wanglab/gogpt-training-data huggingface dataset:
Protein: Granzyme H (EC 3.4.21.-) (CCP-X) (Cathepsin G-like 2) (CTSGL2) (Cytotoxic T-lymphocyte proteinase) (Cytotoxic serine protease C) (CSP-C) (P20718)
Organism: Homo sapiens (Human)
Function: Cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3' and P4' sites. Probably necessary for target cell lysis in cell-mediated immune responses. Participates in the antiviral response via direct cleavage of several proteins essential for viral replication.
Subcellular location: Cytolytic granule {ECO:0000269|PubMed:23269243}.
Interaction partners:
- Protein NKG7
- Granulysin
- Perforin-1
- Fibroblast growth factor-binding protein 2
- T-cell surface glycoprotein CD8 alpha chain
- Granzyme K
- Granzyme A
- Natural killer cells antigen CD94
- C-C motif chemokine 5
- Tissue-resident T-cell transcription regulator protein ZNF683
Sequence:
MQPFLLLLAFLLTPGAGTEEIIGGHEAKPHSRPYMAFVQFLQEKSRKRCGGILVRKDFVLTAAHCQGSSINVTLGAHNIKEQERTQQFIPVKRPIPHPAYNPKNFSNDIMLLQLERKAKWTTAVRPLRLPSSKAQVKPGQLCSVAGWGYVSMSTLATTLQEVLLTVQKDCQCERLFHGNYSRATEICVGDPKKTQTGFKGDSGGPLVCKDVAQGILSYGNKKGTPPGVYIKVSHFLPWIKRTMKRL
Protein: Polycomb complex protein BMI-1-B (Polycomb group RING finger protein 4-B) (Q7T3E6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of rnf2 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase RING2
- Chromobox homolog 8b.
- Polyhomeotic-like protein 2
- Chromobox homolog 7b.
- Polyhomeotic homolog 2b
- Neuronal pentraxin receptor a.
- Chromobox homolog 6b
- Chromobox homolog 4
- Chromobox homolog 6a
- Chromobox homolog 2
Sequence:
MHRTTRIKITELNPHLMCVLCGGYFIDATTIVECLHSFCKMCIVRYLETSKYCPICDVQVHKTKPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAEHPVDATNGSNEDRGEVSDEDKRIIADDEIISLSIEFFDQKKLDGKDGEEKESTKEVTVKRYLQCPAAMTVMHLRKFLRSKMDIPCTFQIEVMYEDEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPGCKKIKLSSPRNDMSGGRRPDTESDSSSDKPNSPSIVAAPSTSSSMPSPNTPVQSTHPSFPHISTINGVSAKVGHNGQTPFSSKVCKTSHNGSNSLG
Protein: Epoxide hydrolase (EC 3.3.2.9) (Q7JRC3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|PIRNR:PIRNR001112}. Microsome membrane {ECO:0000256|ARBA:ARBA00004111}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004111}.
Interaction partners:
- Carboxylic ester hydrolase
- Juvenile hormone acid O-methyltransferase
- Epoxide hydrolase
- Epoxide hydrolase
- Carboxylic ester hydrolase
- RH17287p
- GH01837p)
Sequence:
MGVTVKILVLILAIAGGLVYRNVTQLWADLPAPKLDPQEWWGDEAQPKDYEAYLKNNSEVIGNRLSYPDKTIADLKERLNRTLRLTPPLEGVAFEYGFNTNYLKEVVEYWRDDYLPRWREREVFLWQFNHFTTDIQGLRTHFLHLMVYDDNKVGKKHYPVLLLHGWPGSVREFYDFIHLLHQTNLDNNNKYIFNVVVPSLPGYGWSQGTSRKGLGPAQVAVMMRNLMLRLGYNKFFIQGGDWGSIIGSNIATLYPENVLGYHSNMCNNLSPKSLAKGLVAEFWPSLFVPSGFEDFFFPKSNEMRYLMEESGYFHIQATKPDTIGAALTDNPVGLAAYILEKFSTWTNPSYRSLPDGGLTKRYKMDALLDNLMIYYLTNSITTSQRLYAEQYAQAQRDLHLDRVPTRVPTGCARFKSDIMQFLDVQLKDKYTNLVHSTYHKKGGHFAALEVPKVLYKDFIDFVETVERKFKIKTL
Protein: creatine kinase (EC 2.7.3.2) (Q804Z2)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Interaction partners:
- Guanidinoacetate N-methyltransferase
Sequence:
MPFGNTHNNFKLNFSAAEEYPDLTKHNNHMAKVLTKEVYAKLRDKQTPTGFTLDDAIQTGVDNPGHPFIMTVGCVAGDEESYEVFKELFDPVICDRHGGYKPTDKHKTDLNFENLKGGDDLDPNYVLSSRVRTGRSIKGYALPPHNSRAERRAVEKLSVEALNSLDGEFKGKYYPLKSMSDAEQEQLIADHFLFDKPVSPLLLAAGMARDWPDARGIWHNDEKTFLVWVNEEDHLRVISMQKGGNMKEVFRRFCVGLNKIEEVFKKHNHGFMWNEHLGYILTCPSNLGTGLRGGVHVKLPKLSVHPKFEEILGRLRLQKRGTGGVDTASVGGVFDISNADRIGSSEVEQVQCVVDGVKLMVEMEKKLEKGEAIDSMIPAQK
Protein: Protein TORNADO 2 (Protein EKEKO) (TETRASPANIN-1) (Q9FIQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the basipetal transport of auxin (IAA) that modulates growth and organs organization, as well as cell differentiation. Regulates shoot apical meristem (SAM) organization in the peripheral zone. Required for initial meristematic divisions in the epidermal/lateral root cap leading to the formation of epidermal cells and a clone of lateral root cap cells, as well as for the maintenance of the radial pattern of cell specification in the root, thus regulating the distinction between the lateral root cap and epidermis. Together with WIH peptides, promotes megasporogenesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein TORNADO 1
- Tetraspanin-16
- Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 13
- Homeobox-leucine zipper protein HDG6
- DNA glycosylase/AP lyase ROS1
- Cysteine-rich and transmembrane domain-containing protein WIH2
Sequence:
MPLSNNVIGCINFITVLLSIPVIGAGIWLAIGTVNSCVKLLQWPVIILGVLILLVGLAGFIGGFWRITWLLVVYLIAMLILIVLLGCLVGFIYMVTIRGSGHPEPSRAYLEYSLQDFSGWLRRRVQRSYKWERIRTCLSTTTICPELNQRYTLAQDFFNAHLDPIQSGCCKPPTKCGFTFVNPTYWISPIDMSADMDCLNWSNDQNTLCYTCDSCKAGLLANIKVDWLKADIFLLLALIGLIIVYIIGCCAFRNAETEDIFRKYKQGYT
Protein: CRN (Crooked neck) protein (Crooked neck protein, putative / cell cycle protein) (Q9FNM3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTGKDAEVKLPRTTRVKNKTPAPVQITAEQILREARERQEAEIRPPKQKITDSTELSDYRLRRRKEFEDQIRRARWNIQVWVKYAKWEESQMDYARARSVWERALEGEYRNHTLWVKYAEFEMKNKFVNNARNVWDRSVTLLPRVDQLWEKYIYMEEKLGNVTGARQIFERWMNWSPDQKAWLCFIKFELRYNEIERARSIYERFVLCHPKVSAFIRYAKFEMKRGGQVKLAREVYERAVDKLANDEEAEILFVSFAEFEERCKEVERARFIYKFALDHIRKGRAEELYKKFVAFEKQYGDKEGIEDAIVGKKRFEYEDEVSKNPLNYDSWFDYVRLEESVGNKDRIREIYERAIANVPPAQEKRFWQRYIYLWINYALYEEIETKDVERTRDVYRECLKLIPHTKFSFAKIWLLAAEYEIRQLNLTGARQILGNAIGKAPKVKIFKKYIEMELKLVNIDRCRKLYERFLEWSPENCYAWRNYAEFEISLAETERARAIFELAISQPALDMPELLWKTYIDFEISEGEFEKTRALYERLLDRTKHCKVWISFAKFEASASEHKEDGIKSARVIFDRANTYYKDTTPELEEERATLLEDWLNMETGFGELGDVSVVQSKLPKKLKKRKMTSREDGSTEYEEYFDYLFPEESGTTNLKILEAAYKWKKLKGEECV
Protein: Ethylene-responsive transcription factor ERF024 (Q9SJR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Probable serine/threonine-protein kinase PBL18
- Probable serine/threonine-protein kinase PBL4
Sequence:
MQGTSKDNGGRHPLYRGVRQRKNSNKWVSEIREPRKPNRIWLGTFSTPEMAAIAYDVAALALKGSQAELNFPNSVSSLPAPTSMSPADIQAAAASAAAAFGAARDAIVMANNNSQTSGVACMNSSYDNTNMNGFMDEDLVFDMPNVLMNMAEGMLLSPPRPTVFDAAYDADGFPGGDDYLWNFP
Protein: Transmembrane protein 225 (Q9D9S2)
Organism: Mus musculus (Mouse)
Function: Probably inhibits protein phosphatase 1 (PP1) in sperm via binding to catalytic subunit PPP1CC.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:25605614}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transmembrane protein 270
- Fascin-3
Sequence:
MMHIPNRSIQAANIFFSSGAILLLIVGLIMEDWVELIPKVRKDKTTHSPWLGCCPPFWPEESLEVVRRIMRMTLNISIYLNLIIGLQFSYMISQNKCVHLLVGFLSFFAGCLLFYAIIVYHHKLNKGQYVYFVNYKTKWIAFTVYLTIALFLTCGIFCFIQSTNRCECMKFCIPHTESKSQEMIPSTIEVVSLPPRCAMPRSIVHVHSVTSKDGSLNRPHTQARRVTWAL
Protein: Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)] (P09858)
Organism: Sus scrofa (Pig)
Function: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively.
Subcellular location: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-2]: Secreted {ECO:0000250|UniProtKB:P01137}.
Interaction partners:
- TGF-beta receptor type-2
- TGF-beta receptor type-1
- Latent-transforming growth factor beta-binding protein 1
- Decorin
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-3 proprotein
- Lumican
- Fibromodulin
- Inhibin beta A chain
- Inhibin beta B chain
Sequence:
MHYCVLSAFLLLHLVTVALSLSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPEEVPPEVISIYNSTRDLLQEKASRRAAACERERSDEEYYAKEVYKIDMPPFFPSENAIPPTFYRPYFRIVRFDVSAMEKNASNLVKAEFRVFRLQNPKARVAEQRIELYQILKSKDLTSPTQRYIDSKVVKTRAEGEWLSFDVTDAVHEWLHHKDRNLGFKISLHCPCCTFVPSNNYIIPNKSEELEARFAGIDGTSTYTSGDQKTIKSTRKKNSGKTPHLLLMLLPSYGLESQQSNRRKKRALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCSKTKLAAFARLYHSHSNLGSET
Protein: Poly(A) polymerase alpha (PAP-alpha) (EC 2.7.7.19) (Polynucleotide adenylyltransferase alpha) (P51003)
Organism: Homo sapiens (Human)
Function: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus.
Subcellular location: Cytoplasm. Nucleus. Note=The 90 kDa form is nuclear while the 100 kDa and the 106 kDa forms are both nuclear and cytoplasmic.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 1
- Symplekin
- Zinc finger CCHC domain-containing protein 7
- Exosome RNA helicase MTR4
- Polyadenylate-binding protein 2
- Cleavage and polyadenylation specificity factor subunit 3
- U1 small nuclear ribonucleoprotein 70 kDa
- Cleavage stimulation factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 2
- Pre-mRNA 3'-end-processing factor FIP1
Sequence:
MPFPVTTQGSQQTQPPQKHYGITSPISLAAPKETDCVLTQKLIETLKPFGVFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMVEEFKQGLAITDEILLSKAEWSKLFEAPNFFQKYKHYIVLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPAPKENPDKEEFRTMWVIGLVFKKTENSENLSVDLTYDIQSFTDTVYRQAINSKMFEVDMKIAAMHVKRKQLHQLLPNHVLQKKKKHSTEGVKLTALNDSSLDLSMDSDNSMSVPSPTSATKTSPLNSSGSSQGRNSPAPAVTAASVTNIQATEVSVPQVNSSESSGGTSSESIPQTATQPAISPPPKPTVSRVVSSTRLVNPPPRSSGNAATSGNAATKIPTPIVGVKRTSSPHKEESPKKTKTEEDETSEDANCLALSGHDKTEAKEQLDTETSTTQSETIQTAASLLASQKTSSTDLSDIPALPANPIPVIKNSIKLRLNR
Protein: Angiopoietin-like 3 (Q5I0L8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MHTIKLLLFVVPLVISSRVDPDLSPFDSVPSEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQCFYDLSLQTNEIKEEEKELRRTTSKLQVKNEEVKNMSLELNSKLESLLEEKMALQHRVRALEEQLTSLVQNPPGAREHPEVTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRKTGIQEPTENSLYSKPRAPRTTPPLHLKEAKNIEQDDLPADCSAIYNRGEHTSGVYTIRPSSSQVFNVYCDTQSGTPRTLIQHRKDGSQNFNQTWENYEKGFGRLDGKVISLHHSLIC
Protein: Cytochrome c oxidase subunit 1+2 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide I+II) (O21042)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00401}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00401}.
Interaction partners:
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 5
- NADH-ubiquinone oxidoreductase chain 1
- Probable protoheme IX farnesyltransferase, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase assembly protein
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase assembly protein COX11
- NADH-ubiquinone oxidoreductase chain 4
- Probable cytochrome c oxidase subunit 6B
Sequence:
MKILEIYDKQIAEKEGNIFIFISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWFIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAINFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEVYILILPGFGLVSIILSKYSNKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMNSTRLFGVVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNIFTPYIRRSVNIKNGAIILMGLDFARDWQIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMGRILWRFSYKWSYPTIGDIEIFKNFTAYNQIIHGTVIEIVWTLIPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDNASNLIEFDSYMVYERDLAEGQLRLLEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEYFSKLNEK
Protein: Coatomer subunit zeta-1 (Zeta-1-coat protein) (Zeta-COP 1) (Q940S5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit delta
- Coatomer subunit gamma
- Coatomer subunit epsilon-2
- Coatomer subunit epsilon-1
- Coatomer subunit alpha-2
- Coatomer subunit alpha-1
- Coatomer subunit beta-1
- Coatomer subunit beta-2
- Coatomer subunit beta'-3
- Coatomer subunit beta'-2
Sequence:
MELPPKVKNILLLDSEGKRVAVKYYSDDWPTNSAQEAFEKSVFTKTQKTNARTEVEVTALENNIVVYKFVQDLHFFVTGGEEENELILASVLEGLFDAVTLLLRSNVDKREALDNLDLIFLSFDEIIDGGIVLETDANVIAGKAGINSTDPNAPLSEQTISQALATAREHLTRSLMK
Protein: DNA polymerase epsilon subunit C (DNA polymerase II subunit C) (P27344)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:11024162}.
Interaction partners:
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase epsilon subunit B
- DNA polymerase epsilon subunit D
- DNA polymerase delta small subunit
- DNA polymerase alpha catalytic subunit A
- DNA polymerase delta catalytic subunit
- DNA polymerase zeta catalytic subunit
- DNA polymerase delta subunit 3
- DNA polymerase alpha subunit B
- DNA primase small subunit
Sequence:
MSNLVKEKAPVFPISKVKKIAKCDPEYVITSNVAISATAFAAELFVQNLVEESLVLAQLNSKGKTSLRLSLNSIEECVEKRDNFRFLEDAIKQLKKNSALDKKRELNMQPGRSDQEVVIEEPELHEDDGVEEEEEEDEVSEEEEPVHNEELLDDSKDQQNDKSTRSVASLLSRFQYKSALDVGEHSDSSDIEVDHTKSTDP
Protein: Autophagocytosis associated protein, putative (Q586I8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy-related protein
- Autophagy-related protein
- Autophagy-related protein
- Uncharacterized protein
- Atg6 BARA domain-containing protein
- Uncharacterized protein
- Guanine nucleotide-binding protein subunit beta-like protein
- phosphatidylinositol 3-kinase
- Protein kinase, putative
Sequence:
MNKQSLYEGFKKVYNSVVGVKTTSSFHETGTLTPMEFIQAGDELLHKMPVWSWAEGPENIQPFLPPNKKYLVYRGAPCYERAAVAGNDDADEIVEDDDDEWITTHANRVLKATTEIAAEKTINWDDDDDDDDANNNNNVVVVDSSRKDEGDDDEDADRDQTERRRCRLYDVYMVYDQYYQTPRIFLIGYAEDHVTPLTTSEMMEDVYPVNRERTVSIDPHPFLQAACISIHPCRHAETMRRMIQHMKQRFEESSPETAKFVFPTHMALFLFLKFISSAVPSIEYDLSTGIDI
Protein: Tubulin polyglutamylase ttll-11 (EC 6.-.-.-) (Tubulin--tyrosine ligase-like protein 11) (H2KZM9)
Organism: Caenorhabditis elegans
Function: Polyglutamylase which preferentially modifies tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction. By controlling tubulin glutamylation, regulates ciliary specialization and motor-based transport. Promotes the formation of A and B tubule singlets by splaying microtubule doublets in cilia. Together with ttll-4 and 5, required for male mating.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:20519502, ECO:0000269|PubMed:29129530}. Perikaryon {ECO:0000269|PubMed:29129530}. Cell projection, dendrite {ECO:0000269|PubMed:29129530}. Cell projection, cilium {ECO:0000269|PubMed:20519502}. Extracellular vesicle {ECO:0000269|PubMed:29129530}.
Interaction partners:
- Cytosolic carboxypeptidase 1
- Spastin homolog
- CILiary localization
- Tubulin alpha chain
- Tubulin polyglutamylase ttll-5
- Kinesin-like protein klp-20
- Kinesin-like protein
- Serine/threonine-protein kinase D1044.8
Sequence:
MGCKISTEFCSDNPVGSISTSKVHPTDLSTPSYAIKPVEFYEEPLKDDQLFYKVALAKKEYREKEKDKKEQLSSNRRVSLQVEPNKLPIPLTRSSSLSSIMENRPPSGISNSSFIRSRNTASRRFTIDTSRAKSNQYVVSLCSKKIGIIEYPDGRSDKQPCDVYWHNVVLSDMNKIVTSPQSRVNKFPGMTELAKKISLTHSISSMQKLFPDEYAFYPNSWFLPAHLADFHAFYRKAQALGKTEMWFIVKPDEGAQGTGIYLINSPNQIRNVDQRQLVQEYVADPLLMNDKLKFDFRVYGVIKSINPLSIYVAREGMARFCTEKYEKPDSSNFKNLYAHLTNYSLNKANEAYVHSNTLQDQTRGSKRLLSTVFHQLESRGVKTKRLWHDIKLILVKTTLAMLPEIMLHYEHHFYDSTGPQCFQIMGFDVMIREDGTPILLEVNAAPSLTADHIVPHPGRTLLEGGQRVRSIVDEVIKIPLVRDTLLLVLGLMEEEYQNNSLKGETKSLDDMQTIKQRRKPHLSEIFPTRYGAHSGHLLFLDKAMYIYMQFVQLRSNVNITNAGLKQFVRKCNLIDIIPVVHVDAKVSEINYYFTGEKRTNGNGLPFHAFLMFLFFIAEKKFVLENDLLSKVQRLLSFCDMSLRRYGVRSARLRRAEVDSTIGNVEIYMLPSRMARNRSGTNGRKQNFTDDNNNPNSFAHLPKINERL
Protein: Uncharacterized protein C1A4.04 (O74337)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MESCTRSSLQQLVAADSKSSNFCFRNLSQSSNNNVSYASSSNRNFVPQNVLNNEYQSFQHSSTSQPSVLRQGKNAFLKPSQLSFNMNSSEISNTHWARDFNILTSNFASSSVTSAPTQSSHISNFTNSQKYFANDLPNSLTDQPLAQPSASQRSTWLPCSAAVSTSSPSSDPFFDSYLEQAFEKAERLANEQQKISKVEKTFGTLDSIGTEQDDCFDPDYSNLPLFPQENASPPLFRKASCNSGFTTKC
Protein: Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein) (Nucleoporin-like protein RIP) (Rev-interacting protein) (Rev/Rex activation domain-binding protein) (P52594)
Organism: Homo sapiens (Human)
Function: Required for vesicle docking or fusion during acrosome biogenesis (By similarity). May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication.
Subcellular location: Nucleus {ECO:0000269|PubMed:10613896, ECO:0000269|PubMed:7634337}. Cytoplasmic vesicle {ECO:0000269|PubMed:10613896}.
Interaction partners:
- Vesicle-associated membrane protein 7
- Epidermal growth factor receptor substrate 15
- Rab GDP dissociation inhibitor beta
- Rab GDP dissociation inhibitor alpha
- F-BAR domain only protein 1
- Intersectin-1
- Stonin-2
- Intersectin-2
- Ras-related protein Rab-3A
- Vesicle transport through interaction with t-SNAREs homolog 1B
Sequence:
MAASAKRKQEEKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQIWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYVPPEQAKVVASVHASISGSSASSTSSTPEVKPLKSLLGDSAPTLHLNKGTPSQSPVVGRSQGQQQEKKQFDLLSDLGSDIFAAPAPQSTATANFANFAHFNSHAAQNSANADFANFDAFGQSSGSSNFGGFPTASHSPFQPQTTGGSAASVNANFAHFDNFPKSSSADFGTFNTSQSHQTASAVSKVSTNKAGLQTADKYAALANLDNIFSAGQGGDQGSGFGTTGKAPVGSVVSVPSQSSASSDKYAALAELDSVFSSAATSSNAYTSTSNASSNVFGTVPVVASAQTQPASSSVPAPFGATPSTNPFVAAAGPSVASSTNPFQTNARGATAATFGTASMSMPTGFGTPAPYSLPTSFSGSFQQPAFPAQAAFPQQTAFSQQPNGAGFAAFGQTKPVVTPFGQVAAAGVSSNPFMTGAPTGQFPTGSSSTNPFL
Protein: Pectin lyase B (PLB) (EC 4.2.2.10) (Q5BA61)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Rhamnogalacturonase A
Sequence:
MRLHAPILSLLAAAASTSAAGVTGSAEGFAKGVTGGGSATPVYPSTTAELVSYLGDSSARVIVLTKTFDFTGTEGTTTETGCAPWGTASACQVAINKNDWCTNYQPNAPSVSVTYDNAGVLGITVKSNKSLVGEGSSGVIKGKGLRIVSGASNVIIQNIAITDLNPKYVWGGDAITLDNADMVWIDHVTTARIGRQHLVLGTSASNRVTVSNSYFNGVTSYSATCDGYHYWGIYLTGSNDMVTLKGNYIYHMSGRSPKVGGNTLLHAVNNYWYDSSGHAFEIDSGGYVLAEGNVFQNIPTVIEGTVGGQLFTSPDSSTNAICSTYLGHTCQVNGFGSSGTFKQADTAFLVNFQGKNIASASAYTVAQSSVPSNAGQGKL
Protein: Protein EPIDERMAL PATTERNING FACTOR 1 [Cleaved into: MEPF1] (Q8S8I4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Controls stomatal patterning. Regulates asymmetric cell division during guard cell differentiation. Mediates stomatal development inhibition. Not cleaved by the protease CRSP (AC Q9LNU1). MEPF1: mobile signal controlling stomatal development in a non-cell-autonomous manner. Uses ERL1 as major receptor. May act by competing with somatogen (AC Q9SV72) for the same receptor, TMM (AC Q9SSD1).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- LRR receptor-like serine/threonine-protein kinase ERL1
- LRR receptor-like serine/threonine-protein kinase ERL2
- Protein TOO MANY MOUTHS
- EPIDERMAL PATTERNING FACTOR-like protein 9
- LRR receptor-like serine/threonine-protein kinase ERECTA
- Transcription factor MUTE
- Transcription factor SPEECHLESS
- Transcription factor FAMA
- Subtilisin-like protease SBT1.2
- EPIDERMAL PATTERNING FACTOR-like protein 6
Sequence:
MKSLLLLAFFLSFFFGSLLARHLPTSSHPSHHHVGMTGALKRQRRRPDTVQVAGSRLPDCSHACGSCSPCRLVMVSFVCASVEEAETCPMAYKCMCNNKSYPVP