wanglab/gogpt-training-data huggingface dataset:
Protein: Phenylalanine/tyrosine ammonia-lyase 1 (FuPAL1) (EC 4.3.1.25) (P0DO55)
Organism: Fritillaria unibracteata (Sichuan fritillary)
Function: Key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton (By similarity). Can use L-phenylalanine (L-Phe) as substrate more efficiently than L-tyrosine (L-Tyr). Promotes drought tolerance by inducing the biosynthesis and accumulation of salicylic acid (SA) and lignin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:35643154}.
Interaction partners:
Sequence:
MAHIGNGNGNGNGFANGNGNGNGAAGLCLHPDPLNWRAAADALTGSHLDEVRRMAAEFRKPVVRLEGASLSISQVAAVAAGREVKVELSEEARGRVKASSDWVMDSMGKGTDSYGVTTGFGATSHRRTKEGGALQKELIRFLNAGIFGAGPEDGQTLPPTTTRAAMLVRVNTLLQGYSGIRFEILEAISSLLNHNVTPILPLRGTISSSGDLVPLSYIAGVLIGRPNSKSIGPDGTYVDATEAFRLAGISGGFFELQPKEGLAMVNGTAVGSGLASMVLFEANIIAVLAEVISAIFCEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILAGSSYMKMAAKIHEQDPLQKPKQDRYALRTSPQWLGPLIEVIRTSTKSIEREINSVNDNPLIDVSRNKAIHGGNFQGTPIGVSMDNTRLVLAAIGKLMFAQISELVNDFYNNGLPSNLSGGRNPSLDYGFKGAEIAMASYCSELQFLANPVTNHVQSAEQHNQDVNSLGLISARKTAEAVEILKLMSSTFLVALCQAVDLRHLEENLKAAVKNTVSQVAKRVLTMGVNGELHPSRFCEKDLIKVIDREYVFAYADDPCSATYPLMQKLRGVLVEHALVNGDKEKEMGTSIFQKITAFEEELKATLPKEVEGVRVAFDNGTNVIPNRISECRSYPLYKFVREELGAGYLTGEKVVSPGEEFNKVFVAMNQWKLIDPLLECLSDWNGAPLPIC
Protein: Zinc finger protein with KRAB and SCAN domains 1 (Zinc finger protein 139) (Zinc finger protein 36) (Zinc finger protein KOX18) (P17029)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- Zinc finger and SCAN domain-containing protein 32
- NADPH oxidase 4
- Zinc finger protein 397
- Zinc finger protein with KRAB and SCAN domains 4
- Zinc finger protein 24
- SCAN domain-containing protein 1
- Zinc finger and SCAN domain-containing protein 20
Sequence:
MMTAESREATGLSPQAAQEKDGIVIVKVEEEDEEDHMWGQDSTLQDTPPPDPEIFRQRFRRFCYQNTFGPREALSRLKELCHQWLRPEINTKEQILELLVLEQFLSILPKELQVWLQEYRPDSGEEAVTLLEDLELDLSGQQVPGQVHGPEMLARGMVPLDPVQESSSFDLHHEATQSHFKHSSRKPRLLQSRALPAAHIPAPPHEGSPRDQAMASALFTADSQAMVKIEDMAVSLILEEWGCQNLARRNLSRDNRQENYGSAFPQGGENRNENEESTSKAETSEDSASRGETTGRSQKEFGEKRDQEGKTGERQQKNPEEKTRKEKRDSGPAIGKDKKTITGERGPREKGKGLGRSFSLSSNFTTPEEVPTGTKSHRCDECGKCFTRSSSLIRHKIIHTGEKPYECSECGKAFSLNSNLVLHQRIHTGEKPHECNECGKAFSHSSNLILHQRIHSGEKPYECNECGKAFSQSSDLTKHQRIHTGEKPYECSECGKAFNRNSYLILHRRIHTREKPYKCTKCGKAFTRSSTLTLHHRIHARERASEYSPASLDAFGAFLKSCV
Protein: SPRY domain-containing SOCS box protein 3 (SSB-3) (Q6PJ21)
Organism: Homo sapiens (Human)
Function: May be a substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:38418882}. Note=Nuclear SPSB3 levels increase during interphase. {ECO:0000269|PubMed:38418882}.
Interaction partners:
- Elongin-C
- Cullin-5
- Cytokine-inducible SH2-containing protein
- Elongin-B
Sequence:
MARRPRNSRAWHFVLSAARRDADARAVALAGSTNWGYDSDGQHSDSDSDPEYSTLPPSIPSAVPVTGESFCDCAGQSEASFCSSLHSAHRGRDCRCGEEDEYFDWVWDDLNKSSATLLSCDNRKVSFHMEYSCGTAAIRGTKELGEGQHFWEIKMTSPVYGTDMMVGIGTSDVDLDKYRHTFCSLLGRDEDSWGLSYTGLLHHKGDKTSFSSRFGQGSIIGVHLDTWHGTLTFFKNRKCIGVAATKLQNKRFYPMVCSTAARSSMKVTRSCASATSLQYLCCHRLRQLRPDSGDTLEGLPLPPGLKQVLHNKLGWVLSMSCSRRKAPVSDPQAATSAHPSSREPRPCQRKRCRRT
Protein: Epididymis secretory protein Li 50 (Ubiquitin B) (Q5U5U6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC
Protein: Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB) (Q99650)
Organism: Homo sapiens (Human)
Function: Associates with IL31RA to form the IL31 receptor. Binds IL31 to activate STAT3 and possibly STAT1 and STAT5. Capable of transducing OSM-specific signaling events.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Interleukin-31
- Oncostatin-M
- Interleukin-31 receptor subunit alpha
- Tyrosine-protein kinase JAK1
- Interleukin-6 receptor subunit beta
- Interleukin-11
- Cardiotrophin-1
- Interleukin-6
- Leukemia inhibitory factor
- Ciliary neurotrophic factor
Sequence:
MALFAVFQTTFFLTLLSLRTYQSEVLAERLPLTPVSLKVSTNSTRQSLHLQWTVHNLPYHQELKMVFQIQISRIETSNVIWVGNYSTTVKWNQVLHWSWESELPLECATHFVRIKSLVDDAKFPEPNFWSNWSSWEEVSVQDSTGQDILFVFPKDKLVEEGTNVTICYVSRNIQNNVSCYLEGKQIHGEQLDPHVTAFNLNSVPFIRNKGTNIYCEASQGNVSEGMKGIVLFVSKVLEEPKDFSCETEDFKTLHCTWDPGTDTALGWSKQPSQSYTLFESFSGEKKLCTHKNWCNWQITQDSQETYNFTLIAENYLRKRSVNILFNLTHRVYLMNPFSVNFENVNATNAIMTWKVHSIRNNFTYLCQIELHGEGKMMQYNVSIKVNGEYFLSELEPATEYMARVRCADASHFWKWSEWSGQNFTTLEAAPSEAPDVWRIVSLEPGNHTVTLFWKPLSKLHANGKILFYNVVVENLDKPSSSELHSIPAPANSTKLILDRCSYQICVIANNSVGASPASVIVISADPENKEVEEERIAGTEGGFSLSWKPQPGDVIGYVVDWCDHTQDVLGDFQWKNVGPNTTSTVISTDAFRPGVRYDFRIYGLSTKRIACLLEKKTGYSQELAPSDNPHVLVDTLTSHSFTLSWKDYSTESQPGFIQGYHVYLKSKARQCHPRFEKAVLSDGSECCKYKIDNPEEKALIVDNLKPESFYEFFITPFTSAGEGPSATFTKVTTPDEHSSMLIHILLPMVFCVLLIMVMCYLKSQWIKETCYPDIPDPYKSSILSLIKFKENPHLIIMNVSDCIPDAIEVVSKPEGTKIQFLGTRKSLTETELTKPNYLYLLPTEKNHSGPGPCICFENLTYNQAASDSGSCGHVPVSPKAPSMLGLMTSPENVLKALEKNYMNSLGEIPAGETSLNYVSQLASPMFGDKDSLPTNPVEAPHCSEYKMQMAVSLRLALPPPTENSSLSSITLLDPGEHYC
Protein: Auxin-responsive protein IAA6 (Indoleacetic acid-induced protein 6) (Q8LQ74)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transport inhibitor response 1-like protein Os05g0150500
- Auxin response factor 11
- Auxin response factor 7
- Auxin response factor 3
- Auxin response factor 9
- Auxin response factor 15
- Auxin response factor 2
- Auxin response factor 14
- Auxin response factor 1
- Transport inhibitor response 1-like protein Os04g0395600
Sequence:
MEEGSNKREGLPPQLLDLIPDEKEWKLREALGLGRSRNAGFDGEEDKKLDLKLGLPGFIEDDEAETLRDYRLQQESPSLSLSFFPKHSKTTSSTTTTTGAKRGFIDTVEDKTEGYNDQKQQARAGCGKELAVEEMIAAVSERKKGCCPPPPPPHGAPATPARNRPQTQGRGAAAPVVGWPPIRSFRRNLASSSSSKHSPEPQNDNANAKVTLTCKKNPLVKINMDGIPIGRKIDLAAYNSYDGLSSAVKQLFHGFLQAQKDQTNAQIAQQGADDKIFYQLLDGSGEYTLVYEDSEGDRMLVGDVPWKVFVSTAKRLRVLRSSELSHTLIGATARV
Protein: Mu-conotoxin Lt5d (Lt5.4) (Q1A3R1)
Organism: Conus litteratus (Lettered cone)
Function: Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin inhibits tetrodotoxin(TTX)-sensitive sodium channels, but does not affect TTX-resistant sodium channels. Reduces the amplitude of currents without changing the activation and inactivation kinetics of currents.
Subcellular location: Secreted {ECO:0000269|PubMed:17961831}.
Interaction partners:
Sequence:
MRCLPVFIILLLLIPSAPSVDAQPTTKDDVPLASLHDNAKRALQMFWNKRDCCPAKLLCCNP
Protein: C-C chemokine receptor type 3 (C C CKR3) (C-C CKR-3) (CC-CKR-3) (CCR-3) (CCR3) (CKR 3) (CKR3) (Eosinophil eotaxin receptor) (CD antigen CD193) (P51677)
Organism: Homo sapiens (Human)
Function: Receptor for C-C type chemokine. Binds and responds to a variety of chemokines, including CCL11, CCL26, CCL7, CCL13, RANTES(CCL5) and CCL15. Subsequently transduces a signal by increasing the intracellular calcium ions level. In addition acts as a possible functional receptor for NARS1.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- C-C motif chemokine 26
- C-C motif chemokine 7
- C-C motif chemokine 5
- Eotaxin
- C-C motif chemokine 13
- C-C motif chemokine 24
- C-C chemokine receptor type 5
- C-C motif chemokine 4
- C-C motif chemokine 3
- C-C motif chemokine 2
Sequence:
MTTSLDTVETFGTTSYYDDVGLLCEKADTRALMAQFVPPLYSLVFTVGLLGNVVVVMILIKYRRLRIMTNIYLLNLAISDLLFLVTLPFWIHYVRGHNWVFGHGMCKLLSGFYHTGLYSEIFFIILLTIDRYLAIVHAVFALRARTVTFGVITSIVTWGLAVLAALPEFIFYETEELFEETLCSALYPEDTVYSWRHFHTLRMTIFCLVLPLLVMAICYTGIIKTLLRCPSKKKYKAIRLIFVIMAVFFIFWTPYNVAILLSSYQSILFGNDCERSKHLDLVMLVTEVIAYSHCCMNPVIYAFVGERFRKYLRHFFHRHLLMHLGRYIPFLPSEKLERTSSVSPSTAEPELSIVF
Protein: Grainyhead-like protein 1 homolog (Grainyhead-like transcription factor 1) (A0A286YAF2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU01313}.
Interaction partners:
Sequence:
MSQEHENKRAVLVLPNDPAYNQRRPYTSEDEAWKSFLENPLTAATKAMMSINGDEDSAAALGLLYDYYKVPRDKRTISQQKTDVLGSDVDPNKRNMLTPLQETSMQLGDNRIQVLKGVPLNIVLPGNQHVQDKRGLFPSPDTTVTVSIAPVASNSVKTEGPSHGFSVTVPNPHCAEPDSHTVVFDRQLPHNQFSPNTQPRTPDSTFPENPDVFSFPGDLQLRMGPITQDDYGTFDTVSGNNFEYILEASKSLRQKSGDGTMTYLNKGQFYPITLRETDNGKLLQGPICKVRSVVMVVFGEEKSRDDQLKHWKYWHSRQHTAKQRCIDIADYKESFNTISNIEEISYNAISFTWDISEEAKIFISVNCLSTDFSSQKGVKGLPLNIQIDTYSYNNRSNKPIHRAYCQIKVFCDKGAERKIRDEERKQSRRKVGADVKVPLLHKRTDMTVFRTLTDFETQPVLFIPDIHFSTFQRHAFTAEDSEEGSAMKRLPYTEEEFGSPPNKLARMDEPKRVLLYVRRETEEVFDALMLKTPTLKGLVEAISEKYEVSLEKIGKVYKKCKKGILVNMDDNIIKHYSNEDTFQIQMEEMGGMIKLTLTEIE
Protein: Prohibitin (A8W340)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU366048}.
Interaction partners:
Sequence:
MAAKVFESIGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIFTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAEDIAYQLSRSRNITYLPAGQSVLLQLPQ
Protein: Secretory 31, isoform C (A0A0B4LEY1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MKIKELQKTVNIAWSPAQQQQILLAAGTAAQQFDSNANSTLELYSPNFSDATYDLELRASVSSQYKFQKLIWSPVGPHPSGLIVGGCEAGQINIYSADKLLAGKEEPLLKRQDKHTGAVSGLDFNPFQNNLLASCASESEILIWDLNNPETSMSPGTKTQPLEDVKNVAWNRQVQHILASVFSTRCVIWDLRKSQQIIKLSDSQSRVRWHAIEWHPEAATQVWLASEDDQAPVVQLWDLRYATAPAKTYQIHERGVLGMSWCLQDNDLMVSCGKDNRIYCWNPNTKIPEGEILSEVATTASWYSDVQFCPRNPALIASASLEGAVSIYSLHGGTHHLVQTANKIADSFPGMDQFAQEPIPQQATQVVYHDLAHAPKWMKRPCGVAFGFGGKLVSFNGTSKTVKVQQLTTESALVDRANALERSLVDANYSDYCRQRADETPDQHGRYIWYFIKANFELNPKEEMLNLLGYNKDDIDSKFNKFIKETDGNSHSDVDTLTTRISTLTHSDSSEVECDQSTNYSTDNSTQDNKFDGNAIDSQNHNDFATPPRPQFKVPSGDHSDSLIAEAILTGNVDAAVELCLEAQRIPEALIIASTAGIETLNRTQTRYLLQQKNELSHVISALVSRDWLDFVNRCTVDSWKEALVAALKHSERKVVDICERLGDRLLSECASSAEFTRNAMLCYICAGSIDKLVTAWYQLKRLEQQNPGYKPNTTELQDLAEMVMLMCKSLEQQGISVDLAGRFAGFLTEYGGLLASQGALTAALQYITTLGGGAAASESDVLQSLRDRINNAVNLDYTQPQAAVAAAPHGYQPTRGRGSFSQPQPSAPMPYGQPPNQYAQPSWPAQVPPLQTSYPGAQQPQAPPQIFNPQPVKPEPLAQPPRPLSNASSSGGPPPAGGASSSGGSGLSGRSKYVLDPSVAAPTSSYGMPYNPVPAPVPSAVPFGGGGVPGPAPQPASVPTYNSNAFNTNPIAAAQPYNPSPLMPAQQNQFVPGVNPIETMPPPAVPPVIQNVQRNPTPPPGWNDPPALKSSRAPKPKPVVEPSAAIFHPLFPVDPNQNQNGYVDPSQYQHAAPLGGVPNTYYNPAAFNNNPQQQQQHQQSYLQPQQPAPGIQQPNWQGQQQTIGYTEQPAPIQQQRQPAPPKEKPPLPEEYIYLQTVLEELKNRCLGATNDPRTKRKFVDVVKRLENLYDCLRDGKLTPTTVQYLNQIVQYIQISDYANAMEIHTQIAFGTDFAQCAGFMQGLKVLLQSASELQLVLR
Protein: ATP synthase subunit 9, mitochondrial (Lipid-binding protein) (P16000)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Subcellular location: Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ATP synthase subunit a
- ATP synthase subunit d
- ATP synthase subunit gamma
- ATP synthase subunit beta
- ATP synthase subunit 5
- Mitochondrial F1F0-ATP synthase g subunit, putative
- ATP synthase subunit 4
- ATP synthase subunit alpha
- ATP synthase subunit alpha
- ATP synthase subunit delta, mitochondrial
Sequence:
MAASRVFAQRLASTMKVARPAARIQARTLTTQRMATPFQTIKRQQPSMIQASARQAFAARRQYSSEIADAMVQVSQNIGMGSAAIGLGGAGIGIGVVFGSLLLAVSRNPALRGQLFSYAILGFAFVEAIGLFDLMVAMMCKYV
Protein: Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Peptidase M) (O60085)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Methionine aminopeptidase 1
- Sphingolipid delta
- 60S ribosome subunit biogenesis protein nip7
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS3
- Guanine nucleotide-binding protein alpha-1 subunit
Sequence:
MTSATTTEATAKDLQEKLSLKENDVVEDDGKVEENDAAEEGASNGEKKKKKKKKSSKKKKTPQEQTNPPTVGLSKIFVNKKYPVGEVCDYAEDNLWRTTDEEKRALDRQNFDQYNDLRRAAEVHRQARQYAQSVIKPGMSMMDVVNTIENTTRALVEEDGLKSGIGFPTGVSLNHCAAHYTPNAGDTTILKEKDVMKVDIGVHVNGRIVDSAFTMSFDPQYDNLLAAVKAATNKGIEEAGIDARLNEIGEAIQEVMESYEVEINGKTHQVKSIRNLCGHNLDPYIIHGGKSVPIVKGGEEIKMEEGEIFAIETFGSTGRGVVHEDMECSHYAKIPDAGHIPLRLPRAKALLNTITQNFGTLPFCRRYLDRIGESKYLLALNNLVSAGIVQDYPPLCDIRGSYTAQFEHTIILHPTQKEVVSRGDDY
Protein: Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau) (P29172)
Organism: Bos taurus (Bovine)
Function: Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.
Subcellular location: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, axon. Cytoplasm {ECO:0000250|UniProtKB:P10636}. Cell projection, dendrite {ECO:0000250|UniProtKB:P10636}. Secreted {ECO:0000250|UniProtKB:P10636}. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion.
Interaction partners:
Sequence:
MAEPRQEFDVMEDHAQGDYTLQDQEGDMDPGLKESPLQTPADDGSEEPGSETSDAKSTPTAEDATAPLVDEGAPGEQAAAQAPAEIPEGTAAEEAGIGDTSNLEDQAAGHVTQARMVSKGKDGTGPDDKKTKGADGKPGTKIATPRGAAPPGQKGQANATRIPAKTTPTPKTSPATMQVQKKPPPAGAKSERGESGKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSAAKSRLQAAPGPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
Protein: Uncharacterized protein YaiL (P51024)
Organism: Escherichia coli (strain K12)
Interaction partners:
- 3-
- Cyclic di-GMP phosphodiesterase PdeL
- Uncharacterized ABC transporter permease YbbP
Sequence:
MAKLTLQEQLLKAGLVTSKKAAKVERTAKKSRVQAREARAAVEENKKAQLERDKQLSEQQKQAALAKEYKAQVKQLIEMNRITIANGDIGFNFTDGNLIKKIFVDKLTQAQLINGRLAIARLLVDNNSEGEYAIIPASVADKIAQRDASSIVLHSALSAEEQDEDDPYADFKVPDDLMW
Protein: Conserved oligomeric Golgi complex subunit 3 C-terminal domain-containing protein (H2L0S2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLAECQYAYFAKRNLLLGPILESTLANLSGTHDDSTCRLTRDACTFMLRTCDDEYRLYRQFFVTRHTEERKLSTDGRISPAMSTITSVFTSAQSPQQVHPFETFSEQMCRTLYDMLRPRIVHNPHLETLAELCTMIKIEMIENRCSLQMVASILGDDASNDQNVSGLNPRAGFVSVMSELVGDIAERIVYRAGMYAQNDIAAYRPAAGDIAYPQMLQMIRKIENEQKEQQEKEPEEGSAPATAIDQHCLWYPTVRRTVMCLSKIFPCLDIGVFHSLARDMLFSCIDSLETASKAIMESPAPAKGWSKKLDAHLFVVKHLLILREQTAPYRQNVLSFRSDSLNTKDFSIDFSKFTNVLFDSKSKWFELSTDNALLELITTVPIEMREQEGDSRRVLDQQLRASTFRLAHEASLLMIRDLADWIEIAEDERMKEGFQLSGHPKLAAGVLKDVSAVAYRNVGTKFTEVNIYSNSTVLYII
Protein: Nurim (Nuclear envelope membrane protein) (Nuclear rim protein) (H0Y6T6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004473}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004473}.
Interaction partners:
Sequence:
XESGREATGEGDLSSKLGTQGLEFWRGGRVRTEGAEKGGDRSILNARQGWLAALQDRSILAPLAWDLGLLLLFVGQHSLMAAERVKAWTSRYFGVLQRSLYVACTALALQLVMRYWEPIPKGPVLWEARAEPWATWVPLLCFVLHVISWLLIFSILLVFDYAELMGLKQVYYHVLGLGEPLALKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLAFLLTLYLGLAHGLDQQDLRYLRAQLQRKLHLLSRPQDGEAE
Protein: Neuregulin 1 (Pro-neuregulin-1, membrane-bound isoform isoform IIb12) (A0A0R4IBM0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Erb-b2 receptor tyrosine kinase 3a.
- Receptor protein-tyrosine kinase.
- Receptor protein-tyrosine kinase.
- Receptor protein-tyrosine kinase.
- Receptor protein-tyrosine kinase.
- Erb-b2 receptor tyrosine kinase 3b.
- Epidermal growth factor.
- Neuregulin 2
- Periostin, osteoblast-specific factor a.
- Epidermal growth factor receptor precursor.
Sequence:
MAILPGRSSSLTVSVLYGAAVCLSLWTRVVRCGSFACSPPGASVQELARRSGVVFEGKLQEEERAERNWTETPMNASRQVRVRVQQVWQLKAGGLIKDSVVSLVWFEGGRCFQLNTGIRYMFFIEPTNDTSVFTAVFPPVETKRTVRKDVSQVLCQDCAEPKLKNLRSVTVEDGKKTVLKCEILAGNPAPNVKWYKNGKELTGKNKPKSIKIKKKKQGKISELLIRKSTEGDAGLYTCEAVNSLGKTNTTANLFIINTATSTTPSAKTSSHVTPCNESEKEYCVNHGKCFTLEVTPGNIRRLCRCPNEFTGDRCQHYVMASFYKHLGIEFMEAEELYQKRVLTITGICIALLVVGIMCVVAYCKTKKQRKKLHDRLRQSLRERNAAAKGPQHPHPPPENLQLVNHYMPTNPVPAHMTDKEAETSLSTNEFTSPTHPSTAITHSSSQCWSNGKAESVVSDSHAVLMKPSAENCQHGTPSHRGRLNATGGVHQLNDYLKNSREAQGSNRDSPYSERYVSAMTTPTRLSPVGLLSPVTPSSPPSEMSAPLSSLATSVPSMLTSPSGEEERPLLFRTPPILRDKSASTQGRKSGHNLRNSAHYNHGLDIPSPPPSPLHIEEEIDCLEQYKSTSVPSSAPHSPSAARTQPSGQAAPEQAVSGSNSESSSSESETEDERVGEDTPFLGLQNPLAAGSLVLDGLEGSRTNPALHLSPQHELQNRLTAVMANQDPIAV
Protein: Casein kinase II subunit alpha' (CK II alpha') (EC 2.7.11.1) (P19784)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O54833}. Cytoplasm {ECO:0000250|UniProtKB:O54833}. Note=Interaction with SIRT6 prevents translocation into the nucleus. {ECO:0000250|UniProtKB:O54833}.
Interaction partners:
- Casein kinase II subunit beta
- Casein kinase II subunit alpha
- Casein kinase II subunit beta
- Pleckstrin homology domain-containing family O member 1
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Kinesin heavy chain isoform 5C
- Catenin beta-1
- Cellular tumor antigen p53
- FUN14 domain-containing protein 1
- Segment polarity protein dishevelled homolog DVL-1
Sequence:
MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCADNAVLSSGLTAAR
Protein: Growth hormone receptor type 2a (Q5I2A8)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MATSHILFICLVLILPVLSQEPPTSKQALFQIRPQITGCVSHDMNTFRCRWNVGVFQNLTEPRDLRIFYYINDRNISPKEWGECPRYVDRTNECFFNESYTKVWITYSVQLRSGDQDILYDEVIFTVEDIVEPDPPIALNWTLLNVGLTGSHFDIMLSWEPPHSADVSMGWMTLQYEVQYREVNSTLWRTVDLDKGMQRSLYGLRTNTDNEVRVRCKTLASRNFGEFSDSIFIHIPTKESRLPVTVLLVFAALGLAVILMLLIYSQQQKFMVILLPPIPGPKIKGIDPELFKKGNLAELTSILGGIPDLRPDLYSDDPWVEFIELDMEEPNDRLTVLDTHCLMDHCASSDCPPITIGFRDDDSGRASCCDPDLPDPEAPFHSLLPNTSRALEPSCLASTKASSPVQTPTTEDSPWASPGREDLYTQVNEVRLTGEVLLTHEEQRNVDENSEKDEKEKEKEKKRNEFQLLVVNADVGGYTSELDAGKMSARLPTGRASQPAPTEDSSLVQGQPFGEYQSLYFEAEMPPIPPASPVSPLLPVSAYTMVEGVDRQNSLLLKPGPTPAPQPDVTKLPLPTPTPEGYLTPDLLGNITP