wanglab/gogpt-training-data huggingface dataset:
Protein: Vertnin (Q9H8Y1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:E1CHH8}.
Interaction partners:
- Zinc finger and SCAN domain-containing protein 10
- Prospero homeobox protein 2
- Synapse differentiation-inducing gene protein 1-like
Sequence:
MTSRNQLVQKVLQELQEAVECEGLEGLIGASLEAKQVLSSFTLPTCREGGPGLQVLEVDSVALSLYPEDAPRNMLPLVCKGEGSLLFEAASMLLWGDAGLSLELRARTVVEMLLHRHYYLQGMIDSKVMLQAVRYSLCSEESPEMTSLPPATLEAIFDADVKASCFPSSFSNVWHLYALASVLQRNIYSIYPMRNLKIRPYFNRVIRPRRCDHVPSTLHIMWAGQPLTSHFFRHQYFAPVVGLEEVEAEGAPGVAPALPALAPLSSPAKTLELLNREPGLSYSHLCERYSVTKSTFYRWRRQSQEHRQKVAARFSAKHFLQDSFHRGGVVPLQQFLQRFPEISRSTYYAWKHELLGSGTCPALPPREVLGMEELEKLPEEQVAEEELECSALAVSSPGMVLMQRAKLYLEHCISLNTLVPYRCFKRRFPGISRSTYYNWRRKALRRNPSFKPAPALSAAGTPQLASVGEGAVIPWKSEAEEGAGNATGEDPPAPGELLPLRMPLSRWQRRLRRAARRQVLSGHLPFCRFRLRYPSLSPSAFWVWKSLARGWPRGLSKLQVPVPTLGKGGQEAEEKQEKEAGRDVTAVMAPPVGASSEDVEGGPSREGALQEGATAQGQPHSGPLLSQPVVAAAGGRDGRMLVMDMIATTKFKAQAKLFLQKRFQSKSFPSYKEFSALFPLTARSTYYMWKRALYDGLTLVDG
Protein: Growth hormone receptor 2 (B5KME7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
AEEKAKEGKEKEKPRKEFQLLVVNADGGGYTTELDAGKMSAKLPTGRGSQPAPTEDSRLVQGQPFGEYQSLYFEAEMPPIPPASPVSSLLPLSVYTMVEGVDRQNSLLLKPSPPPAPQPVLTKLPLPTPTPEGYLTPDLLGNVTP
Protein: MICOS complex subunit MIC60 (Mitofilin) (H7C463)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363000}; Single-pass membrane protein {ECO:0000256|RuleBase:RU363000}.
Interaction partners:
Sequence:
XIQSGPLKISSVSEVMKESKQPASQLQKQKGDTPASATAGDTLSVPAPAVQPEESLKTDHPEIGEGKPTPALSALAKSLEDALRQTASVTLQAIAAQNAAVQAVNAHSNILKAAMDNSEIAGEKKSAQWRTVEGALKERRKAVDEAADALLKAKEELEKMKSVIENAKKKEVAGAKPHITAAEGKLHNMIVDLDNVVKKVQAAQSEAKVVSQYHELVVQARDDFKRELDSITPEVLPGWKGMSVSDLADKLSTDDLNSLIAHAHRRIDQLNRELAEQKATEKQHITLALEKQKLEEKRAFDSAVAKALEHHRSEIQAEQDRKIEEVRDAMENEMRTQLRRQAAAHTDHLRDVLRVQEQELKSEFEQNLSEKLSEQELQFRRLSQEQVDNFTLDINTAYARLRGIEQAVQSHAVAEEEARKAHQLWLSVEALKYSMKTSSAETPTIPLGSAVEAIKANCSDNEFTQALTAAIPPESLTRGVYSEETLRARFYAVQKLARRVAMIDETRNSLYQYFLSYLQSLLLFPPQQLKPPPELCPEDINTFKLLSYASYCIEHGDLELAAKFVNQLKGESRRVAQDWLKEARMTLETKQIVEILTAYASAVGIGTTQVQPE
Protein: UDP-glycosyltransferase 73B4 (EC 2.4.1.-) (Flavonol 3-O-glucosyltransferase UGT73B4) (EC 2.4.1.91) (Q7Y232)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses quercetin 3-O-glucosyltransferase and low 7-O-glucosyltransferase activities in vitro. Also active in vitro on benzoates and benzoate derivatives. Can detoxify the explosive 2,4,6-trinitrotoluene in plant by forming O- or C-glucose conjugates.
Interaction partners:
- 2-nitropropane dioxygenase-like protein
- Cytochrome P450 71B19
Sequence:
MNREQIHILFFPFMAHGHMIPLLDMAKLFARRGAKSTLLTTPINAKILEKPIEAFKVQNPDLEIGIKILNFPCVELGLPEGCENRDFINSYQKSDSFDLFLKFLFSTKYMKQQLESFIETTKPSALVADMFFPWATESAEKIGVPRLVFHGTSSFALCCSYNMRIHKPHKKVASSSTPFVIPGLPGDIVITEDQANVTNEETPFGKFWKEVRESETSSFGVLVNSFYELESSYADFYRSFVAKKAWHIGPLSLSNRGIAEKAGRGKKANIDEQECLKWLDSKTPGSVVYLSFGSGTGLPNEQLLEIAFGLEGSGQNFIWVVSKNENQVGTGENEDWLPKGFEERNKGKGLIIRGWAPQVLILDHKAIGGFVTHCGWNSTLEGIAAGLPMVTWPMGAEQFYNEKLLTKVLRIGVNVGATELVKKGKLISRAQVEKAVREVIGGEKAEERRLRAKELGEMAKAAVEEGGSSYNDVNKFMEELNGRK
Protein: Carotenoid-cleaving dioxygenase, mitochondrial (EC 1.13.11.-) (EC 1.13.11.71) (B-diox-II) (Beta,beta-carotene 9',10'-oxygenase) (Beta-carotene dioxygenase 2) (Q9BYV7)
Organism: Homo sapiens (Human)
Function: Broad specificity mitochondrial dioxygenase that mediates the asymmetric oxidative cleavage of carotenoids. Cleaves carotenes (pure hydrocarbon carotenoids) such as all-trans-beta-carotene and lycopene as well as xanthophylls (oxygenated carotenoids) such as zeaxanthin, lutein and beta-cryptoxanthin at both the 9,10 and the 9',10' carbon-carbon double bond. Through its function in carotenoids metabolism regulates oxidative stress and the production of important signaling molecules.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q99NF1}.
Interaction partners:
Sequence:
MFFRVFLHFIRSHSATAVDFLPVMVHRLPVFKRYMGNTPQKKAVFGQCRGLPCVAPLLTTVEEAPRGISARVWGHFPKWLNGSLLRIGPGKFEFGKDKYNHWFDGMALLHQFRMAKGTVTYRSKFLQSDTYKANSAKNRIVISEFGTLALPDPCKNVFERFMSRFELPGKAAAMTDNTNVNYVRYKGDYYLCTETNFMNKVDIETLEKTEKVDWSKFIAVNGATAHPHYDLDGTAYNMGNSFGPYGFSYKVIRVPPEKVDLGETIHGVQVICSIASTEKGKPSYYHSFGMTRNYIIFIEQPLKMNLWKIATSKIRGKAFSDGISWEPQCNTRFHVVEKRTGQLLPGRYYSKPFVTFHQINAFEDQGCVIIDLCCQDNGRTLEVYQLQNLRKAGEGLDQVHNSAAKSFPRRFVLPLNVSLNAPEGDNLSPLSYTSASAVKQADGTIWCSHENLHQEDLEKEGGIEFPQIYYDRFSGKKYHFFYGCGFRHLVGDSLIKVDVVNKTLKVWREDGFYPSEPVFVPAPGTNEEDGGVILSVVITPNQNESNFILVLDAKNFEELGRAEVPVQMPYGFHGTFIPI
Protein: GEO11329p1 (Ion transport peptide, isoform D) (Ion transport peptide, isoform F) (Ion transport peptide, isoform G) (SD05282p) (Q9W151)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MCSRNIKISVVLFLVLIPIFAALPHNHNLSKRSNFFDLECKGIFNKTMFFRLDRICEDCYQLFRETSIHRLCKKDCFDSKWFGECLKVLLIPEEEISNLQHFLRVVNGSPISFNMGPQT
Protein: Small ribosomal subunit protein mS29 (A5PLH1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MNLHKLSLRLRPAVTQKFRCLSIQSSGQELEAVAAETLSAEPNMLSVFRTSEQDPTCHSETHTGQYYTLPPTHIQKLFPHGLPPRFQMQVKTFNEGCVMVRPAALELISYLKKADYNKPPLRYVLYGQTGSGKSISLCHTLHYCYTQGWLILHVPDAHLWVKNCKEMLPSTYNPLRFDQPVQATQWLKDFKITNEHFLSKIKTTRRYVWTKRESTEEGRTLGELIDQGVNRMKSSSDVVGAVLRELRLQAGATTEGEEVFKLAVAVDGVNALWGNTTLKKEDRTMCEPEELTLIHNLRKMMKTDWRGGAILTALSQTGSLFKPRSAYLPSELLGEEGFDEMEPFVPVCVSGYNEKEFGSCYLYYLDRNWLQHPRSRSEEGKKELIFLSNRNPSILERLCAFL
Protein: Possible transcriptional regulatory protein (P95217)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- uroporphyrinogen-III C-methyltransferase
- Porphobilinogen deaminase
- Sirohydrochlorin chelatase
- Probable uroporphyrin-III C-methyltransferase HemD
- Uroporphyrinogen decarboxylase
- Probable integral membrane nitrite extrusion protein NarK3
- assimilatory sulfite reductase
- Nitrate/nitrite transporter
- Tetracyclin repressor-like C-terminal domain-containing protein
- Probable conserved membrane protein
Sequence:
MAQAHSAPLTGYRIAVTSARRAEELCALLRRQGAEVCSAPAIKMIALPDDDELQNNTEALIADPPDILVAHTGIGFRGWLAAAEGWGLANELLESLSSARIISRGPKATGALRAAGLREEWSPDSESSHEVLEYLLESGVSRTRIAVQLHGAADSWDPFPEFLGGLRFAGAQVVPIRVYRWKPAPLGGVFDHLVTGIARRQFDAVTFTSAPAAAAVLERSRELDIEDQLLAALRTDVHAMCVGPVTSRPLIRKGVPTSAPERMRLGALARHIAEELPLLGSCTFKAAGHVIEIRGTSVLVDDSVKPLSPSGMAILRALVHRPGGVVSRGDLLRVLPGDGSDTHAVDTAVLRLRTALGDKNIVATVVKRGYRLAVDSRHDDV
Protein: Carboxylesterase Culp1 (EC 3.1.1.-) (CFP21) (Cutinase-like protein 1) (Culp1) (P9WP43)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Shows esterase activity, with a preference for short- and medium-chain fatty acids. Has also weak lipase activity, but does not exhibit cutinase activity. Hydrolyzes various p-nitrophenol-linked aliphatic esters, including pNP-butyrate (C4), pNP-valerate (C5), pNP-hexanoate (C6), pNP-octanoate (C8) and pNP-decanoate (C10). Can use pNP-laurate (C12) and pNP-myristate (C14), with lower efficiency. Can also hydrolyze monocaprylin and triolein, with a slow turnover.
Subcellular location: Secreted {ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:9673225}.
Interaction partners:
- Carboxylesterase/lipase Culp6
- Immunogenic protein MPT64
- Esterase Rv0045c
Sequence:
MTPRSLVRIVGVVVATTLALVSAPAGGRAAHADPCSDIAVVFARGTHQASGLGDVGEAFVDSLTSQVGGRSIGVYAVNYPASDDYRASASNGSDDASAHIQRTVASCPNTRIVLGGYSQGATVIDLSTSAMPPAVADHVAAVALFGEPSSGFSSMLWGGGSLPTIGPLYSSKTINLCAPDDPICTGGGNIMAHVSYVQSGMTSQAATFAANRLDHAG
Protein: Mediator of RNA polymerase II transcription subunit 7 (Mediator complex subunit 7) (Q08278)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16630888}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 21
Sequence:
MSNDPGNEVSSLYPPPPPYVKFFTQSNLEKLPKYKEKKAASAKQTAPNNSNGGSEEEITCALDYLIPPPMPKNQQYRAFGSIWQVKDQLPDLESMGLTQLYKKSTENESTNYQYKIQELRKLLKSLLLNYLELIGVLSINPDMYERKVENIRTILVNIHHLLNEYRPHQSRESLIMLLEEQLEYKRGEIREIEQVCKQVHDKLTSIQDTLRTGSQSPPSSSQ
Protein: Phospholipase (EC 3.1.4.4) (Q7KML4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037868}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037868}.
Interaction partners:
Sequence:
MADAGTVGGALPPYALTNSDEEHGSGEEDASEENSNNEEGEGVFRDCTDEAVVEHHNRCLPEFQFSLVDSEYDETLAFPDSVTILSNVGDKPVLVERKETDDDEEEFDDEENNSVVLRHEIPFTSIYGPSVKFNSFQRKVFIPGREIHVRIVDTERSVTTHLLNPNLYTIELTHGPFKWTIKRRYKHFNSLHQQLSFFRTSLNIPFPSRSHKEKRTTLKATAREMADESTLKDLPSHTKVKQTSTPLRAEGRSSKIAGSNANNAMAMISPNHSSILAGLTPRRIQKKRKKKKKRKLPRFPNRPESLVTVENLSVRIKQLEDYLYNLLNISLYRSHHETLNFVEVSNVSFVPGMGIKGKEGVILKRTGSTRPGQAGCNFFGCFQKNCCVRCNYFCSDVVCGTWRNRWFFVKETCFGYIRPTDGSIRAVILFDQGFDVSTGIYQTGMRKGLQVLTNNRHIVLKCWTRRKCKEWMQYLKNTANSYARDFTLPNPHMSFAPMRANTHATWYVDGAQYMSAVADGLEAALEEIYIADWWLSPEIYMKRPALDGDYWRLDKILLRKAEQGVRVFVLLYKEVEMALGINSYYSKSTLAKHENIKVMRHPDHARGGILLWAHHEKIVVIDQTYAFMGGIDLCYGRWDDHHHRLTDLGSISTSSFSGSTRRTPSLYFTKDDTDSAFGSRKSSRNAHYDTSAKERPPSPPPDEPNTSIELKTLKPGDRLLIPSTLVSSPGETPAESGIALEGMKLNTPEMERKNVLDRLKNNAMKGARMGKDFMHRLTATETEEKSAEVYTIESEEATDHEVNLNMASGGQEVAITTSSTQILSEFCGQAKYWFGKDYSNFILKDWMNLNSPFVDIIDRTTTPRMPWHDVGLCVVGTSARDVARHFIQRWNAMKLEKLRDNTRFPYLMPKSYHQVRLNPNIQQNRQQRVTCQLLRSVSAWSCGFIEADLVEQSIHDAYIQTITKAQHYVYIENQFFITMQLGMGVPGAYNNVRNQIGETLFKRIVRAHKERKPFRVYVIMPLLPGFEGDVGGSTGIAVRAITHWNYASISRGRTSILTRLQEAGIANPENYISFHSLRNHSFLNNTPITELIYVHSKLLIADDRVVICGSANINDRSMIGKRDSEIAAILMDEEFEDGRMNGKKYPSGVFAGRLRKYLFKEHLGLLESEGSSRSDLDINDPVCEKFWHGTWRRISMQNTEIYDEVFKCIPTDFVKTFASLRKYQEEPPLAKTAPDLAANRANDIQGYLVDLPLEFLNKEVLTPPGTSKEGLIPTSVWT
Protein: Tubulin beta-5 chain (P69897)
Organism: Rattus norvegicus (Rat)
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.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P07437}.
Interaction partners:
- Tubulin alpha-1B chain
- Microtubule-associated protein tau
- Tubulin alpha-4A chain
- Tubulin alpha-1A chain
- Tubulin alpha-8 chain
- Tubulin alpha-1C chain
- Tubulin alpha chain
- Gap junction alpha-1 protein
- Tubulin alpha-3 chain
- Cytoplasmic dynein 1 heavy chain 1
Sequence:
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDFGEEAEEEA
Protein: Phosphomannomutase 1 (PMM 1) (EC 5.4.2.8) (PMMH-22) (Q92871)
Organism: Homo sapiens (Human)
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O35621}.
Interaction partners:
- Mannose-6-phosphate isomerase
- Mannose-1-phosphate guanylyltransferase regulatory subunit alpha
- Phosphomannomutase 2
- Hexokinase-2
- Hexokinase-1
- Hexokinase HKDC1
- Hexokinase-3
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Glucose-6-phosphate isomerase
- Thymidine kinase, cytosolic
Sequence:
MAVTAQAARRKERVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIAEQLGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFPETAHEA
Protein: RNA polymerase I-specific transcription initiation factor rrn3 (Q10110)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for efficient transcription initiation by RNA polymerase I.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase I subunit rpa43
- DNA-directed RNA polymerase I subunit rpa49
- Probable DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerase I subunit rpa1
- Uncharacterized protein C3B8.11
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase I subunit RPA12
- RNA polymerase I-specific transcription initiation factor rrn11
- DNA-directed RNA polymerases I and III subunit RPAC2
- TATA-box-binding protein
Sequence:
MPSIISSTNPQYINKCVNNGTMASSTNVPDRTVGSKSFASSVSKNDGRLMQQMLRAFVNKALDDKAEGNFAGYEDLRRQFAAKSDTKDAPSSLQLQNLLSALTCNVSRLDSSNSSLVMSVLDSVWVSRDESFVRCYTRFLGNLISAQSNYLPLVMTMLIQHMLYRPDSLAIHYEHAHMALKYVLELVPRAHSFLYSSILEEFPYKDESLLAQMTYISNVLSICEYVPSIKGPVLHAIIDKIIQIDVEIQVEVDDDDEEEDEVVTDDDGTSNADSEVITASTLYERHTAISSEMTSSTILTPPSLTDTRQLMQQLDQLLYTLFSYLDSNLKSTSRDRYLVYNSLIKSFVNTVLKTFRCRYTQFLIFWASQLDPEFTDIFLGVLTEVCLDPSQPYTLRLSGAMYIGSYVARAKALEKNTIQIIVNMMTRWVEAYLDQCENELSDDLLSKHSVFYAINQSIFYIFCFRWRELCVSDESESMEPRPNEWIPGLEILHRSVLSRLNPLRYCSPNIVLQFAKVANHLNFMYVYSIIEQNRKGIFREGFDTMDAYFPFDPYRLTKSSIIVQPFYNEWQQIPGLDDDEEEEDTDYESSTVMLGESPF
Protein: Essential nuclear protein 1 (P38333)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for normal export of the pre-40S particles from the nucleus to the cytoplasm. Its subcellular location and association with pre-40S subunit shifts from mixed cytoplasm/nucleus to all nuclear in RPS19 disruptions, suggesting it acts after the ribosomal protein.
Subcellular location: Cytoplasm. Nucleus, nucleolus.
Interaction partners:
- U3 small nucleolar RNA-associated protein MPP10
- Periodic tryptophan protein 2
- Protein SOF1
- Ribosomal RNA-processing protein 7
- Small ribosomal subunit protein eS17A
- NET1-associated nuclear protein 1
- Ribosomal RNA-processing protein 12
- Ribosome biogenesis protein ENP2
- Small ribosomal subunit protein uS19
- Protein LTV1
Sequence:
MARASSTKARKQRHDPLLKDLDAAQGTLKKINKKKLAQNDAANHDAANEEDGYIDSKASRKILQLAKEQQDEIEGEELAESERNKQFEARFTTMSYDDEDEDEDEDEEAFGEDISDFEPEGDYKEEEEIVEIDEEDAAMFEQYFKKSDDFNSLSGSYNLADKIMASIREKESQVEDMQDDEPLANEQNTSRGNISSGLKSGEGVALPEKVIKAYTTVGSILKTWTHGKLPKLFKVIPSLRNWQDVIYVTNPEEWSPHVVYEATKLFVSNLTAKESQKFINLILLERFRDNIETSEDHSLNYHIYRAVKKSLYKPSAFFKGFLFPLVETGCNVREATIAGSVLAKVSVPALHSSAALSYLLRLPFSPPTTVFIKILLDKKYALPYQTVDDCVYYFMRFRILDDGSNGEDATRVLPVIWHKAFLTFAQRYKNDITQDQRDFLLETVRQRGHKDIGPEIRRELLAGASREFVDPQEANDDLMIDVN
Protein: Sad1 and UNC84 domain containing 1 (H0Y742)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004540}.
Interaction partners:
Sequence:
GDVGAAAATAHNGFSCSNCSMLSERKDVLTAHPAAPGPVSRVYSRDRNQKCGASFYVNRILWLARYTASSFSSFLVQLFQVVLMKLSYESENYKLKTHESKDCESESYKSKSHESKAHASYYGRMNVREVLREDGHLSVNGEALCYFLLQILRRIGAVGQAVSRTAWSALWLAVVAPGKAASGVFWWLGIGWYQFVTLISWLNVFLLTRCLRNICKFLVLLIPLFLLLAGLSLRGQGNFFSFLPVLNWASMHRTQRVDDPQDVFKPTTSRLKQPLQGDSEAFPWHWMSGVEQQVASLSGQCHHHGENLRELTTLLQKLQARVDQMEGGAAGPSASVRDAVGQPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKTISAVGEQLLPTVEHLQLELDQLKSELSSWRHVKTGCETVDAVQERVDVQVREMVKLLFSEDQQGGSLEQLLQRFSSQFVSKGDLQTMLRDLQLQILRNVTHHVSVTKQLPTSEAVVSAVSEAGASGITEAQARAIVNSALKLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALMSLFGIPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMMIHPAAFTLEHIPKTLSPTGNISSAPKDFAVYGLENEYQEEGQLLGQFTYDQDGESLQMFQALKRPDDTAFQIVELRIFSNWGHPEYTCLYRFRVHGEPVK
Protein: Neurexin 1, isoform A (Neurexin 1, isoform C) (Q9VCZ9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKAPHSATYQDNYADAAMTARTRPSMDMDQQRNRNQAELRLLPAQRTSTSAFESPDLRFNKARRRRRSEQVPPVVVEYRRSYRVLIVSALLVSLAASFVTLSAGFQLDGSQNSFYTFRKWYTGLNGTLELEFKTEQPNGLVLYTDDGGTYDFFELKLVEGALRLRYNLGGGAQIITVGRELHDGHWHKVQVLRNDEQTSLIVDGVSQQRSTKGKEFQFGKFASNSDVYVGGMPNWYSSKLALLALPSVIFEPRFRGAIRNLVYADQPGGSTRRQEIKQQRDIKCGDVPCDHGELPARERPLRGVRGGNTTDACERNDPCQHGGICISTDSGPICECRNLEYDGQYCEKEKAPSEATFRGTQFLSYDLGQTGAEPIVSAQDAISFYFRTRQPNGLLFYTGHGTDYLNLALRDGGVSLTMGLANGKQEMHIKPSKVRFDDHQWHKVTVHRRIQEISSITSFCRLVTVVDDVYTDHSHIAGKFTMLSSSRVYVGGAVNPRALLGARVHTNFVGCLRKVEFSADTLNLNLIDLAKSGSKLIQVAGNLEYQCPSGDPQDPVTFTTRESHLVLPPWETGKQSSISFKFRTKEPNGIIVLATGSKQPRAKNPVLIAIELLNGHIYIHLDLGSGASKVRASRRRVDDGDWHDLILRRNGRDAKVSVDGVWNDFRTPGDGTILELDGHMYLGGVGPAYNSVSWPAAIWTATLRQGFVGCLRDLVLSGKAIDIAAFARVQDSASVKPSCHVQANVCNGNPCLNGGTCLEGWNRPICDCSATLYGGPTCGRELATLAFNGSQHMTIWLGNGQGTKTQTEELVIRFKTSRPAGLLLLTSAESNSPDRLEIALVAGRVRASVRLSDREKNLLAGQSVLNDNNWHTIRFSRRASNLRLQVDGAPPVRAETILGRHSTMEIRSVHLGGLFHAEEEIQMTSTMPNFVGQMQGLVFNGQRYLDIVKSLGPELSALPSATFKLTARFVNSPAGQPYHAATFRSKHSYVGLAMLKAYNSISIDFRFKTVEPNGLLVFNGGRRNDFVAVELVNGHIHYTFDLGDGPVTMRDKSRIHMNDNRWHQVSIRRPGPKTHTLTVDDSFEIISLTGNNMHLELAGILYIGGVFKDMYSKLPASISSRSGFEGCLASLDLGDASPSLTSDAVVPSSLVVSGCEGPTKCSQNACANRGNCVQQWNAYACECDMTSYTGPTCYDESIAYEFGNNKGMVQYTFPENAQADTEEDNIALGFITTRPDAVLLRVESATTQDYMELEIVEGNIFMVYNIGSVDLPLGEIGTKVNDNAYHVVRFQRKGGNATLQLDDYNVQALTPQSHHSTVFNTMSNVQVGGKFSRNGRNRIERPFAGVIAGLSVNKLRILDLAVERDPHITIRGDVQLVTGVLDRNDLQRMQQTPASGYPGALDDLIFSGAGSGCRGDDEDECTPPFESGSGDDLITPVYVPPTKQTTTSQQGNSLSTGGSSSGGVITNGTERACDDEDCVHGSGDYGETTEQFTSTSTARGSESNNEMVTITTTGRSDVTTEQHQGSSSSSSSGSTPSYATTQSSSSSSSGGSAASTPGQVSTTSSVATSSTQRATSSSTSTSSSTTSTTTTTTTTQATPPPEIRSTVTERETTPYDIYIAGGGMGGSGRNDHDRMQLPDEHHPLPPLPPPIPPQDPPPYGPYGGNTYNTNMNNYRPKGKGGRINSIEEERTAMIIGIVAGILIAVVLVILLVLWLKSNGDRGYKTESEKAAAYGSHNPNAALLGNTSTNGSYHQQRQHHMHGGGGGGGAGQQQHHAQQQMHNGHNGNGNGGGGGGGGMMSSGSGSLGYGSDGRPQMAGLVQPKAKKRDSKDVKEWYV
Protein: Crystal protein (P21837)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasmic vesicle, esterosome membrane. Note=Membrane-enclosed crystals (esterosome).
Interaction partners:
Sequence:
MNKIIILLIILLSFDIISAAKKFGRKGIRTLGDNEVLLSDGAIRGTVTDTHRVFYGIPFARPPIDELRYEDPQPPKPWSYVRDGTKQRDQCIQDCKLGKGSCSEVGTSEDCLYLDVFIPRTVNPGSKVPVMVFIPGGAFTQGTGSCPLYDGLKFANSSVIVVNVNYRLGVLGFLCTGLLSGNFGFLDQVMALDWVQENIEVFGGDKNQVTIYGESAGAFSVAAHLSSEKSEGKFHRAILSSTPYTVGLKSQTVARGFAGRFSSKIGCDLEDIDCHRSKSPEEILAIQKELGLAIGDKILDAFTIWSPVVDGINVNEQPLTMIKQGTTHDVPTIIGDNQDEAILFVYMTYKNVVIPSSYRTMVHVLFGIANGNKVLEHYPLPGFLKDSRPILSKLLTDYLFRCPGRYHVSKSAQANESPIYHYQYKQVLSGGHSFEACEGLVCHGTELPMVFNTYESALDLDLEEEEEEFAEQLNNYFVNFIKYSNPSHPNGLPTPKVWNPTTKTTNTSLVMKLGFEVKDLITNDPKCDLFDSLSYNGYTKDQNRMRKSKK
Protein: Bone morphogenetic protein 10 (BMP-10) (Q9R229)
Organism: Mus musculus (Mouse)
Function: Required for maintaining the proliferative activity of embryonic cardiomyocytes by preventing premature activation of the negative cell cycle regulator CDKN1C/p57KIP and maintaining the required expression levels of cardiogenic factors such as MEF2C and NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6, leading to activation of SMAD1, SMAD5 and SMAD8 transcription factors. Inhibits endothelial cell migration and growth. May reduce cell migration and cell matrix adhesion in breast cancer cell lines (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Activin receptor type-1-like
- Bone morphogenetic protein receptor type-2
- Endoglin
- Activin receptor type-1
- Activin receptor type-2A
- Activin receptor type-2B
- Growth/differentiation factor 2
- TGF-beta receptor type-1
Sequence:
MGSLVLPLSAVFCLVAHSASGSPIMGLEQSPLEEDMPFFDDIFTEQDGIDFNTLLQSMKNEFLKTLNLSDIPVQDTGRVDPPEYMLELYNKFATDRTSMPSANIIRSFKNEDLFSQPVTFNGLRKYPLLFNVSIPHHEEVVMAELRLYTLVQRDRMMYDGVDRKITIFEVLESADGSEEERSMLVLVSTEIYGTNSEWETFDVTDATRRWQKSGPSTHQLEIHIESRQNQAEDTGRGQLEIDMSAQNKHDPLLVVFSDDQSNDKEQKEELNELITHEQDLDLDSDAFFSGPDEEALLQMRSNMIDDSSARIRRNAKGNYCKKTPLYIDFKEIGWDSWIIAPPGYEAYECRGVCNYPLAEHLTPTKHAIIQALVHLKNSQKASKACCVPTKLDPISILYLDKGVVTYKFKYEGMAVSECGCR
Protein: L-type lectin-domain containing receptor kinase I.9 (LecRK-I.9) (LecRK79) (EC 2.7.11.1) (Protein DOES NOT RESPOND TO NUCLEOTIDES 1) (Purinoreceptor kinase 1) (Q9LSR8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential receptor for extracellular ATP. Binds ATP with high affinity through its extracellular legume-lectin like region. Is required for ATP-induced intracellular calcium response, mitogen-activated protein kinase 3 (MPK3) and MPK6 activation and ATP-induced gene expression. May play a variety of roles in stress resistance. May be involved in protein-protein interactions with RGD motif-containing proteins as potential ligands. Plays probably a structural and signaling role at the plant cell surfaces.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21483488, ECO:0000269|PubMed:25301072}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Respiratory burst oxidase homolog protein D
- AT5g09390/T5E8_190
- Nucleoside hydrolase 3
- Apyrase 2
- High mobility group B protein 2
- At1g58420
- Apyrase 1
Sequence:
MARWLLQILIISSLHLSSVSSQQETSFVYESFLDRQNLYLDKSAIVLPSGLLQLTNASEHQMGHAFHKKPIEFSSSGPLSFSTHFVCALVPKPGFEGGHGIVFVLSPSMDFTHAESTRYLGIFNASTNGSSSYHVLAVELDTIWNPDFKDIDHNHVGIDVNSPISVAIASASYYSDMKGSNESINLLSGNPIQVWVDYEGTLLNVSVAPLEVQKPTRPLLSHPINLTELFPNRSSLFAGFSAATGTAISDQYILWWSFSIDRGSLQRLDISKLPEVPHPRAPHKKVSTLIILLPVCLAILVLAVLAGLYFRRRRKYSEVSETWEKEFDAHRFSYRSLFKATKGFSKDEFLGKGGFGEVYRGNLPQGREIAVKRVSHNGDEGVKQFVAEVVSMRCLKHRNLVPLFGYCRRKRELLLVSEYMPNGSLDEHLFDDQKPVLSWSQRLVVVKGIASALWYLHTGADQVVLHRDVKASNIMLDAEFHGRLGDFGMARFHEHGGNAATTAAVGTVGYMAPELITMGASTGTDVYAFGVFMLEVTCGRRPVEPQLQVEKRHMIKWVCECWKKDSLLDATDPRLGGKFVAEEVEMVMKLGLLCSNIVPESRPTMEQVVLYLNKNLPLPDFSPYTLGIGTFAPVLVDASSLVVSSASWSLSGPSMSSSSPNHSPYAWQSTDQPWGQTIDTKNSLHIVAEPEKPSPAVKMVTLPAEDPQSNHSSISSQRVQPVKREKRRLHQILVAFPWINKQYFKLGLPKHIVHVSLFFFLQLARL