSYLTELDNSKNGTDLSERISLNYPITSIYSRKMSIQPNFFGIEMMNETKKSITNIRSSKLIALQLRSERKEGWNSNGIKDFEMSITNYLEKEFESPEIRVLTLSTSYVEAEVVRAGMSLLPFLIVGFVIMAIVSSVTTFFSAVYMQQVSIHKFSLAIAACICPFMACGTALGALFFCGVRFGSILCVTPFLVLAIGVDDAYLMIHSWQRVTAERRKHPVANDSPGSRLSEVLVDTGPAILISALTNIFADVAGCFTSSPEISLLGYGNMACIFCDFLYQITFYSAIMTLTGYFEMKDEEQKRHIKKIACGADSDDSSCTSSSVESFDVIVKRRVTSFLENYISLITNAFFQIFVVLVWIAFLVVSIYGITIMNINLSPRKLFMEDSSLREMDDLRVKYVIPNFYLANVFVRKPGDLTDGARLQRLNQFVEEMEHLNGSWGSLGTNYFVRDFVNFQAAMVEEEEAEGGEEEASIVKRGGIDVNNLPMFLEWPEYLFWKGFVQFHSAENRTVLDRFFITFAIHGTNLQSWPARGDALREWRNVVDKYSAEFGLSVFSDDGIYVDLIENMPTDAWQSAVATLACMAFICFVFMYDVPTVMVATSIIASIMTGILGILSLTGTDLDPIVMSALIISIGFSVDIPAHISYHYHTSPSDNGIRHRLHKTLSSVGFPALQATVSTSLCVLSLKFSSIYMSCAFVKTMITCMILCVFHALVLLPCLFAIFHRIHSLFRVPKTSPIESK
Protein: Uncharacterized membrane protein C16E9.09c (O14324)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Endoplasmic reticulum vesicle protein 25
- Endosomal protein P24B
- Uncharacterized membrane protein C17A5.08
- Phospholipid-transporting ATPase neo1
- ER-derived vesicles protein erv14
- Meiotically up-regulated gene 165 protein
- Protein transport protein sec22
- Meiotically up-regulated gene 168 protein
- Meiotically up-regulated gene 123 protein
- Surfeit locus protein 4 homolog
Sequence:
MKLGIFGLLLFTFFFQSQAVHFYFDGSKPKCFLKDMPKGMMVTGIVKAEQWNNEANKWVTSNNIKIRVQVDETFANNHLIYKNDLRSNEAVRFTTTNEGTHRICYLSTSDGAWFSSTKTRLHVDLASDDKYNLIASSEDEAKDLTDRVAALNTRLESILGEQMLQRSREMTFRDTSESANSRVVRWTIVQIVVLLVTCIWQLSHLQRFFVKEKLV
Protein: Poly(A) RNA polymerase protein 2 (EC 2.7.7.19) (DNA polymerase kappa) (DNA polymerase sigma) (Topoisomerase 1-related protein TRF4) (P53632)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of the TRAMP complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Polyadenylates RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. TRF4 is also required for proper nuclear division in mitosis, DNA damage repair and sister chromatid cohesion. Involved in the regulation of histone mRNA levels. May mediate mitotic chromosome condensation.
Subcellular location: Nucleus {ECO:0000269|PubMed:10066793, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein AIR2
- ATP-dependent RNA helicase DOB1
- Protein AIR1
- Protein CAF40
- Protein NRD1
- Poly
- Exosome complex exonuclease RRP6
- Poly
- Probable E3 ubiquitin-protein ligase HUL4
- Nuclear polyadenylated RNA-binding protein 3
Sequence:
MGAKSVTASSSKKIKNRHNGKVKKSKKIKKVRKPQKSISLNDENEVEILPSRNEQETNKLPKDHVTADGILVLEHKSDDDEGFDVYDGHFDNPTDIPSTTEESKTPSLAVHGDEKDLANNDDFISLSASSEDEQAEQEEEREKQELEIKKEKQKEILNTDYPWILNHDHSKQKEISDWLTFEIKDFVAYISPSREEIEIRNQTISTIREAVKQLWPDADLHVFGSYSTDLYLPGSDIDCVVTSELGGKESRNNLYSLASHLKKKNLATEVEVVAKARVPIIKFVEPHSGIHIDVSFERTNGIEAAKLIREWLDDTPGLRELVLIVKQFLHARRLNNVHTGGLGGFSIICLVFSFLHMHPRIITNEIDPKDNLGVLLIEFFELYGKNFGYDDVALGSSDGYPVYFPKSTWSAIQPIKNPFSLAIQDPGDESNNISRGSFNIRDIKKAFAGAFDLLTNRCFELHSATFKDRLGKSILGNVIKYRGKARDFKDERGLVLNKAIIENENYHKKRSRIIHDEDFAEDTVTSTATATTTDDDYEITNPPAKKAKIEEKPESEPAKRNSGETYITVSSEDDDEDGYNPYTL
Protein: Carbohydrate kinase, FGGY family (O53793)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MSRDDVTIGIDIGTTAVKAVAADDNGRVTARVRIGHQLAVPAPDRLEHDADEAWRRGPLAALDRLVGPDTRALAVAAMVPSLTAVDPAGRPITPGLLYGDARGRVPNASVARAQSVPSVGETAEFLRWTAGQALDASGYWPAPAVANYALSGEAVIDYATAVTTLPLFDGTGWNATACADCGVTVDRMPRVETFGVGVGQVRGTGAVLAVGAVDALCEQIVAGADRDGDVLVLCGATLIVWTTISAARQVPGLWTIPHTAPGKSQIGGASNAGGLFLNWVDRVIGPGDPALADPRRVPVWLPYIRGERTPFHEPDRRAVLDGVDLSQDAASVRRAAYEASGFVVRQLIELSGAPVARIVAAGGGTRIQPWMQAIADATGRPVEVSRVAEGAALGAAFLGRLAAGLESSIADAARWASTDRIVEPSADWAGPTKERYRRFLALSGSKLA