wanglab/gogpt-training-data huggingface dataset:
Protein: Transforming growth factor-beta-induced protein ig-h3 (A0A8I5ZSM4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAVFPLSRPQCGLTAGYLSNTVALVSSPNVCAVQKVIGTNKKYFTNCKQWYQRKICGKSTVISYECCPGYEKVPGEKGCPAALPLSNLYETLGIVGSTTTQLYTDRTEKLRPEMEGPGSFTIFAPSNEAWSSLPAEVLDSLVSNVNIELLNALRYHMVDRRVLTDELKHGMALTSMYQNSNIQIHHYPNGIVTVNCARLLKADHHATNGVVHLIDKVISTVTNNIQQIIEIEDTFETLRAAVAASGLNTVLEGDGQFTLLAPTNEAFEKIPAETLNRILGDPEALRDLLNNHILKTAMCAEAIVAGMAMETLGGTTLEVGCSGDMLTINGKAVISNKDILATNGVIHFIDELLIPDSAKTLLELASESDVSTAIDLLRQAGLSTHLSGKEQLTFLAPLNSVFKDGVPRIDGQMKTLLLNHMVKGQLASKYLYSGQTLDTLGGKKLRVFVYRNSLCIENSCIAAHDKKGRYGTLFTMDRMLTPPMGTVMDVLKGDNRFSMLVAAIQSAGLMETLNREGVYTVFAPTNEAFQAMPPEELNKLLANAKELTNILKYHIGDEILVSGGIGALVRLKSLQGDKLEVSSKNNVVSVNKEPVAETDIMATNGVVYAINTVLQPPANRPQERGEELADSALEIFKKASAYSRSAQSSMRLAPVYQRLLERMKRRG
Protein: TOM1-like protein 1 (Q9LFL3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Might contribute to the loading of the ESCRT machinery.
Subcellular location: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- HAT transposon superfamily
- HAT transposon superfamily
- HAT transposon superfamily
- DEAD-box ATP-dependent RNA helicase 40
- AT3g13990/MDC16_11)
- Actin family protein
- Spc97 / Spc98 family of spindle pole body
Sequence:
MGDNLMDKVTAFGERLKIGGSEVSNKISAGVSSMSFKVKELFQGPNPTDKIVEDATTENLEEPDWDMNLEICDMINQETINSVELIRGIKKRIMMKQPRIQYLALVLLETCVKNCEKAFSEVAAERVLDEMVKLIDDPQTVVNNRNKALMLIEAWGESTSELRYLPVFEETYKSLKARGIRFPGRDNESLAPIFTPARSTPAPELNADLPQHVHEPAHIQYDVPVRSFTAEQTKEAFDIARNSIELLSTVLSSSPQHDALQDDLTTTLVQQCRQSQTTVQRIIETAGENEALLFEALNVNDELVKTLSKYEEMNKPSAPLTSHEPAMIPVAEEPDDSPIHGREESLVRKSSGVRGGFHGGGGSGDDMMDDLDEMIFGKKNGCDSSTNPDHDPKKEQSSSKNDDLIRF
Protein: PHD finger protein 10 (BRG1-associated factor 45a) (BAF45a) (Q9D8M7)
Organism: Mus musculus (Mouse)
Function: Involved in transcription activity regulation by chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- AT-rich interactive domain-containing protein 2
- Bromodomain-containing protein 7
- Actin-like protein 6A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- Protein polybromo-1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF complex subunit SMARCC1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF complex subunit SMARCC2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
Sequence:
MTAAGPGAAPSPGRCDSDPASPGAQSPKDDNEDNSNDGTHPCKRRRMGSGDSSRSCETSSQDLSFSYYPAENLIEYKWPPDETGEYYMLQEQVSEYLGVTSFKRKYPDLERRDLSHKEKLYLRELNVITETQCTLGLTALRSDEVIDLMIKEYPAKHAEYSVILQEKERQRITDHYKEYSQMQQQSTQKVEASKVPEYIKKAAKKAAEFNSNLNRERMEERRAYFDLQTHVIQVPQGKYKVLPTDRTKVSSYPVALIPGQFQEYYKRYSPDELRYLPLNTALYEPPLDPELPALDSDGDSDDGEDGGGDEKRKNKGTSDSSSGNVSEGDSPPDSQEDTFHGRQKSKDKMATPRKDGSKRSVLSKSAPGYKPKVIPNALCGICLKGKESNKKGKAESLIHCSQCDNSGHPSCLDMTMELVSMIKTYPWQCMECKTCIICGQPHHEEEMMFCDVCDRGYHTFCVGLGAIPSGRWICDCCQRAPPTPRKVGRRGKNSKEG
Protein: Pirin (EC 1.13.11.24) (Probable quercetin 2,3-dioxygenase PIR) (Probable quercetinase) (Q9D711)
Organism: Mus musculus (Mouse)
Function: Transcriptional coregulator of NF-kappa-B which facilitates binding of NF-kappa-B proteins to target kappa-B genes in a redox-state-dependent manner. May be required for efficient terminal myeloid maturation of hematopoietic cells. Has quercetin 2,3-dioxygenase activity (in vitro).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O00625}. Cytoplasm {ECO:0000250|UniProtKB:O00625}. Note=Predominantly localized in dot-like subnuclear structures. {ECO:0000250|UniProtKB:O00625}.
Interaction partners:
- B-cell lymphoma 3 protein homolog
- Piwi-like protein 2
- Piwi-like protein 4
- Cardiotrophin-1
Sequence:
MASSKKVTLSVLSREQSEGVGARVRRSIGRPELKNLDPFLLFDEFKGGKPGGFPDHPHRGFETVSYLLEGGSMAHEDFCGHVGKMNPGDLQWMTAGRGILHAEMPCSEEPAHGLQLWVNLRRSEKMVAPQYQELKSEEIPKPTKDGVTVAVISGEALGIKSKVYTRTPTLYLDFKLDQGAKHSQPIPKGWTSFIYTISGDVYIGPDDAQQKIEPHHTAVLGEGDAVQLENKDPKRSHFVLIAGEPLREPVVQHGPFVMNTNEEISQAILDFRNAKNGFEGARTWKSKIGN
Protein: Zinc finger protein 64 (Zfp-64) (Q99KE8)
Organism: Mus musculus (Mouse)
Function: May be involved in the regulation of mesenchymal cell differentiation through transactivation of NOTCH1 target genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:18430783}.
Interaction partners:
Sequence:
MNASVEGDTFSGSMQIPGGTTVLVELAPDIHICGLCKQHFSNLDAFVAHKQSGCQLTTTPVTAPSTVQFVAEETEPATQTTTTTISSETQTITVSAPEFVFEHGYQTYLPTESTDNQTATVISLPTKSRTKKPTAPPAQKRLGCCYPGCQFKTAYGMKDMERHLKIHTGDKPHKCEVCGKCFSRKDKLKTHMRCHTGVKPYKCKTCDYAAADSSSLNKHLRIHSDERPFKCQICPYASRNSSQLTVHLRSHTASVLENDVQKPAGLPAEESDAQQAPAVTLSLEAKERTATLGERTFNCRYPGCHFKTVHGMKDLDRHLRIHTGDKPHKCEFCDKCFSRKDNLTMHMRCHTSVKPHKCHLCDYAAVDSSSLKKHLRIHSDERPYKCQLCPYASRNSSQLTVHLRSHTGDTPFQCWLCSAKFKISSDLKRHMIVHSGEKPFKCEFCDVRCTMKANLKSHIRIKHTFKCLHCAFQGRDRADLLEHSRLHQADHPEKCPECSYSCSNPAALRVHSRVHCTDRPFKCDFCSFDTKRPSSLAKHIDKVHREGAKTENRAPPGKDGPGESGPHHVPNVSTQRAFGCDKCGASFVRDDSLRCHRKQHSDWGENKNSNLVTFPSEGIATGQLGPLVSVGQLESTLEPSHDL
Protein: Tuberous sclerosis 1 isoform A (X5D9D2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAQQANVGELLAMLDSPMLGVRDDVTAVFKENLNSDRGPMLVNTLVDYYLETSSQPALHILTTLQEPHDKHLLDRINEYVGKAATRLSILSLLGHVIRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCLKKPGHVAEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENLETFEEVVKPMMEHVRIHPELVTGSKDHELDPRRWKRLETHDVVIECAKISLDPTEASYEDGYSVSHQISARFPHRSADVTTSPYADTQNSYGCATSTPYSTSRLMLLNMPGQLPQTLSSPSTRLITEPPQATLWSPSMVCGMTTPPTSPGNVPPDLSHPYSKVFGTTAGGKGTPLGTPATSPPPAPLCHSDDYVHISLPQATVTPPRKEERMDSARPCLHRQHHLLNDRGSEEPPGSKGSVTLSDLPGFLGDLASEEDSIEKDKEEAAISRELSEITTAEAEPVVPRGGFDSPFYRDSLPGSQRKTHSAASSSQGASVNPEPLHSSLDKLGPDTPKQAFTPIDLPCGSADESPAGDRECQTSLETSIFTPSPCKIPPPTRVGFGSGQPPPYDHLFEVALPKTAHHFVIRKTEELLKKAKGNTEEDGVPSTSPMEVLDRLIQQGADAHSKELNKLPLPSKSVDWTHFGGSPPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEKDGLLKKLEEEKAEAAEAAEERLDCCNDGCSDSMVGHNEEASGHNGETKTPRPSSARGSSGSRGGGGSSSSSSELSTPEKPPHQRAGPFSSRWETTMGEASASIPTTVGSLPSSKSFLGMKARELFRNKSESQCDEDGMTSSLSESLKTELGKDLGVEAKIPLNLDGPHPSPPTPDSVGQLHIMDYNETHHEHS
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (Q9VZU7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin carboxyl-terminal hydrolase 7
- Polyubiquitin
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin carboxyl-terminal hydrolase
- GH17761p
- Ubiquitin carboxyl-terminal hydrolase 16/45
- Ubiquitin carboxyl-terminal hydrolase 39
- Beclin-1-like protein
- E3 ubiquitin-protein ligase sina
Sequence:
MEELRKHLSKVNVPCASGAGSPPIYKDECVYSYDNPETPTGLYVCLHSFLGFGEAYVREYADKTGNRVFLHIQRVKTIKEGADMEAECAESEAGPERKITRLAIGVEGGYNESDMAKKYEIKDTYSIVVAPHLDKKLPYPDPELPMRVTQSVEAILAADSAIAKLEKATLMGTWDGEVRQASKYADNLQQLDNGKRIPPSGWQCEKCDLTNNLWLNLTDGSIMCGRKFFDGSGGNDHAVEHYRVTGFPLAVKLGTITADGKSDVFSYPEDEMVLDPHLERHLSHFGINMAAMKKSEKSMVELELDINQRIGEWTALTESESELQPVAGPGYTGMRNLGNSCYINSVMQVLFVIPDFQQRFVGTGAERYFKEFPSDPANDFNIQMAKLGTGLQSGKYSSIAENTLDTDHSTGISPAMFKNIVGKNHPDFSTKQQQDANDFYLHLLTLLDRNSRNQTNPADALKFLLEDRVECLASHKVKYNTREEYSFRLPVPLDKATNLDEVREFQERKKAARETGQRLPDRDIVRHKVPLQACLERFFGPELIEQFYSTAIGSKTNARKITRLATMPDCLMIHVGKFTLGDDWVPKKLDVSVDMPDELDLSNWRSAGGLQPGEEALPEPATEEVKFAFDEAVMSELLTMGFPPEACKRACYHTKNSGLEAASNWLMEHIADEDISEPFVVPNNSIGDCAANQFVANPESLAMLMSMGFDERQAVAALKATDGNVERATDWIFSHADSIGVEDAAPAANSSAAAASSTPNKTNYRDGRGKYRLVAFISHMGTSAQVGHYVCHIRKKGEWVIFNDSKVAKSQNPPKDLGYLYLYMREQ
Protein: Early growth response protein 1 (EGR-1) (Zinc finger protein ZENK) (O73692)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Function: Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (By similarity). Binds double-stranded target DNA, irrespective of the cytosine methylation status (By similarity). Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia. Plays a role in the regulation of cell survival, proliferation and cell death. Mediates responses to ischemia and hypoxia; regulates the expression of proteins that are involved in inflammatory processes (By similarity). Plays a role in regulating the expression of circadian clock genes (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P18146}. Cytoplasm {ECO:0000250|UniProtKB:P18146}.
Interaction partners:
Sequence:
CDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKVEKAASVSTTSSPVAAYSSSVATSYSSSIATTYPSPVRTVYSSPASSSYPSPAHTAFPSPSIATTYPSGTATFQTQVATSFPSPAVTNNFSSQVTSALSDMTSTFSPRTIEIC
Protein: Myocardin-related transcription factor B (MRTF-B) (MKL/myocardin-like protein 2) (Megakaryoblastic leukemia 2) (Q9ULH7)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional coactivator of serum response factor (SRF). Required for skeletal myogenic differentiation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Serum response factor
- Phosphatase and actin regulator 1
- Actin, alpha skeletal muscle
- Transforming protein RhoA
- RNA-binding protein 15
Sequence:
MIDSSKKQQQGFPEILTAGDFEPLKEKECLEGSNQKSLKEVLQLRLQQRRTREQLVDQGIMPPLKSPAAFHEQIKSLERARTENFLKHKIRSRPDRSELVRMHILEETFAEPSLQATQMKLKRARLADDLNEKIAQRPGPMELVEKNILPVDSSVKEAIIGVGKEDYPHTQGDFSFDEDSSDALSPDQPASQESQGSAASPSEPKVSESPSPVTTNTPAQFASVSPTVPEFLKTPPTADQPPPRPAAPVLPTNTVSSAKPGPALVKQSHPKNPNDKHRSKKCKDPKPRVKKLKYHQYIPPDQKGEKNEPQMDSNYARLLQQQQLFLQLQILSQQKQHYNYQTILPAPFKPLNDKNSNSGNSALNNATPNTPRQNTSTPVRKPGPLPSSLDDLKVSELKTELKLRGLPVSGTKPDLIERLKPYQEVNSSGLAAGGIVAVSSSAIVTSNPEVTVALPVTTLHNTVTSSVSTLKAELPPTGTSNATRVENVHSPLPISPSPSEQSSLSTDDTNMADTFTEIMTMMSPSQFLSSSPLRMTNNEDSLSPTSSTLSNLELDAAEKDRKLQEKEKQIEELKRKLEQEQKLVEVLKMQLEVEKRGQQQRPLEAQPSAPGHSVKSDQKHGSLGSSIKDEASLPDCSSSRQPIPVASHAVGQPVSTGGQTLVAKKAVVIKQEVPVGQAEQQSVVSQFYVSSQGQPPPAVVAQPQALLTTQTAQLLLPVSIQGSSVTSVQLPVGSLKLQTSPQAGMQTQPQIATAAQIPTAALASGLAPTVPQTQDTFPQHVLSQPQQVRKVFTNSASSNTVLPYQRHPAPAVQQPFINKASNSVLQSRNAPLPSLQNGPNTPNKPSSPPPPQQFVVQHSLFGSPVAKTKDPPRYEEAIKQTRSTQAPLPEISNAHSQQMDDLFDILIKSGEISLPIKEEPSPISKMRPVTASITTMPVNTVVSRPPPQVQMAPPVSLEPMGSLSASLENQLEAFLDGTLPSANEIPPLQSSSEDREPFSLIEDLQNDLLSHSGMLDHSHSPMETSETQFAAGTPCLSLDLSDSNLDNMEWLDITMPNSSSGLTPLSTTAPSMFSADFLDPQDLPLPWD
Protein: Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase (Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase) (EC 2.4.1.265) (Asparagine-linked glycosylation protein 8 homolog) (Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase) (Protein xiantuan) (Q9W3V8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol (By similarity). Functions in developmental processes such as germband extension, the apical constriction of mesoderm precursor cells and ventral furrow formation in early embryogenesis prior to gastrulation. Involved in the glycosylation and intracellular distribution of shg (E-cadherin). Function in cell intercalation in the lateral epidermis during germband extension may be due to its effect on shg.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24681004}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P40351}.
Interaction partners:
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dol-P-Glc:Glc
- Uncharacterized protein
- FI08810p
- Dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase Alg3
Sequence:
MKDLFWHLVGIATGLKILLIPAYHSTDFEVHRNWLAITHSLPLNQWYVDATSEWTLDYPPFFAYFEWLLSQVAKYVDPRMLVVDNLNYESKATVYFQRLSVIVTDLVYVLGVRSCLGSLGLGRDTQQFFAASMLLLLNVGLIFVDHIHFQYNGLLFGILLLSIGSLIRQRFLWSAFAFAVLLNFKHIFLYMAPAFGVYLLRFYCLEQASVVSAVGAVVKLLVVGLTPFAVSFGPFWQQLPQVLSRLFPFKRGLTHAYWAPNFWALYNAADKLAAGVLKVQDGGASTTSGLVQEVRHSVLPAITPPVTFALTALFMLPILVKLFRSAKKQSPLVFLRAVVLCGCSSFVFGWHVHEKAILMVLLPLCLLTLVNREDARYAYVLGIAGYFSLFPLLFDADLYIPRYSLYMSYVAMMYGQLYRIFPGFRGFHTLEWLYMLGFMAIPLYEHLLSFLLHLDQRLPFLPLLLTSVYSALGVLYFFGAYYLYALGISWGKVPIASSTSAAAVKRKRKTK
Protein: Exocrine gland secreted peptide 38 (A0A3B2W3Y6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
METHIQSSGKAMASFPLMYFFIILVFPTILPEGRALKRTEEEPHISADLKVDFEIPVCQSKINDINVMLMSRVSDQGGVLFLPFRFVLHTC
Protein: Gustatory receptor for sugar taste 64b (P83294)
Organism: Drosophila melanogaster (Fruit fly)
Function: One of the few identified sugar gustatory receptors identified so far and which promotes the starvation-induced increase of feeding motivation.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MPQGETFHRAVSNVLFISQIYGLLPVSNVRALDVADIRFRWCSPRILYSLLIGILNLSEFGAVINYVIKVTINFHTSSTLSLYIVCLLEHLFFWRLAIQWPRIMRTWHGVEQLFLRVPYRFYGEYRIKRRIYIVFTIVMSSALVEHCLLLGNSFHLSNMERTQCKINVTYFESIYKWERPHLYMILPYHFWMLPILEWVNQTIAYPRSFTDCFIMCIGIGLAARFHQLYRRIAAVHRKVMPAVFWTEVREHYLALKRLVHLLDAAIAPLVLLAFGNNMSFICFQLFNSFKNIGVDFLVMLAFWYSLGFAVVRTLLTIFVASSINDYERKIVTALRDVPSRAWSIEVQRFSEQLGNDTTALSGSGFFYLTRSLVLAMGTTIITYELMISDVINQGSIRQKTQYCREY
Protein: PR domain zinc finger protein 8 (EC 2.1.1.-) (PR domain-containing protein 8) (Q8BZ97)
Organism: Mus musculus (Mouse)
Function: Probable histone methyltransferase, preferentially acting on 'Lys-9' of histone H3. Histone methyltransferase activity has not been confirmed in other species. Involved in the control of steroidogenesis through transcriptional repression of steroidogenesis marker genes such as CYP17A1 and LHCGR. Forms with BHLHE22 a transcriptional repressor complex controlling genes involved in neural development and neuronal differentiation. In the retina, it is required for rod bipolar and type 2 OFF-cone bipolar cell survival.
Subcellular location: Nucleus {ECO:0000269|PubMed:19646955}.
Interaction partners:
- Class E basic helix-loop-helix protein 22
Sequence:
MEDSGIQRGIWDGDAKAVQQCLTDIFTSVYTTCDIPENAIFGPCVLSHTSLYDSIAFVALKSTDKRTVPYIFRVDTSAANGSSEGLMWLRLVQSARDKEEQNLEAYIKNGQLFYRSLRRIAKDEELLVWYGKELTELLLLCPSRAHKMNGSSPYTCLECSQRFQFEFPYVAHLRFRCPKRLHSTDANPQDEQGGGLGTKDHGGGGGGKEQQQQQQQQQQEAPLIPGPKFCKAGPIHHYPASSPEASNPPGSAGAGSAKPSTDFHNLARELENSRGSSSCVAAPGVGSGGSGHQEAELSPDGVATGGCKGKRRFPEEAAAEGGGAGLAGGRARFSERPLATSKEELVCTPQQYRAAGSYFGLEENGRLFAPPSPETGEAKRSAFVEVKKAGRAVGLQEEAAATDGAGGTAEDPDAGGGVAGGGSNGSSTPAAGSPGAPEKLLAPRPGGSLPGRLEGGSPARGSAFTSVSQLGGGGGAGTAGTAGGSGGGQTAASDERKSAFSQPARSFSQLSPLVLGQKLGALEPCHPGDGVGPTRLYPAAADPLAVKLQGAADLNGACGPLASGGGGGLPKQSPFLYATAFWPKSSAAAAAAAAAAAGPLQLQLPSALTLLPPSFTSLCLPAQNWCAKCNASFRMTSDLVYHMRSHHKKEYAMEPLVKRRREEKLKCPICNESFRERHHLSRHMTSHN
Protein: Transglycosylase (EC 4.2.2.n1) (Protein P7) (P27380)
Organism: Enterobacteria phage PRD1 (Bacteriophage PRD1)
Function: Component of the phage ejection machinery which acts as an exolysin. Muralytic protein involved in host peptidoglycan digestion necessary for viral DNA entry into the host cell.
Subcellular location: [Isoform Transglycosylase P7]: Virion membrane {ECO:0000269|PubMed:11741849}; Single-pass membrane protein {ECO:0000269|PubMed:11741849}. Note=Part of the capsid inner membrane. Approximately 20 copies per virion. {ECO:0000303|PubMed:10931330}.; SUBCELLULAR LOCATION: [Isoform Protein P14]: Virion membrane {ECO:0000269|PubMed:11741849}; Single-pass membrane protein {ECO:0000305}. Note=Approximately 20 copies per virion. {ECO:0000303|PubMed:10931330}.
Interaction partners:
Sequence:
MSGALQWWETIGAASAQYNLDPRLVAGVVQTESSGNPRTTSGVGAMGLMQLMPATAKSLGVTNAYDPTQNIYGGAALLRENLDRYGDVNTALLAYHGGTNQANWGAKTKSYPGKVMKNINLLFGNSGPVVTPAAGIAPVSGAQEMTAVNISDYTAPDLTGLTMGAGSPDFTGGASGSWGEENIPWYRVDKHVANAAGSAYDAVTDAVSAPVEAAGNYALRGVVIIAAVAIVVVGLYFLFQDEINSAAMKMIPAGKAAGAAAKALA
Protein: malate dehydrogenase (EC 1.1.1.37) (Q38BZ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Citrate synthase
- fumarate hydratase
- Aspartate aminotransferase
- fumarate hydratase
- Malic enzyme
- Malic enzyme
- aspartate transaminase
- phosphoenolpyruvate carboxykinase
- Malate dehydrogenase
- NAD-specific glutamate dehydrogenase
Sequence:
MVIFFGRAQTRRVTGKVVVFGATTNVGKHLSLLLTLSPQVKELCCFDPLNDVTLRMTETRVRGIVKDLSHIDTGVVLRAVDDPQQWEPAMRNAQLVLICTGSIPNPSRLQRDLALAECAPEYLVAMELVARAAPHAIVGIASGPVNSLVPLAREVLLRHSAFDPRKLFGITSRDVMRTRVLFAKELHMNPYDVNVHVVGGKGDATVCPLITQTGFQLPHQRMVQLCEEVQRPENFTAGDHNSTGCRVDSQNVQGQEKFTCPTLSTANAAYEWVTSIMKAQRGDRGITECSFVESSIKRETPFFSSRVELGEEGAAQLLPLGALTPYEEELVAAAVPLIVEDVEAGLRLSKTGVDAVS
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (Q57V97)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- non-specific serine/threonine protein kinase
Sequence:
MPPKNRNRAATADSAAIASSGAKLINNPKSNSSGVKGKNNNKSAPVAAKARRQSEADDFERVLADLNRATAAVGKEREKQVKREKPRKERHEDVRALAQKPEGIDEEFSMMLRKKQQQKQFQQLIQQLLAARSPFLDAPEKEVRCEVATENPNFDVAVGEMQGWRVSMEDKHAIDVTFPSGAKDSKEGFFCVFDGHSGDGCAKKCSELIPKVSRAHMVEHTDGFMEIDFEAAYMEVDTLLEKELTDQSGCTAVTVHITPTRITCASVGDSRAVLCRNGIAVALSEDHKPDREAERARIEEAGGHVAENRVNGQLAMSRAMGDFTYKTQKERGPRQQLVIAVPDVVMVNREADDGFVVLACDGIFDVMSNDELIKAVLIRKAENKPNSVICEEICHECLAPPAEEGKYAPRPEGTDNMTIMIVDLK
Protein: MKIAA0345 protein (Q6ZQD4)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
KYLRNFGSAREQPNIRKGLAMVFSQREDRHLLLWLLLFAAWEAGSGQLHYSVPEEAKHGTFVGRIAQDLGLELAELVPRLFRVASKDRGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVEVEVRDINDNPPVFPVATKNLFIYESRPLGSRFSLEGASDADIGTNSLLSYSLNSSEYFSLDVKRKDEEIKSLGLVLKKLLNREDIPEHNLLITAVDGGKPELTGTTQVKITVLDVNDNAPAFEKTFYKVRLPENAPNGTVVVDVDASDLDEGVNKDIVYSFHQDMSLEILSKFHLDPISGYITVKGNIDFEETKSFEIQIEAADKGTPPMTDHCTVLVEIVDVNDNVPELVIKSLSLPVLENSAPSTVIALISVSDRDSGANGQVTCSLTPQVPFKLVSTFKNYYSLVLDSVLDRETISNYNVVVTARDGGSPPLCTTASVSVEVADVNDNAPAFAQPEYTVFVKENNPPGAHIFTVSAMDADAQENALVSYSLVERRVGERLLSSYVSVHAESGKVFALQPLDHEELELLQFQVSARDAGVPALGSNVTLQVFVLDENDNAPTLLGPHAGSAVSELVSRTVGAGHVVTKVRAVDADSGYNAWLSYELQSAAGSGRLPFRVGLYTGEISTTRVLDETDAPRQRLLVLVKDHGEPVLTATATLLVSLVESGHTPNTPSRTLVDSAGREASLVDINVYLIIAICAVSSLLVLTLLLYLALRCSTAPTEGGPGKPMLVCSSAVGTWSYSQQRRQRVCSGEGPPKTDLMAFSPSLTPCPVNQDKEDKLVGDIDFSIKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
Protein: Bone marrow stromal antigen 2 (BST-2) (Protein DAMP-1) (CD antigen CD317) (Q811A2)
Organism: Rattus norvegicus (Rat)
Function: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV), filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and rhabdoviridae: vesicular stomatitis virus (VSV). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection (By similarity). Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells.
Subcellular location: Golgi apparatus, trans-Golgi network. Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchor, GPI-anchor. Late endosome {ECO:0000250}. Membrane raft. Cytoplasm {ECO:0000250}. Apical cell membrane. Note=Shuttles between the cell membrane, where it is present predominantly in membrane/lipid rafts, and the trans-Golgi network. Forms a complex with MMP14 and localizes to the cytoplasm (By similarity). {ECO:0000250}.
Interaction partners:
- Sialic acid binding Ig-like lectin H
- Ubiquitin-like protein ISG15
Sequence:
MAPSFYHYLPVAMDERWEPKGWSIRRWWLVAAILVVLIGVVLVCLIVYFANAAHSEACKNGLRLQDECRNTTHLLKHQLTRAQDSLLQTEMQANSCNQTVMDLRDSLKKKVSQTQEQQARIKELENKIERLNQELENLRTQKEISTTVQVNSGGSVVVSSLLVLVAVLFLHF
Protein: Biofilm-associated surface protein (Q79LN3)
Organism: Staphylococcus aureus
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004168}; Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00004168}.
Interaction partners:
Sequence:
MGNKQGFLPNKLNKYSIRKFTVGTASLLVGTTLFFGIGSEAQAAELDTITKEDVKSQDKGEALDIKNIKESEKDVTTEDDNNAEVQNSAQTVDKSENSNDTAVESTNDSVKTDETKETSENKSAQDDDNIKEDSNTQEESTNTSSQSSEVPQTKKDTNETSETAIDEDASTKEQNNKDNDTAQDDDNIKEDSNTQEESTNTSSQSSEVPQTKKEQPDKSSNSIKEPDKQQEEVAKEEKAITEIADKNKELELKNNKTDKNEESELESNLSSSENKKDTVESFLNSQLSDSETKKIMENANIDYDKATDEEINTEILRASLIEMANNKKKTETLATPQRTMFRAMATPTALRAAVNQDEELQKSLGYTDNYTFASMLFDPGKLDSDDALNSNIIPFDLHSYMSGANSGNRYKIDLKLDPIIAEHVTKISANPSGSNKPVEFVRNKDENGNLTDTWEVNFIRANDGLFGGAEILSQYTAKNGKIELDDTVGNIISNAGNLSNNKLNHQVFVRDSRENKIVRTSESSGYFLTKADDDLVNLENNVSTENNNAFKASSGSATYNENVGEFGGILIDQQIMKNGIFSYSKTKANQWAYNYQIDKDLLPYIEGVELHQYDYKGLNGFDKNYDAKNKVADLTIDEVGNGTITSDNLNKLIEFNNALPETVGVRVVLKLNKSVNNILTKDAKYDSEGNLIRETTKQKEDFTFAGYLTDSKGALINNTLGTSTLALQDYDKDGLLDRYERQLSLSDAENEDTDGDGKNDGDEVVNYKTSPLVGKPQAADITTEDTVVSGSVPLKEGAATQTAKVINAEGTTVGTATVNSDGTFSVSIPNSPEGTYTIAIDSPNYDNDEVNTFEIVDNSKLPAPSINPVDDNDQQIVVNGTSGSTVTVTDSNNNVLGTVTIPADDTSAAINVDTPLEAGTVLTSTASKDGKTSDVSDQITVTDATAPDAPTLDEVNTDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSEPSSANVTDTTAPDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSEPSSANVTDTTAPDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSEPSSANVTDTTAPDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSEPSSANVTDTTAPDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSEPSSANVTDTTAPDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSEPSSANVTDTTAPDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSEPSSANVTDTTAPDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNGDLNGGEELQVTATDKDGNTSEPSSANVTDTTASDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSEPSSANVTDTTAPDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSEPKLTNVTDTTASDAPTVNDVTSDASQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSEPSSANVTDTTAPDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNGDLNGGEKLQVTATDKDGNTSEPSSANVTDTTAPDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSEPSSANVTDTTAPDAPTVNDVTSDATQVTGQAEPNSTVKLTFPDGTTATGTADDQGNYTIDIPSNVDLNGGEELQVTATDKDGNTSESTNTTIIDSDDNSDNGNNSGAGDTSDSDDNSGNGDNSGAGDNSDSDDNSDNGNNSGAGDNSDSDDNSDNEDNSSSNKDSINQDSNVNSNDSKHDKQNELPETGEKEVRNGTLFGTLFAGLGSLLLFTKRRRKENDKK