wanglab/gogpt-training-data huggingface dataset:
Protein: Latrophilin-like protein 1 (G5EDW2)
Organism: Caenorhabditis elegans
Function: Has a role in the establishment of anterior-posterior polarity in tissues during embryogenesis. Required for the alignment of the mitotic spindles and division planes. May have a role in cell death events. Required for normal defection and oocyte fertilization. Involved in sperm function. Operates in pharyngeal pumping during feeding.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19853563}; Multi-pass membrane protein {ECO:0000269|PubMed:19853563}.
Interaction partners:
- Teneurin-1
- Netrin receptor unc-5
- Guanine nucleotide-binding protein subunit beta-1
- Guanine nucleotide-binding protein subunit beta-2
- FERM domain-containing protein
- Protein kinase domain-containing protein
- G protein gamma domain-containing protein
- Guanine nucleotide-binding protein subunit gamma
- CYtochrome P450 family
- Probable U2 small nuclear ribonucleoprotein A'
Sequence:
MRRNKTTYSLLQTILVACLLTVTPTFASNKPTTDESGTISHTICDGEAAELSCPAGKVISIVLGNYGRFSVAVCLPDNDIVPSNINCQNHKTKSILEKKCNGDSMCYFTVDKKTFTEDPCPNTPKYLEVKYNCVVPATTTTTTTTTSTTTTDSSLIVDEEEEAQKDALNSDVIKPVKKKEDVFCSATNRRGVNWQNTKSGTTSSAPCPEGSSGKQLWACTEEGQWLTEFPNSAGCESNWISSRNSVLSGVISSEDVSGLPEFLRNLGSETRRPMVGGDLPKVLHLLEKTVNVIAEESWAYQHLPLSNKGAVEVMNYMLRNQEIWGSWDVTKRKEFASRFILAAEKAMVASAKGMMTSAESNVIVQPAITVEISHKIKMSSQPTDYILFPSAALWNGQNVDNVNIPRDAILKINKDETQVFFSSFDNLGAQMTPSDVTVAIAGTDQTEVRKRRVVSRIVGASLIENGKERRVENLTQPVRITFYHKESSVRHLSNPTCVWWNHHELKWKPSGCKLSYHNKTMTSCDCTHLTHFAVLMDVRGHDLNEIDQTLLTLLTYVGCIISIICLLLTFFAYLIFSRNGGDRVFIHENLCLSLAIAEITFLAGITRTEDSLQCGIIAVALMYMFLSALTWMLLEGYHIHRMLTEVFPSDPRRFTYLLVGYIPPAIITLVAYLYNSDGFGTPDHCWLSTQNNFIWFFAGPACFIFCANSLVLVKTLCTVYQHTSGGYLPCRHDVDSGRSIRNWVKGSLALASLLGVTWIFGLFWVEDSRSIVMAYVFTISNSLQGLFIFLFHVVFAEKMRKDVGHWMYRRGCGGSSNSSPNHKRHNVQRDLMSPGVNSSTGSDFLYNTNDKYLTNSDTTNRLVYNGIMNHPNQMSVYQQHPHHQIYEQQPGTYDYATIAYGDMMPGHRVAAPPAYQRLAVAEGRYGSQHQLYQGWHHRPPPEFSPPPPPLSTGPPNSRHYGTGSSGRRPPSSKMSDDSAYSDGSSSMLTTEVTPQGQTVLRIDLNKPSMYCQDL
Protein: Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 [Includes: Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (EC 1.14.11.4) (Lysyl hydroxylase 3) (LH3); Procollagen glycosyltransferase (EC 2.4.1.50) (EC 2.4.1.66) (Galactosylhydroxylysine-glucosyltransferase) (Procollagen galactosyltransferase) (Procollagen glucosyltransferase)] (Q5U367)
Organism: Rattus norvegicus (Rat)
Function: Multifunctional enzyme that catalyzes a series of post-translational modifications on Lys residues in procollagen. Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (By similarity). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (By similarity). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the ADIPOQ collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues. Essential for normal biosynthesis and secretion of type IV collagens. Essential for normal formation of basement membranes (By similarity).
Subcellular location: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:O60568}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:O60568}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9R0E1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9R0E1}; Lumenal side {ECO:0000250|UniProtKB:Q9R0E1}. Secreted {ECO:0000250|UniProtKB:O60568}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q9R0E1}. Note=The majority of the secreted protein is associated with the extracellular matrix. {ECO:0000250|UniProtKB:Q9R0E1}.
Interaction partners:
- Glycosyltransferase 25 domain containing 1
- Collagen beta
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
- Calmodulin-lysine N-methyltransferase
- [histone H3]-lysine
- Prolyl 4-hydroxylase subunit alpha-1
- Collagen alpha-1
Sequence:
MAASVPEPRLLLLLLLLLPPLPPVTSASDRPRGANPVNPDKLLVITVATAETEGYRRFLQSAEFFNYTVRTLGLGQEWRGGDVARTVGGGQKVRWLKKEMEKYASQEDMIIMFVDSYDVILASSPTELLKKFVQSGSHLLFSAESFCWPDWGLAEQYPEVGVGKRFLNSGGFIGFAPTIHRIVRQWKYKDDDDDQLFYTQLYLDPGLREKLKLSLDHKSRIFQNLNGALDEVVLKFDQNRVRIRNVAYDTLPVVVHGNGPTKLQLNYLGNYVPNGWTPQGGCGFCNLNRRTLPGGQPPPRVLLAVFVEQPTPFLPRFLQRLLLLDYPPDRISLFLHNNEVYHEPHIADAWPQLQDHFSAVKLVGPEEALSSGEARDMAMDSCRQNPECEFYFSLDADAVLTNPETLRILIEQNRKVIAPMLSRHGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGLWNVPYISQAYVIRGETLRTELPEKEVFSSSDTDPDMAFCRSVRDKGIFLHLSNQHEFGRLLSTSHYDTDHLHPDLWQIFDNPVDWREQYIHENYSRALDGEGLVEQPCPDVYWFPLLTEQMCDELVEEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTEHLFPGYHTKTRAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGVDYEGGGCRFLRYDCRVSSPRKGWALLHPGRLTHYHEGLPTTRGTRYIMVSFVDP
Protein: DNA-binding response regulator (Q9A912)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
- histidine kinase
- histidine kinase
- histidine kinase
- Sensory/regulatory protein RpfC
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- Sensory/regulatory protein RpfC
- histidine kinase
Sequence:
MENVQNAAQSELEAVRGAPSRILIVDDDPGIRDVVSDFLAKHGYVVETAQDGRTMEQVLARGPIDLIVLDVMLPGEDGLAICRRLSATPEAPAIIMLSAMGEETDRIVGLELGADDYLPKPCNPRELLARVRAVLRRRQEPRAVDDAMGAACEFAGWRLDLVRRELRSPQSIVVNLSSGEFSLLRAFVERPQRVLTRDQLLDLARGRDSDAYDRAIDVQISRLRRKLDDGGGSELIRTIRSEGYMFTAKVVRTP
Protein: Cyclic nucleotide-binding domain-containing protein (Q9N4C1)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Cyclic nucleotide-binding domain-containing protein
- Guanine nucleotide-binding protein alpha-17 subunit
- Receptor-type guanylate cyclase daf-11
- Receptor-type guanylate cyclase gcy-10
- Ion transport domain-containing protein
- Cyclic nucleotide-gated channel
Sequence:
MFSSFNFEDPPPSEVPRKVQRKDRSVRYLRALSAKNQERTANEHSSVDVAVTQASLSVPRPGILRLPSSDPGEEDPQPSTSSIPHRPSKWATVREKSPQIIGGHAKEVTFQERHHKLDLNKSRSTSKNRRKSAQNGGAEDPGQKSFSDVVKTAMMLRTWISAMEHDERESEPDRDATTTNAEITAADDRSILPSPPIFQQRQTGFTQIKDILTDKCRKLYYFYVTENSTFFYYWTAIISIGILYNMFAMVIFIFDDVHFGYFNQWLYVNLFFDFCFLLDCLVGSRMTFVSEGNEVSQTDKMFKNYRQSRRCKLDLLCLAPADFYLFIDTKASLVRAIRLVKAYRLYEFIMLTQRRTDFPHFMKILFLTSSCAILFHWNACVYFLFSLYQGLTEDDPNAFGFSYYKVFDPRFSICDALYDQDCYYPEDTEVLDIRDERPHYMEDMYKFWDKKFNILQIGNFSREYSMTIYWSSLTITKCGQQPWPSKSSQNSLEIFDTLIGVLVFATIIGGVGSVVTQMSQNVNDFREMMDGIKFYMKYRGVQSAIQDRVLNCFLYLNSHNQLYDEEEILSLLPPFFQARIAANLHQDTLSKVSLFYKCDQRLLQEVVMLVKQQVYSPNDYLCRKNEKAKEMFIVKKGLLAVIDDDTGVELDSLKEGHTFGELSIVQVKGNILGDRRSVSLRSVGYSDVYVLHQDDVTRLLQEYPEERVRLMENARRMLHSRGLLETNELGEMCETDDGLDDEAMLEFLSVDEQLNRLENIIDSIDTDLANMITSFSYNSVAYKKRVTALENIFNSNKKRIRGDLYNGILKTDYDDRMMF
Protein: Laminin subunit beta 3 (F1LPI5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Laminin subunit gamma-2
- Laminin subunit alpha 3
- Integrin beta-4
- Laminin subunit alpha-5
- CD44 antigen
- Integrin beta-6
- Laminin subunit gamma-1
- Integrin beta-1
- Integrin alpha-6
- Integrin subunit alpha 5
Sequence:
MMTALFLLWLALPGLLCAQQPCSRGACYPPVGDLLIGRTQLLRASSTCGLTKPETYCTQYGQWQMKCCKCDSRLPRNYNSHRVENVVSSSGPMRWWQSQNDVSPVSLQLDLDKRMQLQDIMMDFKGLMPAGMLIERSSDFGKTWRVYQYLATDCASTFPQVHQGQPKNWQDVRCRPLSQRPNGHLTGGKVQLNLMDLASAIPASQSKKIQELGDITNLRVNFTKLAPVPQRGSYPPSAYFAVSQLRLQGSCFCHGHADRCAPNPGGPTGSTTAVQVNDVCVCQHNTAGPNCDRCAPFYNNRPWRPAEGQDIHECQRCDCNGHSETCHFDPAVFAASQGTSGGVCDNCQDHTEGKNCERCQLHYFRNRRPGAPIHETCIPCECDPDGAVPGAPCDRLTGQCVCKDHVQGERCDLCKPGFTGLTFANPQGCHPCDCSILGTRQDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKLASGRGCEPCACDPRNSLSSQCNQFTGQCPCREGFGGLTCSSAAIRQCPDRTHGDVATGCRACDCDFRGTEGPGCDKTSGRCLCRPGLTGPRCDQCQRGYCDRYPVCVACHSCFQAYDTDLQEQAWRLGSLRNTTEGLGTGTGLEDRGLASRLLDAKSKIEQIRQILGGTSVTERDVAQVANAILSIRRTLQGLPLDLPLEEEMESFSGDLGNLDRSFNRLLLMYRSKKEQFEKLSSVDPSGAFRMLTMAYEQSSRAAQQVSDSSSLLSQLRDSRREVEGLERQTGEGGAGGAQLMALRLEMASLPDLTPTINKLCGGSRQTACTPGDCPGLLCPQDNGTACGSHCRGALPRARGALHMAGQVAEQLRSFNTQLQQTRQMIRAAEEAASKVQSDAQRLETQVSTSRLQMEEDVRRTRLLIQQVRGFLTDPHTDAATIQQVSEAVLALWLPTDSATVLRKMKEIQDIAARLPNVDLVLSQTKQDIARARRLQAEAEKARSRAHVVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVTEVQQVLVPAERLVKGMKEQMSGFWARVKELRHQAQEEQAQAMKAQQLAEGASNQAMNAQEGFERLKQRYTELKDRLGQSSMLGEQGNRILSIKAEAEELFGETMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATCK
Protein: Interferon regulatory factor 6 (IRF-6) (P97431)
Organism: Mus musculus (Mouse)
Function: Probable DNA-binding transcriptional activator. Key determinant of the keratinocyte proliferation-differentiation switch involved in appropriate epidermal development. Plays a role in regulating mammary epithelial cell proliferation. May regulate WDR65 transcription.
Subcellular location: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:19036739}. Note=Translocates to nucleus in response to an activating signal. {ECO:0000305}.
Interaction partners:
- Grainyhead-like protein 3 homolog
- Ventral anterior homeobox 1
- Receptor-interacting serine/threonine-protein kinase 4
Sequence:
MALHPRRVRLKPWLVAQVDSGLYPGLIWLHRDSKRFQIPWKHATRHSPQQEEENTIFKAWAVETGKYQEGVDDPDPAKWKAQLRCALNKSREFNLMYDGTKEVPMNPVKIYQVCDIPQTQGSVINPGSTGSAPWDEKDNDVDEDEEEDELEQSQHHVPIQDTFPFLNINGSPMAPASVGNCSVGNCSPESVWPKTEPLEMEVPQAPIQPFYSSPELWISSLPMTDLDIKFQYRGKEYGQTMTVSNPQGCRLFYGDLGPMPDQEELFGPVSLEQVKFPGPEHITNEKQKLFTSKLLDVMDRGLILEVSGHAIYAIRLCQCKVYWSGPCAPSLAAPNLIERQKKVKLFCLETFLSELIAHQKGQIEKQPPFEIYLCFGEEWPDGKPLERKLILVQVIPVVARMIYEMFSGDFTRSFDSGSVRLQISTPDIKDNIVAQLKQLYRILQTQESWQPMQPAPSMQLPQALPAQ
Protein: Vacuolar protein sorting-associated protein 26 (Q10243)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor pep1/vps10. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The vps29-vps26-vps35 subcomplex may be involved in cargo selection.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein vps5
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 17
- Sorting nexin-3
- Vacuolar protein sorting/targeting protein 10
- Sorting nexin-4
- Syntaxin pep12
- Sorting nexin-41
Sequence:
MDYFFKSPIDVDLHLDNEEERTFVDYEFEQGRKDKAPIYESDETVKGTVMIRLKDGRKLDHDGVKIEFIGQIENTYDKGNIHEFTRSVQELASPGEMRHAQMFEFEFKHVDKPYESYIGKNVKLRYICRVTVSRKMKDVIREKDLWVYRFENEPETNSLIRMDVGIDECLHIEFEYSKNKYHLKDVIIGKIYFILVRIKVQRMEVSIIRRETIGTSPNQYSNSETITRFQIMDGNPNRGETIPLRMFLNGYALTPTFRDVNKKFSVRYYLSLILVDEDQRRYFKQSEITLWRRRDEHE
Protein: Imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) (Q5AYU4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Histidine biosynthesis trifunctional protein
- histidinol-phosphate transaminase
- Histidinol dehydrogenase
- Imidazole glycerol phosphate synthase hisHF
- 1-
- ATP phosphoribosyltransferase
- Protein qutG
- DNA excision repair protein Rad16, putative
- Multifunctional tryptophan biosynthesis protein
- phosphoserine phosphatase
Sequence:
MPLPARTASLSRNTNETKIQVSLSLDGGVLPPYEPSSHFPVPTDPLEAEAAKKGIVPNKDAAHATQFTPTQQITISTGIGFLDHMLHALAKHSGWSLAIRAKGDLYIDDHHTTEDTFLALGTAFTTALGARQSLARFGRGDAPLDEALSWAVIDLSSRPWAVINIGFKREKIGDLSTEMITHGLQSFAQAAGVTLHIGCTYGDNDHHRAESAFKALAVAIRAACARRVEGEVGAGDVVSTKGVL
Protein: Collagen type V alpha 3 chain (Collagen, type V, alpha 3) (Q9JLI2)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Lumican
- Collagen alpha-1
- Collagen alpha-1
Sequence:
MRSCRRLDQLQAGLCLLLASLQLVSWTLAAEPVDVLEAWGVHRDQAGVAEGPGFCPLRIPQGDRAFRVGKSSLLSVPTWQLFPDGHFPENFSVLLTLRAQPANQSVLLSIYDEKGVRQLGLALGPALGLLGDSFRPLPKQVNIMDGRWHRVAVSISGNKVTLVVDCEPQPPTFGQGPRFISTAGLTVMGTQDTREESFEGDIQELLLIPDPQAAFQACESYLPGCETLDSTTTGAPKDDEPETPAPRRRKGKGKKKGRGRKGKGRKKNKETSELSPTPGAPENQTSLHIPETEKTVPHLPLTPTPLAITTTVTIGQNATVSQGLDSGTETEQTTPEVDSTEEGEGGGPTMGPKFRAAEQSLQTEFQIFPGAGEKGAKGEPATVEQGQQFEGPAGAPGPRGISGPSGPPGPPGFPGDRGLPGPAGLPGIPGIDGARGLPGTVIMMPFHFASSSMKGPPVSFQQAQAQAVLQQAQLSMKGPPGPVGLTGRPGPVGLPGYPGLKGELGEVGPQGPRGLQGPPGPPGREGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQAGEPGPRGLIGPRGLPGPLGRPGVTGSDGAPGAKGNVGPPGEPGPPGQQGNHGSQGIPGPQGPIGTPGEKGPPGNPGIPGVPGSEGPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKGDRGNPGPPGPRGEDGPEGQKGPGGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGPPGEKGLPGLQGPPGFPGPKGPPGPQGKDGISGHPGQRGELGFQGLTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGEQGLPGIEGREGAKGELGPLGSVGKEGPPGPRGFPGPQGAPGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGLQGPSGAAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEKGEVGDVGSMGPHGAPGPRGPPGPSGSEGPPGLPGGVGQPGAVGEKGEPGDAGDAGPPGIPGIPGPKGEIGEKGDSGPSGAAGPPGKKGPPGEDGSKGNMGPTGLPGDLGPPGDPGVPGIDGIPGEKGNAGDIGGPGPPGASGEPGARGLPGKRGSPGRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGPDGLPGIPGPVGEPGLLGPPGLIGPPGPLGPPGLPGLKGDAGPKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSPGSLGPRGDPGPAGPPGPPGSPAEVHGLRRRRSVTDTLEGGLEEVMASLNSLSLELQQLQRPLGTAESPGLMCRELHRDHPHLPDGEYWIDPNQGCARDAFKVFCNFTAGGETCLYPDKKFETVKLASWSREKPGGWYSTFRRGKKFSYVDADGSPVNVVQLTFLKLLSAAAHQRFTYICQNSVAWLDEAAGDHRHSIRFQGTNWEELSFNQTTAATIKVSHDGCRVRKGQAKTLFEFSSSVGFLPLWDVAASDFGQTNQKFGFELGSICFSS
Protein: Elongation factor 2 (EF-2) (EC 3.6.5.-) (P13639)
Organism: Homo sapiens (Human)
Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25064856}. Nucleus {ECO:0000269|PubMed:24648518}. Note=Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product. {ECO:0000269|PubMed:24648518}.
Interaction partners:
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS7
Sequence:
MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSPEGKKLPRTFCQLILDPIFKVFDAIMNFKKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGLVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL
Protein: Serine/threonine-protein kinase pakB (dPAKb) (EC 2.7.11.1) (Myosin I heavy chain kinase) (Q869N2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Regulator of the myosin I component of the cytoskeleton: required for regulation of cytokinesis, phagocytosis and pinocytosis.
Subcellular location: Membrane {ECO:0000269|PubMed:15509655, ECO:0000269|PubMed:9774403}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15509655, ECO:0000269|PubMed:9774403}. Note=Mainly cytosolic but enriched at the leading edge of migrating cells and at macropinocytic and phagocytic cups, possibly due to binding to acidic phospholipids.
Interaction partners:
- Rho-related protein rac1A
- Rho-related protein racC
- Rho-related protein racB
- Rho-related protein racF1
- Myosin, essential light chain
- Rho-related protein rac1B
- Ras GTPase-activating-like protein gapA
- Myosin-K heavy chain
- Rho-related protein racG
Sequence:
MEQSKRVSMMREKFEAQSNEAESSPPPNRKPPPPNKRVQTNGTSSLNSSGSSFVSPSPSPSPSPQQPVKRPLPSPGVNKQAPPALPTQPRPQQQQPEIPVRPTTPTRTPPNLINSNGTSGGSGFSSSSGNSGYSSSNNNNSNSNSSINMNGNHSNGLNGGSSNPVPMRKVSSPINIANGTTPPPPPQPTPSQQPQQSPSSASHNNTQHNIPSPPPLPNNKPKKLAPTAVPAGLGSIIGGPKTPAISPGSTSPSLGSSNGNIPISTTSTPITPTPPISVPLATSPNNSHKDSISNSNSNNNNNNNNNNNNNSSNATTSPPSPPVSNVGNKQDEEKKGFLSIFTNKKKNKDKKKEFSVGSPFNVKHNIHVNYHSVTGFEGLPKEWEVILQSSGITREDVVEHSEVVIDVLDFHMQQQQQQAQQEQQALMQKQMQQSGIPAHMLNNPKPPTIPIRDANKQPHNQLQPTPHQPPQHHHQQQPPQQHHHQQQQQQHNNNNNNNNNNNNNNNNQQSAQQQSAGILSQQQEQQLEEMMCGGAYDDEQYDLNNQPLPDETNVSLYDLVSQEDPTKLFGEGSTKIGEGAAGEVFVVTQLKTNNKVAIKKMPLNQQNMKLIVTEIGIMKSCRHQNIIDYIDSYLVGDSLWVAMEFMGGGCLTEILEQFNSVKLVEAQIAYVCAETLKGLAYIHSQHRIHRDIKSDNILLGSDGSVKLADFGYAAQLTKSKQKRVTIVGTPYWMAPELIRGQNYDRKVDIWSLGIMAMEMAESEPPYMSFPPLRALFLITTKGIPDLKDQNKWSDDFKDFVKKCLDKDVENRPEAKVLLNHPFLKTACNSNGLVPAIMEAKKAKEAHSKFSIH
Protein: Tubulin beta-3 chain (Tubulin beta-4 chain) (Tubulin beta-III) (Q13509)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. TUBB3 plays a critical role in proper axon guidance and maintenance. Binding of NTN1/Netrin-1 to its receptor UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion. Plays a role in dorsal root ganglion axon projection towards the spinal cord.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:34996871, ECO:0000269|PubMed:35482892}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9ERD7}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9ERD7}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9ERD7}.
Interaction partners:
- Tubulin alpha-1A chain
- Tubulin alpha-1B chain
- Tubulin alpha-4A chain
- Tubulin alpha-1C chain
- Microtubule-associated protein tau
- Tubulin alpha chain-like 3
- Tubulin alpha-8 chain
- Tubulin alpha-3C chain
- Tubulin alpha-3E chain
- Microtubule-associated protein RP/EB family member 3
Sequence:
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYVPRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEMYEDDEEESEAQGPK
Protein: E3 ubiquitin-protein ligase makorin-2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase makorin-2) (Q9ERV1)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Promotes the polyubiquitination and proteasome-dependent degradation of RELA/p65, thereby suppressing RELA-mediated NF-kappa-B transactivation and negatively regulating inflammatory responses. Plays a role in the regulation of spermiation and in male fertility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28378844}. Nucleus {ECO:0000269|PubMed:28378844}.
Interaction partners:
Sequence:
MSTKQVTCRYFMHGVCREGSQCLFSHDLANSKPSTICKYYQKGYCAYGARCRYDHTKPPAAAGGAVGPAPNPSPSSGLHSPHPSPDIATSVMRTHSNEPGKREKKTLVLRDRNLTGLAEDKTPPSKVNNPGGCSDPQTSPEMKPHSYLDAIRTGLDDLEASSSYSNEPQLCPYAAAGECRFGDACVYLHGDMCEICRLQVLHPFDPEQRKAHEKMCMSTFEHEMEKAFAFQASQDKVCSICMEVILEKASASERRFGILSNCSHTYCLSCIRQWRCAKQFENPIIKSCPECRVISEFVIPSVYWVEDQNKKNELIEAFKQGMGKKACKYFEQGKGTCPFGSKCLYRHAYPDGRLAEPEKPRKQLSSEGTVRFFNSVRLWDFIENRETRQVPSTDDVDVTELGDLFMHLSGVESSEP
Protein: RING-CH-type domain-containing protein (Q57V79)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Endosome {ECO:0000256|ARBA:ARBA00004177}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004656}.
Interaction partners:
Sequence:
MEHLKIFPRLGRTLLVITVFLMAFPPGVAKCQKQRYQKPQLEKVGEGNQKTPKVRNRLSGTLSSGDVRTFSGIRSVLHKGGDGIKYKTQRRDYTTTSKPTGAQFLTAQTAQLEEGTQQDKANQTDINIRVYDMRKQKEINKFRQSTGVYLVNAVPGSTKYLEFESSTRDEISVVTQLLSNRYDTDVPADNCVGYFVNVEIRNSSEVNLTALTTPKDPPAVGEEDKNGSSTSTHGGEGENYELEGGWKFLWSVIATMLDTSSFCDLLPKVMLRVEPDPEPQSYVVLFQSHIGMGLGSQRRGKDCLLRVFVTRTPKERERRMQNTFALGVPLLILLLMAPMTFMHAHLLPDFMADIDVVFWLIYPAVAMRNGLACLFVYLYRVSREAYVARREERRQRQLEEQHRQIMEQEALVLADVTMNNVDKNNKGSSSNAKLSHQPLAHMSQTPQGAEEGFDGAEGGAHAEKHKKQEGWNANADQRNREGPSGAAVAQVEHAPLLSSRKALTAEDVVVMDDMVDMDLDGDDEAHGGLRRPLITGQKKVKKATGSVEGEFAGSTVGEGSAPATRSEEADGSNDAEPAAVVGQGKAVSTRSAVSGGAPAKSDCEEEDDERICRICRDDETDEKLISACECIGSVRWIHVSCLDRWRIESTKRNLHNVNCCEICKKPFHVPISRHAQIMRNLKSVSRGLLLVFSIIFTFITATIGQRVTLGEMTCRTPWHTVSYSTMFEIDGVVLTVFMQFTLTMLAVYAFALVSARFHADPETLEHLLTFQTFPPFWTMRNTGMIVLIFAGGVLQALALGLLTKLFIYRTSNIVWSWEASPCIGAVLFLGYVAMGTLVSVKVHSWAQRRRLRQARRVQVRNVEEQGDQQRQLP
Protein: N-acetylgalactosamine kinase AgaK (GalNAc kinase) (EC 2.7.1.-) (N-acetylglucosamine kinase) (GlcNAc kinase) (EC 2.7.1.59) (A0KYQ6)
Organism: Shewanella sp. (strain ANA-3)
Function: Involved in the pathway of N-acetyl-D-galactosamine degradation. Catalyzes the phosphorylation of N-acetyl-D-galactosamine (GalNAc) to yield D-galactosamine 6-phosphate (GalN-6-P). It can also phosphorylate N-acetylglucosamine (GlcNAc).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:22711537}.
Interaction partners:
- N-acetylgalactosamine-6-phosphate deacetylase
- PTS system, glucose-like IIB subunint
- N-acetylgalactosamine-6-phosphate deacetylase
- beta-N-acetylhexosaminidase
- Beta-hexosaminidase
- chitinase
- Aminoglycoside phosphotransferase
- D-galactosamine-6-phosphate deaminase AgaS
- Glycosyl hydrolase family 109 protein 2
- Tagatose-bisphosphate aldolase noncatalytic subunit
Sequence:
MYYGLDIGGTKIELAIFDTQLALQDKWRLSTPGQDYSAFMATLAEQIEKADQQCGERGTVGIALPGVVKADGTVISSNVPCLNQRRVAHDLAQLLNRTVAIGNDCRCFALSEAVLGVGRGYSRVLGMILGTGTGGGLCIDGKLYLGANRLAGEFGHQGVSANVACRHQLPLYVCGCGLEGCAETYVSGTGLGRLYQDIAGQTADTFAWLNALRCNDPLAIKTFDTYMDILGSLMASLVLAMDPDIIVLGGGLSEVEEILAALPQATKAHLFDGVTLPQFKLADFGSASGVRGAALLGHGLDAGISYEA