wanglab/gogpt-training-data huggingface dataset:
Protein: Non-specific serine/threonine protein kinase (Q57Z70)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLSCAAVQKLERYGQLAQKRKTASDFVNSSLRDAKRSNIHALTHIPTWQACLEELDPDISKGQDKEKDAATVESVQPGGGDVNVTYHGVPSKVTVSESLLYAVSYATALVVRHMDEQRFNLRNENERNGENVSLDGKVFATPLEEAVGLHTLLWKVAEACGRHTKVYMGDSPQMAQALVHLLSSALDAFIVSTMLRHAAVNDTNGEAALLNSLCRSSTGLVMAVVRQLRVMQSKQPFNALYSVRPCPTLLSQYLSKAGAGMSPTKTTGNVKEVKNTECSGPQCSPNCIIRSRSRDVENDSFMTSCLLTWADTVASGSLIASLSYFSTFQKVSFCDAMVSEAPSGCCCTDVGSFRRTLSSLFSTAACNRATRIVVYFRGDDIKLMQNNVRDSTEYSMLTHVTTPPVERSTLSLFTKLPVAEQHHAALLLAGWIASIPFFFRSFCAEESWTVFAQEQRRMVWLRERETRQDRGRRRWGSSSRANSVSSGGKDDSDHASTHSSDGYSRVEVNTDKGDGGDGLTNSHASDRYAGKRMRNSNIDDDEDRCSVVSQLSSFSLMSRASMISTLSKPSIASYREFLSVIDASNTDNGQTHNAPCLHQSEDDNTNLPLILLEEVVLGLQKFLVAVGEAGLSDNLLETTGLRALIWRTIGDLFTFVRNTISFSATNITAKGTPSVFHLGNDLRYNKGLGYEVLGLLFAKVVLPQLLTSCHDVAHETRPVVERALTQCLSTYELIAPQVIDKNVPAILQIASRISKANASSHLGGEKAEAFPTTILHDFLVNLITRLGKGNRISMLLDAIVLQVKEDGNAIYRSKVVEGEDTVVGGTAASSTTVGLREIFSRPDIRAALIEACNVSMDPEHLLLRLLSYVSNWASEEEVNEESGGGDDAATNPEKDEVTALGTEDQKLNVKTTMSRMEPQGVLFILDVVSTVLSGVVPTSISATSILERAAELELALSSFFVNKLHKTFLPVKEQNSREDDKLKKKNEKSSLLLCSAAVIPQKMVHRLVLLTLNAIYSSRTLILSCLQDLGISNLDAYLQLLEESMWCLQQQVDALVGSLTVDDLCASLSITTQMRHAHTTQCPPLIPRFVLQRLMLARSTSMALGFTVGPASSARRLGNTVLSYMLVESEGGVLPDHEADLALSLADTLNEEEWSSLVHFTKPKRVRAAFVWLLQLSFTKSKSAQWLSRCMAACGGLLLEALCEVLVNVDDSELLACRHDMTSKNENDSAGGKGSEDTPLIRLFAALNDVLGRVGHLPQWLPILQNFVHWLMIIYKEERNVQRSMSCLLRQQILQFVLNLLVCEEGVRTLFRWVLLHTQSEENQENHRFEHYRGRKSDRKRDGLNEAFMETVGVQFTVADAMLYASNRYTAEGESCTDAEGIRVAAAKQGIDDCTKLVRRMFSAKFAALLIQQCSTKDSDSGLSLSSRYALGILRQLYTMAMTACRYDTKTAMSSPIAQKFIISVADKMHACLEDGNYAVLSIFLDAMSGTSLTYVLKEGHRDTASTVRVPEKRRRVENSESGDNGEKTRLADKKHHRSAEDIRAKEETVGERKVFEASLGGVDHVEATEDKKESAIVVEGTKLTEVSLRWVDLLRKLLQEVVKGLVEERHQPQSSVPLLHAMSSLYVTLERVRLPALKDASENVNHRGKGGKANKRGRSYERQPVGNGRSLAAVAVASGELSDTAAKLRKLFAPSKSASRRRSASVLLPMLSSCNRAVTRALWVLYAAYEERRQSDLSEDGGFEDTTNHSPSRWFAALLGSFNVHECGNYDNFCSDSTDCLLEEAQEIASQHESECVTLRIVALQRDPAYQTEKATLWLIEQLCIIPEILHTFATSPSQSLLVEYMHALLHASIPLATGACQHLRKLQDRHQKLLTAVAEALHRLSFVPHMRFSIWRNDAKRLLVNAEAAVVSSHDCSKRNDEGTHSLCCRVLQLCTLPLAALHEDEVFIDHEMSFITSLLFTGTSGYRNGSQYLSESVILRIIRLLSATLLPRHVLWQRAHLLPTLLSFLFTRCLDGVSRGYCSSVVLNQLASFLFQLVKDATHGHCHGISPSLKSLCLSSITSCLFRHSAAYIDVFTTHSNDLDYIAADLLKALQHVHLPSRRMQAVPKKFKTEGNETGGDEDEEEEEDAAKQSDATMCDLSYACVGNTDAQLLLRQAAERVEEEEGNGSRHIFLLPE
Protein: Spn43Ac (Q6V6V0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
ELFKEIIKSQSQQNVVFSPFSVHALLALIYGASDGKTFRELQKAGEFSKNAMAVAQDFESVIKYKKHLEGADLTLATKVYYNRELGGVNHSYDEYAKFYFSAGTEAVDMQNAKDTAAKINAWVMDTTRNKIRDLVTPTDVDPQTQALLVNAVYFQGRWEHEFATMDTSPYDFQHTNGRISKVAMMFNDDVYGLAELPELGATALELAYKDSATSMLILLPNETTGLGKMLQQLSRPEFDLNRVAHRLRRQSVAVRLPKFQFEFEQDMTEPLKNLGVHQMFTPNSQVTKLMDQPVRVSKILQKAYINVGEAGTEASAASYAKFVPLSLPPKPTEFVANRPFVFAVRTPASVLLI
Protein: Insulin-like growth factor 2 preproprotein (Q2F6J1)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGITAGKSVLVLLAFLAFASCCYAAYRPSETLCGGELVDTLQFVC
Protein: ATMRK1 (A0A384KC16)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASGGGEADKSLEIGSGTADPKIGGTGSRSAGEERYFRADTLDFSKWDLHMGQTSTSSVLTNSASTSAPAPAMQEWEIDLSKLDMKHVLAHGTYGTVYRGVYAGQEVAVKVLDWGEDGYATPAETTALRASFEQEVAVWQKLDHPNVTKFIGASMGTSDLRIPPAGDTGGRGNGAHPARACCVVVEYVAGGTLKKFLIKKYRAKLPIKDVIQLALDLARGLSYLHSKAIVHRDVKSENMLLQPNKTLKIADFGVARVEAQNPQDMTGETGTLGYMAPEVLEGKPYNRKCDVYSFGVCLWEIYCCDMPYADCSFAEISHAVVHRNLRPEIPKCCPHAVANIMKRCWDPNPDRRPEMEEVVKLLEAIDTSKGGGMIAPDQFQGCLCFFKPRGP
Protein: Type-5 uracil-DNA glycosylase (EC 3.2.2.-) (Pa-UDGb) (Q8ZXE0)
Organism: Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)
Function: DNA glycosylase with broad substrate specificity. Can remove uracil from double-stranded DNA containing either a U/G or U/A base pair. Can also process hydroxymethyluracil (mispaired with guanine or adenine), hypoxanthine and fluorouracil. Exhibits a clear preference for double-stranded DNA substrates, but can also process uracil in single-stranded DNA, with lower efficiency.
Interaction partners:
- Type-4 uracil-DNA glycosylase
- EamA domain-containing protein
- PaREP2a
- Putative esterase PAE1329
Sequence:
MDLARVHTPRGWYDDFVNRLVNCARCPRLVSYRSTVKPLRRYESWSYWGRPVPPWGDLNARVMVVGLAPAAHGGNRTGRMFTGDASAQNLFKALFLLGLSNKPYSVSRDDGVEVRCVYITSAVKCAPPKNRPTAEEVYNCSSWLREELEAVRPRAVVALGELAWRAVLKILGATTAAFKHGEVVNAAGVRVYASYHPSPLNVNTGRLTVETLAEVLRRAAADAGCL
Protein: Monocarboxylate transporter 9 (MCT 9) (Solute carrier family 16 member 9) (Q7RTY1)
Organism: Homo sapiens (Human)
Function: Proton-linked monocarboxylate transporter. May catalyze the transport of monocarboxylates across the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31784090}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Solute carrier family 22 member 11
- Solute carrier family 22 member 12
- Sodium-dependent phosphate transport protein 1
- Solute carrier family 2, facilitated glucose transporter member 9
- Sodium-dependent phosphate transport protein 4
Sequence:
MELKKSPDGGWGWVIVFVSFLTQFLCYGSPLAVGVLYIEWLDAFGEGKGKTAWVGSLASGVGLLASPVCSLCVSSFGARPVTIFSGFMVAGGLMLSSFAPNIYFLFFSYGIVVGLGCGLLYTATVTITCQYFDDRRGLALGLISTGSSVGLFIYAALQRMLVEFYGLDGCLLIVGALALNILACGSLMRPLQSSDCPLPKKIAPEDLPDKYSIYNEKGKNLEENINILDKSYSSEEKCRITLANGDWKQDSLLHKNPTVTHTKEPETYKKKVAEQTYFCKQLAKRKWQLYKNYCGETVALFKNKVFSALFIAILLFDIGGFPPSLLMEDVARSSNVKEEEFIMPLISIIGIMTAVGKLLLGILADFKWINTLYLYVATLIIMGLALCAIPFAKSYVTLALLSGILGFLTGNWSIFPYVTTKTVGIEKLAHAYGILMFFAGLGNSLGPPIVGWFYDWTQTYDIAFYFSGFCVLLGGFILLLAALPSWDTCNKQLPKPAPTTFLYKVASNV
Protein: Translationally-controlled tumor protein (A0A0B4J2C3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIIYRDLISHDEMFSDIYKIREIADGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFFIGENMNPDGMVALLDYREDGVTPYMIFFKDGLEMEKCDAKERNPCAFCLSLWRPRLNWGIHL
Protein: Serine/arginine-rich splicing factor 9 (Splicing factor, arginine/serine-rich 9) (Q5PPI1)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Serine/arginine-rich splicing factor 2
- SRSF protein kinase 1
- Serine and arginine rich splicing factor 11
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 7
- Splicing factor U2AF subunit
- Serine/arginine-rich splicing factor 3
- Transformer-2 protein homolog beta
- Serine/arginine-rich splicing factor 5
- Polyadenylate-binding protein 2
Sequence:
MSGWADERGGEGDGRIYVGNLPTDVREKDLEDLFYKYGRIREIELKNRHGLVPFAFVRFEDPRDAEDAIYGRNGYDYGQCRLRVEFPRAYGGRGGWPRASRNGPPTRRSDFRVLVSGLPPSGSWQDLKDHMREAGDVCYADVQKDGMGMVEYLRKEDMEYALRKLDDTKFRSHEGETSYIRVYPERGTSYGCSRSRSGSRGRDSPYQSRGSPHYFSPFRPY
Protein: Protein Wnt-11b (Protein Wnt-11) (XWnt-11) (P49893)
Organism: Xenopus laevis (African clawed frog)
Function: Ligand for the frizzled7 transmembrane receptor. Primarily acts via non-canonical Wnt pathways mediated by either Ca(2+) and PKC, or by JNK and dvl2/dsh. Depending on the cellular context, can also signal via the canonical Wnt pathway mediated by beta-catenin and dvl2/dsh. May also inhibit canonical Wnt signaling. Maternally initiates dorsal/ventral axis formation by a canonical route, which signals via lrp6. In a complex with wnt5a, activates the canonical and non-canonical processes involved in axis formation. In the non-canonical pathway, acts through fzd7/fz7 to induce phosphorylation of dvl2/dsh. Signals through a non-canonical Wnt pathway to regulate convergent extension movements during gastrulation. Interactions with the secreted Wnt antagonist sfrp5 to coordinate foregut development, acting via a non-canonical Wnt pathway whereby sfrp5 restricts wnt11b activity to prevent inappropriate foregut formation. Mediates cardiogenesis via non-canonical Wnt signaling involving JNK-activation and PKC. Acts redundantly with wnt11/wnt11r during pronephros induction.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:10862746, ECO:0000269|PubMed:18927149, ECO:0000269|PubMed:19747829, ECO:0000269|PubMed:19906850}.
Interaction partners:
Sequence:
MAPTRHWVTPLLLLCCSGICGAIQWLGLTVNGSRVAWNESEHCRLLDGLVPDQSQLCKRNLELMQSVVNAAKQTKLTCQMTLSDMRWNCSSVENAPSFTPDLSKGTRESAFVYALASATLSHTIARACASGELPTCSCGATPAEVPGTGFRWGGCGDNLHYGLNMGSAFVDAPMKSSKSAGTQATKIMNLHNNAVGRQVLMDSLETKCKCHGVSGSCSVKTCWKGLQDLPHIANELKSKYLGATKVIHRQTGTRRQLVPRELDIRPVRESELVYLVSSPDYCTKNPKLGSYGTQDRLCNKTSVGSDSCNLMCCGRGYNAYTETIVERCQCKYHWCCYVMCKKCERTVERYVCK
Protein: Protein GPR15LG (Antimicrobial peptide with 57 amino acid residues) (AP-57) (Antimicrobial peptide-57) (Colon-derived SUSD2 binding factor) (CSBF) (Protein GPR15 ligand) (Protein GPR15L) (Secreted protein C10orf99) (Q6UWK7)
Organism: Homo sapiens (Human)
Function: Highly cationic protein that has multiple functions. Acts as a chemotactic factor that mediates lymphocytes recruitment to epithelia through binding and activation of the G-protein coupled receptor GPR15. May be a tumor suppressor; together with SUSD2 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest. May regulate keratinocyte proliferation. In addition, through activation of Mas-related G protein-coupled receptors (MRGPRs) contributes to pruritogenesis by activating itch-selective sensory neurons and mast cells degranulation.
Subcellular location: Secreted {ECO:0000269|PubMed:25351403, ECO:0000269|PubMed:25585381}.
Interaction partners:
- G-protein coupled receptor 15
- Sushi domain-containing protein 2
Sequence:
MRLLVLSSLLCILLLCFSIFSTEGKRRPAKAWSGRRTRLCCHRVPSPNSTNLKGHHVRLCKPCKLEPEPRLWVVPGALPQV
Protein: F1F0-ATPase putative regulatory protein IF1 (Q9GSE7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Large ribosomal subunit protein uL24
Sequence:
MSSSVSKLLKLTRASMIAAPKRSIAFRGDEFKEREEAFESQYVKQKERDDLKRMAEKKKQEETKKAGSQPTPNASSSANNSKAAKIKEIEDKISKLQKELADLKK
Protein: Uncharacterized protein (Q57YE5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYFFFFQVIDREKLAYASNISIILELLCAVLIFVLIGVFLRVAPLKWAHFVAPRRVNVCRAELNIINPKVEDALESTAVERPKENITNVKRHKEEDSRGNKISPIVEKTTNRAEKTSRVVRDISLEDTLDEFFREEQLLHDTLLDVETDMNLHRVEIEPTMRLLSPPKVVNQRIKVPASPEKRRENGRGKVVPVSKVHEKSLDEALECFFNDEELLEGTLQEVF
Protein: Protein phosphatase PP2A regulatory subunit A (Protein phosphatase 2A 65 kDa regulatory subunit) (PR65) (Q9UT08)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subsets of substrates (By similarity).
Interaction partners:
- Protein phosphatase PP2A regulatory subunit B
- Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 1 isoform
- Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 2 isoform
- Uncharacterized WD repeat-containing protein C1773.01
- Factor arrest protein 11
- Putative serine/threonine-protein phosphatase C22H10.04
- mRNA export factor elf1
- Serine/threonine-protein phosphatase 2A activator 2
Sequence:
MQTENQVNDLYPIAVLIDELKHDEITYRLNALERLSTIALALGPERTRDELIPFLDESIDDEDEVLSALADQLGNFVDYVGGPEYAHVLLSPLENLAATEETVVRDKAVDSLNKVCICLSQEQLEQYFVPLVQRLSTAEWFTSRASSAGLYCAAYSQSENPAVKVSLRQSFSHLCHDEAPMVRRPAATNCAKFVFLVTKQEAIDEFIPLFNSLSNDDQDSVRLLSFDIMVSLAEVLKSDSEIRHYLLQPLRSFVSDSSWRTRYMVAANFVKLAKVVGPSLIKDELIKPFVLLMKDTEQEVRRAIATQIPGFCELLDKRIVLEEIIPVIQELINDPAQHVRAALGMNIGALAPQLGKEKTTEYLLPMFLELLKDENPEVRLNIISKLEVVNKVVGIELLSQSLLPAIVTLAEDKQWRVRLAIIDYIPLLAQQLGVEFFNEKMGNLCMSWLEDHVYSIREAAIKNLRKLTEIFGLEWATETIIPKFLAMRSHPNYLYRMTTIFAISEIAPALNAEVIEKQILPTLEQLVNDPIPNIRFNVAKAFEVLKPVLAAGGDSTVYEQQIIPLLEQLTKDNDPDVQYFATQALEQTND
Protein: HCS2 neuropeptides (CNP neuropeptides) (Command neuron-specific peptides) [Cleaved into: Peptide CNP1 (CNP1); Peptide CNP2 (CNP2) (DYPRLamide); Peptide CNP3 (CNP3); Peptide CNP4 (CNP4)] (Q25077)
Organism: Helix lucorum (Snail)
Function: Neurotransmitter or neuromodulator peptides that mediate withdrawal behavior such as pneumostome activity in the respiratory system. Possibly regulates calcium levels in command premotor interneurons.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16763780, ECO:0000269|Ref.3}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:16763780, ECO:0000269|Ref.3}. Perikaryon {ECO:0000269|Ref.3}. Endoplasmic reticulum {ECO:0000269|PubMed:16763780}. Note=Occurs mainly on the granule surface (Ref.3). Present in the perikaryon of command neurons in the cytoplasm surrounding giant nuclei (Ref.3). {ECO:0000269|Ref.3}.; SUBCELLULAR LOCATION: [Peptide CNP3]: Cytoplasm {ECO:0000269|Ref.3}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:16763780, ECO:0000269|Ref.3}. Perikaryon {ECO:0000269|Ref.3}. Note=Occurs mainly within the granule. {ECO:0000269|Ref.3}.; SUBCELLULAR LOCATION: [Peptide CNP4]: Cytoplasm {ECO:0000269|Ref.3}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|Ref.3}. Perikaryon {ECO:0000269|Ref.3}.
Interaction partners:
Sequence:
MQHQIRALLLFLLSGSACAMFYPRPKDYPRLGKRSFFTTVNGNHYPRIGRRDATGSSLVLPEADYTDLGDLTKRGVFTQGAHGSYPRVGRGGAVLSRDYLNERSKNLEKMSGDKDDDLEVDNGDGSRRLQAGHSGIPLEILFIAYDSDNDGKLSKEEFVTGLAQYQMQCPLY
Protein: DNA methyltransferase 1-associated protein 1 (A0A8I6A1B5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATGADVRDILELGGPEGDAASGTISKKDIINPDKVAGTELLGFSGSSHTLKAKLGSKKVRPWKWMPFTNPARKDGAMFFHWRRAAEEGKDYPFARFNKTVQVPVYSEQEYQLYLHDDAWTKAETDHLFDLSRRFDLRFVVIHDRYDHQQYKKRSVEDLKERYYHICAKLANVRAVPGTDLKIPVFDAGHERRRKEQLERLYNRTPEQVAEEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKLPQKKEAEKPAVPETAGIKFPDFKSAGVTLRSQRMKLPSSVGQKKIKALEQMLLELGVELSPTPTEELVHMFNELRSDLVLLYELKQACANCEYELQMLRHRHEALARAGVLGGPATPAVGPTPASAEPTVSESGLGLDPSKDTIIDVVGAPLTPNSRKRRESASSSSSVKKAKKP
Protein: Origin recognition complex subunit 6 (H3BT22)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MCLDLAASWMKCPLDRAYLIKLSGLNKETYQSCLKSFECLLGLNSNIGIRDLAVQFSCIEAVNMASKILKSYESSLPQTQQVDLDLSRPLFTSAALLSACKILKLKVDKNKMVATSGVKKAIFDRLCKQLEKIGQQVDREPGDVATPPRKRKKIVVEAPAKEMEKVEEMPHKPQKDEDLTQDYEEWKRKILENAASAQKATAE
Protein: Pathogen-associated molecular patterns-induced protein A70 (PIG A70) (F4K956)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- U-box domain-containing protein 8
- Probable galacturonosyltransferase-like 10
- General transcription factor IIH subunit 2
- 7-dehydrocholesterol reductase-like protein
- PLASTID TRANSCRIPTIONALLY ACTIVE protein 6, chloroplastic
- UDP-glycosyltransferase 87A2
- At4g27438
Sequence:
MELLTTVASFFTPTTLFLLLNLMIGTIVVTSRLGSGSRKHYQHHDGFGSGHAPAPLARAPSIIDRVKSINFHLYKFPHPETELFSMTAHHDIIGSDLHVYPDPNPAPLQRAPSLLDRVKSINMSYFKFPHDVTGSDPHSHSHSHLDLHPDPAPAPLQRAPSLLDRVKSINMSYFKFQQYNPEENDYAHHTEPTRFESIPTRMGRVDPIDISKFRIPEEDQPTGTGVNSQINPPGLTRAPSILERVKSIKLSSFYRSDPDLDQKQNPDPVLHEEHKHVRSKSESKKPVKKKKKALTKMTKSASEKSGFGFAGSHAEAPETVESLERRRPDTTRVERSTSFGDGEDGVDAKASDFINKFKQQLKLQRLDSILRYKEMLKAH
Protein: Bifunctional uridylyltransferase/uridylyl-removing enzyme (UTase/UR) (Bifunctional [protein-PII] modification enzyme) (Bifunctional nitrogen sensor protein) [Includes: [Protein-PII] uridylyltransferase (PII uridylyltransferase) (UTase) (EC 2.7.7.59); [Protein-PII]-UMP uridylyl-removing enzyme (UR) (EC 3.1.4.-)] (Q2RNG2)
Organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Interaction partners:
- Nitrogen regulatory protein P-II
- Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
- Ammonium transporter
- Nitrogen regulatory protein P-II
- Nitrogen regulatory protein P-II
- Glutamate synthase large chain
- Probable lipid II flippase MurJ
- DNA-binding transcriptional regulator NtrC)
Sequence:
MTIPRIRQPRAVIDRKALTVVLEDLAATVTDNRERRARLLAVLKGALGDGRAEVRRRFLEEKGTGAAVFAENSHLMDQIIRLLFDFTTTHVYPRANRTIGEQMTVLAVGGYGRGEMSPQSDVDLLFLLPYKATPLHEQVVEYMLYTLWDMGLKVGHATRSIEECIRQARGDLTIRTAMLETRYLWGDRALYGQLKTKFWTGVVTGTGPDFVEAKLAERDERHLRMGDSRYVLEPNIKDGKGGLRDLHTLLWIARYIYGVSDMRELVELGVLSADAATKFGRARAFLWTVRCHLHYLADRPEERLTFDVQPAIAARMGYTDRNSGRGVERFMKHYFLMAKTVGDLTRIFCAVLEDQQKRRPILSIATLLMRKRNLGDFVLDGGRLAVAGRGAFREHPLQLISLFKVAHDHGLDIHPDTLRLVTEHLPTVTLLRNDAKANALFMEILTSRKDPELALRQLSESGVLARFIPDFGRVTAQMQFDMYHVYTTDEHTIRAIGLLHRLETGALRDRMPAAADAVHKVQSRRALYLAVLLHDIAKGRGGDHSILGAEVAMRLGPRLGMSEEETETVAWLVRHHLDMSRTAFKRDLDDIKTILDFTGLVQSVERLHLLLALTTVDILAVGPAVWNNWKSSLLRELYTHSKDVLTSGFQAEARDKRVAHKREELAAALADWPQASRERYLDLHYPAYWLTFDSATHLRHARMLRRARDAGLTVAVEVLPDPERAVSEVLVATDDHPGLFSKIAGAMALAGVNILDAKITTMSDGGALDIFTVQTLEGHAIEKEERIARLAKTVRDVLTGDLPLEKALRRQPPRLPERTRHLTVPPRVIVDNQASKTHTVIEINGRDRPGFLYAVTRALTDVAVQISSARVSTYGERVVDSFYVKDVFGMKIVHRAKLAQIREALEAAITQTVPRKVEEGAEQGAEKADAGEIVAA
Protein: Long conserved protein (Q50732)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv2567
- Probable conserved transmembrane protein
- Uncharacterized protein Rv2411c
- Uncharacterized protein Rv2568c
- Fatty acid ABC transporter ATP-binding/permease protein
- Uncharacterized NTE family protein Rv2565
- Conserved protein
Sequence:
MPLRPTQVSGTGRTRCAGRSGVISSAAMSIKVALEHRTSYTFDRLVRVYPHIVRLRPAPHSRTSIEAYSLRIEPADHFINWQQDALGNFLARLVFPNPMRQLRITVGLIADLKVINPFDFFIEDWAEIWPCAGMAYPKALADDLRPYLRPVDEDGDGSGPGELTQAWVRNFTVPDGTRTIDFLVALNRAINADVGYCVRMEPGVQTPDFTLRTGVGSCRDSAWLLVSILRQFGLAARFVSGYLVQLASDIEALDGPSGPAADFTDLHAWAEAYIPGAGWIGLDPTSGLLAGEGHIPLAATPHPASAAPISGGTDVCDTVLEFSNTVTRVHEDPRVTLPYTDESWKTICEVGQRVDERLAAADVRLTVGGEPTFVSVDNQVAEEWRTAADGPHKRERASDLAARLKAVWAPQGLIHRGQGRWYPGEPLPRWQIALYWRTDGRPLWTNDALLADPWGAPPADPVDDDAAYRVLAGIADGLGLPISQVRPAYEDPLSRLAAAVRMPAGDPVESGDDLGCDTNPDTPTGRAALLARLDEAITSPAAYVLPLHRRDDGQGWASANWRLRRGRIVLLEGDSPAGLRLPLDSISWRPPRASFDADPVAVRSTLPAELHTDRAVVEDPETAPTTALVAEVRGGLVHIFLPPTDALEHFIDLVARVEAAATTANCPVVIEGYGPPPDPRLTSTTITPDPGVIEVNIAPTASFAEQRQQLETLYQQARLARLTTEAFDVDGTHGGTGGGNHITLGGVTPADSPLLRRPDLLVSLLTYWQRHPSLSYLFAGRFVGTTSQAPRVDEGRAEALYELEIAFAEILRLSPSSGGGRPQPWVTDRALRHLLTDITGNTHRAEFCIDKLYSPDSARGRLGLLELRGFEMPPHLHMAMVQSLLVRSLVAWFWDQPLRAPLIRHGANLHGRYLLPHFLIHDIADVAADLRAHGIAFETSWLDPFTEFRFPRIGTAVFDGIEIELRGAIEPWHTLGEEATAAGTARYVDSSVERIQVRIIGADRHRYVVTCNGYPMPLLATDNPDIHVGGVRFKAWQPPSALHPTITVDGPLRFELIDIATATSCGGCTYHVAHPGGRAYDEPPVNAVEAEARRARRFEATGFTPGKLDLSDIREKQARISTDIGAPGILDLRRVRTVQQ
Protein: DnaJ homolog subfamily B member 5 (Heat shock protein Hsp40-2) (Heat shock protein Hsp40-3) (Heat shock protein cognate 40) (Hsc40) (O75953)
Organism: Homo sapiens (Human)
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock protein 105 kDa
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 4
- DnaJ homolog subfamily B member 4
- Heat shock-related 70 kDa protein 2
- Heat shock 70 kDa protein 6
- Heat shock 70 kDa protein 1-like
- P2X purinoceptor 6
- DnaJ homolog subfamily B member 1
Sequence:
MGKDYYKILGIPSGANEDEIKKAYRKMALKYHPDKNKEPNAEEKFKEIAEAYDVLSDPKKRGLYDQYGEEGLKTGGGTSGGSSGSFHYTFHGDPHATFASFFGGSNPFDIFFASSRSTRPFSGFDPDDMDVDEDEDPFGAFGRFGFNGLSRGPRRAPEPLYPRRKVQDPPVVHELRVSLEEIYHGSTKRMKITRRRLNPDGRTVRTEDKILHIVIKRGWKEGTKITFPKEGDATPDNIPADIVFVLKDKPHAHFRRDGTNVLYSALISLKEALCGCTVNIPTIDGRVIPLPCNDVIKPGTVKRLRGEGLPFPKVPTQRGDLIVEFKVRFPDRLTPQTRQILKQHLPCS
Protein: Tape measure protein (TMP) (E7DNB6)
Organism: Pneumococcus phage Dp-1 (Bacteriophage Dp-1)
Function: Plays a role in virion tail formation. The length of the tape measure protein is proportional to the length of the phage's tail.
Subcellular location: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Virion {ECO:0000305}.
Interaction partners:
Sequence:
MDFGSIAAKMTLDISNFTSQLNLAQSQAQRLALESSKSFQIGSALTGLGKGLTTAVTLPLMGFAAASIKVGNEFQAQMSRVQAIAGATAEELGRMKTQAIDLGAKTAFSAKEAAQGMENLASAGFQVNEIMDAMPGVLDLAAVSGGDVAASSEAMASSLRAFGLEANQAGHVADVFARAAADTNAETSDMAEAMKYVAPVAHSMGLSLEETAASIGIMADAGIKGSQAGTTLRGALSRIAKPTKAMVKSMQELGVSFYDANGNMIPLREQIAQLKTATAGLTQEERNRHLVTLYGQNSLSGMLALLDAGPEKLDKMTNALVNSDGAAKEMAETMQDNLASKIEQMGGAFESVAIIVQQILEPALAKIVGAITKVLEAFVNMSPIGQKMVVIFAGMVAALGPLLLIAGMVMTTIVKLRIAIQFLGPAFMGTMGTIAGVIAIFYALVAVFMIAYTKSERFRNFINSLAPAIKAGFGGALEWLLPRLKELGEWLQKAGEKAKEFGQSVGSKVSKLLEQFGISIGQAGGSIGQFIGNVLERLGGAFGKVGGVISIAVSLVTKFGLAFLGITGPLGIAISLLVSFLTAWARTGEFNADGITQVFENLTNTIQSTADFISQYLPVFVEKGTQILVKIIEGIASAVPQVVEVISQVIENIVMTISTVMPQLVEAGIKILEALINGLVQSLPTIIQAAVQIITALFNGLVQALPTLIQAGLQILSALINGLVQALPAIIQAAVQIIMSLVQALIENLPMIIEAAMQIIMGLVNALIENIGPILEAGIQILMALIEGLIQVLPELITAAIQIITSLLEAILSNLPQLLEAGVKLLLSLLQGLLNMLPQLIAGALQIMMALLKAVIDFVPKLLQAGVQLLKALIQGIASLLGSLLSTAGNMLSSLVSKIASFVGQMVSGGANLIRNFISGIGSMIGSAVSKIGSMGTSIVSKVTGFAGQMVSAGVNLVRGFINGISSMVSSAVSAAANMASSALNAVKGFLGIHSPSRVMEQMGIYTGQGFVNGIGNMIRTTRDKAKEMAETVTEALSDVKMDIQENGVIEKVKSVYEKMADQLPETLPAPDFEDVRKAAGSPRVDLFNTGSDNPNQPQSQSKNNQGEQTVVNIGTIVVRNNDDVDKLSRGLYNRSKETLSGFGNIVTP
Protein: Protocadherin 10a (Protocadherin-10a isoform X1) (A0A2R8QI99)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MILIFLFFSILDGGLSQLHFSVPEEQERGTVVGNIAEDLGLDITKLSARRFQTVPSSRTPYLEVNLENGALVVNERIDREEICRQTVPCLLHLEVFLENPLELFRVEIEVMDINDNPPSFPETDITVEITESATPGTRFPVENAFDPDVGTNALSTYAITTNNYFYLDVQTQGDGNRFAELVLDKPLDREQQAIHKYVLTAVDGGQPQRTGTALLVVKVLDSNDNAPTFDQSVYSVSLRENSPVGTLVIQLNASDMDEGQNGEIVYSLSSHNSPRIRDLFNIDSRTGRIEVTGEVDYEESSTHQIYVQAKDMGPNAVPAHCKVLVKLIDVNDNTPEISFSTVTESVSEQAAPGTVIALLSVTDRDSGENGQMTCELHGEVPFKLKSSFKNYYTIVTDGPLDREKAESYTLTVVAKDKGVPSLSTSKSIKVHVSDENDNAPRFMQSVYDVYVTENNVPGAYIYAVSAVDPDVGQNAYVTYSILECEIQGMSILTYVSINSENGYLYALRSFDYEQIKEFSFMVHAKDSGAPELTANATVNVIIVDQNDNAPSVIAPLGKNGTAREHLPRSAEPGYLVTRIVATDADDGENARLSYSILRGNELGMFRMDWRTGELRTARRVSSKRDPPHPYDLLIEVRDHGQPPLSSSASINVLLVDSVVEGRSGDRGSVKSKEGSLDLTLILIIALGSVSFIFLLAMIVLAVRCQKDKKLNIYTCMAGDSCCQCCSRQARGRKKKLSKSDIMLVQSTNVASTAQVPVEESGSFGSHHQNQNYCYQVCLTPESAKTDLMFLKPCSPSRSTDTEHNPCGAIVTGYADQQPDIISNGSILSSETKHQRTELSYLVDRPRRVNSSAFQEADIVSSKDSGHGDSEQGDSDHDATNRGHTAGADLFSNCTEECKALGHSDRCWMPSFMPGDSRQGADYRSNLHVPGMDAVPDTEVQESVVPGDACNRADDRSFSTFGKDKSHHGTLTRHELHTLLPSARAPYKPNYLSRKRIS