wanglab/gogpt-training-data huggingface dataset:
Protein: Maternal gene required for meiosis, isoform H (Maternal gene required for meiosis, isoform I) (Q9VY72)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein tramtrack, alpha isoform
- Transcription initiation factor IIA subunit 1
Sequence:
MGSEHYCLRWNNYQSNLLGVFSQLLQDGSLVDVTLVCSEGTSIRAHKVVLSACSSYFQSLFLEHPEGHLIVILKDVRFAELQTLVEFMYKGEVNVQYCQLSALLKTAESLKVKGLAEMTNQNTTLREPEREPDRLRPQGGGGSGGSAHKAADSPAAALDATAATQAATATATATAAAATSTSTSATSAAATAAATAATSASTTATAAAGSSNTTTTTAATTTATCATAATSTAATSSSSSVTSAAAAAAAAASASGVAHSEEATSSSSSTGGQKREASDRSSPTPAKRSSRMHPADKVDVAEDREQEQNQADELLSEELLGRNLKDEEDDDVDELDENEETKLRGRDEDDDDEDEEEDTPMPLDLYQRPNVEPKSAAAATAAQQGGSNSLSGSSNACHTNSSSNSNNNNNNNNNSSSNNNNNTSSGKTSASSNGGTASSGGTADSVVAVDDDDDDDDGGHHHQRQVMDDRLEQDVDEEDLDDDVVVVGPATAMARGIAQRLAHQNLQRLHHTHHHAQHQHSQHHHPHSQHHHTPHHQQHHTHSDDEDAMPVIAKSEILDDDYDDEMDLEDDDEADNSSNDLGLNMKMGSGGAGGGGGVDLSTGSTLIPSPLITLPSSSAAAAAAAAAAMESQRSTPAMSAAQAAGAGASDLSIGGCGGRPASRSSRDGGGNDGGRGGASSSSLLSPGTVANLLPVQSVPLSLKKEIDCSEDDNSSHSRHMQQRSASAGGGLGGDLDYRASHESLLRNFSSPMSAMAASRCPTPFAFPFSPLGLSLFDIDPSRILSLLHHQTWLAEEALRTRGLLTAPKDFPHRFTTLSDLLTKDYQPGAGQPMVTATATATTASSTSQVSASRSGDTQYNKHAQQPQQPQTGGATGSGVGGLGGSPTAGASFNLRYPTPTAFYQQQQQQGKGAKSSPSPQQMATSSTTVMSNDSGEDSCKRSSADSDEVTIMELPSERSAQLYKESLEQLLQRQRRTPILAGSGSGSGSGTGSGSVIVDAAGLRQYTQLLLAGAGSGGASDLKEKSSSSSTSSTPPLLTQQLSQMLKSPSDTCSSLFSSSGGGTGSTGPGITGETIEEETRCVVCNAHFPNVWLLEQHAALQHPHVGPGEEKPFICEQCGQSYRYRSAYAKHKEQNHRARLPADKLFTCDVCGMQFRYLKSFKKHRLNHALERLHGKKSVGVIGRLGGSGSGPSSSAISVSVAAPTSVSASGSVTSVDQDVVTSSQEPMLADEGEDLRVNVKREGTADEQSAESRANDLEEHEQDNTVDSAGITMLYQDNNSSASASTSATEPNISSSDGIHSTNKRSRLHHLETDPSYPHHHHHHHHHHHQQQHHQAQHQHHNPQSQLPTHLGHVSLPLVATSAAGSSSSAAAAAVVAAAQAQVSSGATGSGATGSGAPGSGNVGSAGSSGAGGGISSLSSLTSLINAERIPNEQFLGLNPQEASILNFLRVDAAERQRDKRPATSRFACPFCGKCVRSKENLKLHVRKHTGERPFVCLFCGRAFGGKSDLTRHLRIHTGERPYHCESCGKCFARADYLSKHLTTHIHNAPR
Protein: Zgc:66127 (Q7SXQ3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSKEQQTPREPEQLRKLFIGGLSFETTDESLRAHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYSSVGEVDAAMDARPHKVDGRAVEPKRAVSREDSSKPGAHSTVKKMFVGGIKEDTDEEHLREYFGQFGKIDEVNIMTEKNSDKRRGFAFITFDDHDAVDRIVIQKYHTVNGHNCEVRKALSREGMNRVSMNSRGGRGGGGGSGGGNFGRGGGGGGGGYGGGYGGGGGRGGGGGYGGGDGYNGYGGGNGGYGGGGPNYGGNRGYGSGGGGGGGGYGNQGGGYGGGGGYDNYNNNGGGGGGGGGNFGGGNFGGGGDYNDFGNYNNQSSSNYGPMKGGNYGGGGGGGGRSGGGPYGGGYGGGSGGGGGYGGGSGGGGGGYGGGSGGRRF
Protein: UspA domain-containing protein (A0A0H3LJ87)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Interaction partners:
Sequence:
MSSGNSSLGIIVGIDDSPAAQVAVRWAARDAELRKIPLTLVHAVSPEVATWLEVPLPPGVLRWQQDHGRHLIDDALKVVEQASLRAGPPTVHSEIVPAAAVPTLVDMSKDAVLMVVGCLGSGRWPGRLLGSVSSGLLRHAHCPVVIIHDEDSVMPHPQQAPVLVGVDGSSASELATAIAFDEASRRNVDLVALHAWSDVDVSEWPGIDWPATQSMAEQVLAERLAGWQERYPNVAITRVVVRDQPARQLVQRSEEAQLVVVGSRGRGGYAGMLVGSVGETVAQLARTPVIVARESLT
Protein: ATP synthase subunit a (ATP synthase F0 sector subunit a) (F-ATPase subunit 6) (A0A0F6B941)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Subcellular location: Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01393}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01393}. Cell membrane {ECO:0000256|RuleBase:RU000483}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU000483}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MASENMTPQEYIGHHLNNLQLDLRTFSLVDPQNPPATFWTLNIDSMFFSVVLGLLFLVMFRSVAKKATSGVPGKFQTAIELIVGFVHGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHWLGLPATRVVPSADVNITLSMALGVFILILFYSIKMKGIGGFAKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH
Protein: Heme oxygenase 1 (HO-1) (EC 1.14.14.18) (HSP32) [Cleaved into: Heme oxygenase 1 soluble form] (P06762)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:3865203}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}.
Interaction partners:
- Biliverdin reductase A
- Ferrochelatase
- Biliverdin reductase B
- NADPH--cytochrome P450 reductase
- Ceruloplasmin
- Hephaestin
- Nuclear factor erythroid 2-related factor 2
- Kelch-like ECH-associated protein 1
- NAD
- Glutathione peroxidase 1
Sequence:
MERPQLDSMSQDLSEALKEATKEVHIRAENSEFMRNFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEAIPYTPATQHYVKRLHEVGGTHPELLVAHAYTRYLGDLSGGQVLKKIAQKAMALPSSGEGLAFFTFPSIDNPTKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLLNIELFEELQALLTEEHKDQSPSQTEFLRQRPASLVQDTTSAETPRGKSQISTSSSQTPLLRWVLTLSFLLATVAVGIYAM
Protein: CAP, isoform K (CAP, isoform O) (SD03761p) (Q86P80)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
Sequence:
MSEPETGSDRPRKMAQLGRRQYDGIGPVTNDGMPIILRSEVKEPHQHEWYKRLYQTIHKQKNGDDFVIRYKCPRARPSYKSNGYVSEPEPNYDSDYSTVRYRTQNPHRVQSVSSAVNVRNLNQDEKLYGTMPNPIKSAQNSYKNQPGRIENYTTGHSSVSEKEKKEWWDEVMDIFNGNLEQSKLSPLYTEGNLSRALAKESGYTSDSNLVFRKKEVPVSSPLSPVEQKQAYKSLQAGGEPPLLGFRKPAPEKPRDLDPNAPPIPPQPPVKGLSSYDFPYSTDTVDGSDVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: Discoidin domain-containing receptor 2 (Discoidin domain receptor 2) (EC 2.7.10.1) (CD167 antigen-like family member B) (Discoidin domain-containing receptor tyrosine kinase 2) (Neurotrophic tyrosine kinase, receptor-related 3) (Receptor protein-tyrosine kinase TKT) (Tyrosine-protein kinase TYRO10) (CD antigen CD167b) (Q16832)
Organism: Homo sapiens (Human)
Function: Tyrosine kinase involved in the regulation of tissues remodeling. It functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:9659899}; Single-pass type I membrane protein {ECO:0000269|PubMed:18201965, ECO:0000269|PubMed:20223752, ECO:0000269|PubMed:9659899}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-1
- Integrin alpha-2
- SHC-transforming protein 1
Sequence:
MILIPRMLLVLFLLLPILSSAKAQVNPAICRYPLGMSGGQIPDEDITASSQWSESTAAKYGRLDSEEGDGAWCPEIPVEPDDLKEFLQIDLHTLHFITLVGTQGRHAGGHGIEFAPMYKINYSRDGTRWISWRNRHGKQVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHSMNVCMRVELYGCVWLDGLVSYNAPAGQQFVLPGGSIIYLNDSVYDGAVGYSMTEGLGQLTDGVSGLDDFTQTHEYHVWPGYDYVGWRNESATNGYIEIMFEFDRIRNFTTMKVHCNNMFAKGVKIFKEVQCYFRSEASEWEPNAISFPLVLDDVNPSARFVTVPLHHRMASAIKCQYHFADTWMMFSEITFQSDAAMYNNSEALPTSPMAPTTYDPMLKVDDSNTRILIGCLVAIIFILLAIIVIILWRQFWQKMLEKASRRMLDDEMTVSLSLPSDSSMFNNNRSSSPSEQGSNSTYDRIFPLRPDYQEPSRLIRKLPEFAPGEEESGCSGVVKPVQPSGPEGVPHYAEADIVNLQGVTGGNTYSVPAVTMDLLSGKDVAVEEFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSDEQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQQGDE
Protein: Box C/D snoRNA protein 1 (P38772)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14690591}.
Interaction partners:
- Histone chaperone RTT106
- Nucleolar protein 58
- Protein interacting with Hsp90 1
- RNases MRP/P 32.9 kDa subunit
- RuvB-like protein 2
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- TPR repeat-containing protein associated with Hsp90
- Protein HIT1
- 13 kDa ribonucleoprotein-associated protein
- RuvB-like protein 1
Sequence:
MAVLCGVCGIKEFKYKCPRCLVQTCSLECSKKHKTRDNCSGQTHDPKEYISSEALKQADDDKHERNAYVQRDYNYLTQLKRMVHVQKMDARMKNKRVLGPVGGHNSNFKKRRYDIDEDDRDSTECQRIIRRGVNCLMLPKGMQRSSQNRSKWDKTMDLFVWSVEWILCPMQEKGEKKELFKHVSHRIKETDFLVQGMGKNVFQKCCEFYRLAGTSSCIEGEDGSETKEERTQILQKSGLKFYTKTFPYNTTHIMDSKKLVELAIHEKCIGELLKNTTVIEFPTIFVAMTEADLPEGYEVLHQEPRPLEHTSTLNKFIDNAREEEDAEEDSQPTEEPVQKETQDASDSDSDSDDDYNPGLSMDFLTA
Protein: Zinc transporter ZIP6 (Estrogen-regulated protein LIV-1) (Solute carrier family 39 member 6) (Zrt- and Irt-like protein 6) (ZIP-6) (Q13433)
Organism: Homo sapiens (Human)
Function: May act as a zinc-influx transporter.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18272141}; Multi-pass membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:12839489}; Multi-pass membrane protein {ECO:0000269|PubMed:12839489}. Membrane raft {ECO:0000269|PubMed:34394081}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q4V887}. Note=Localizes to lipid rafts in T cells and is recruited into the immunological synapse in response to TCR stimulation (PubMed:34394081). In the choroid plexus is limited to the apical membrane in epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q4V887, ECO:0000269|PubMed:34394081}.
Interaction partners:
- Zinc transporter ZIP1
- Zinc transporter ZIP9
- Proton-coupled zinc antiporter SLC30A1
- Proton-coupled zinc antiporter SLC30A5
- Zinc transporter 6
- Zinc transporter ZIP11
- Probable proton-coupled zinc antiporter SLC30A4
- Zinc transporter 7
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Proton-coupled zinc antiporter SLC30A2
Sequence:
MARKLSVILILTFALSVTNPLHELKAAAFPQTTEKISPNWESGINVDLAISTRQYHLQQLFYRYGENNSLSVEGFRKLLQNIGIDKIKRIHIHHDHDHHSDHEHHSDHERHSDHEHHSEHEHHSDHDHHSHHNHAASGKNKRKALCPDHDSDSSGKDPRNSQGKGAHRPEHASGRRNVKDSVSASEVTSTVYNTVSEGTHFLETIETPRPGKLFPKDVSSSTPPSVTSKSRVSRLAGRKTNESVSEPRKGFMYSRNTNENPQECFNASKLLTSHGMGIQVPLNATEFNYLCPAIINQIDARSCLIHTSEKKAEIPPKTYSLQIAWVGGFIAISIISFLSLLGVILVPLMNRVFFKFLLSFLVALAVGTLSGDAFLHLLPHSHASHHHSHSHEEPAMEMKRGPLFSHLSSQNIEESAYFDSTWKGLTALGGLYFMFLVEHVLTLIKQFKDKKKKNQKKPENDDDVEIKKQLSKYESQLSTNEEKVDTDDRTEGYLRADSQEPSHFDSQQPAVLEEEEVMIAHAHPQEVYNEYVPRGCKNKCHSHFHDTLGQSDDLIHHHHDYHHILHHHHHQNHHPHSHSQRYSREELKDAGVATLAWMVIMGDGLHNFSDGLAIGAAFTEGLSSGLSTSVAVFCHELPHELGDFAVLLKAGMTVKQAVLYNALSAMLAYLGMATGIFIGHYAENVSMWIFALTAGLFMYVALVDMVPEMLHNDASDHGCSRWGYFFLQNAGMLLGFGIMLLISIFEHKIVFRINF
Protein: BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2 (hBACURD2) (BTB/POZ domain-containing protein TNFAIP1) (Protein B12) (Tumor necrosis factor, alpha-induced protein 1, endothelial) (Q13829)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(TNFAIP1) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. Its interaction with RHOB may regulate apoptosis. May enhance the PCNA-dependent DNA polymerase delta activity.
Subcellular location: Cytoplasm. Nucleus. Endosome. Note=Colocalizes with RHOB in endosomes.
Interaction partners:
- FAS-associated factor 1
- UBX domain-containing protein 7
- UBX domain-containing protein 1
- Cullin-3
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3
- E3 ubiquitin-protein ligase RBX1
- BTB/POZ domain-containing protein KCTD17
- Kelch-like protein 20
- Kelch-like protein 12
Sequence:
MSGDTCLCPASGAKPKLSGFKGGGLGNKYVQLNVGGSLYYTTVRALTRHDTMLKAMFSGRMEVLTDKEGWILIDRCGKHFGTILNYLRDDTITLPQNRQEIKELMAEAKYYLIQGLVNMCQSALQDKKDSYQPVCNIPIITSLKEEERLIESSTKPVVKLLYNRSNNKYSYTSNSDDHLLKNIELFDKLSLRFNGRVLFIKDVIGDEICCWSFYGQGRKLAEVCCTSIVYATEKKQTKVEFPEARIYEETLNVLLYETPRVPDNSLLEATSRSRSQASPSEDEETFELRDRVRRIHVKRYSTYDDRQLGHQSTHRD
Protein: F1K23.6 (Guanosine-3',5'-bis (Diphosphate) 3'-pyrophosphohydrolase, putative (DUF2215)) (Q9SHQ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004575}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004575}; Nucleoplasmic side {ECO:0000256|ARBA:ARBA00004575}.
Interaction partners:
Sequence:
MTTSSSFLRLPHRIWFLLPLIVFLLLSYAAALKSVGPGEPALNISLRSCERIQVSGYSRTKLGKFANSLRVNLVPIPEKLHLKIQVCVHRNATLGMCHCEKSNWKNLQSSSVISPYDKQYIDVRFTGSEYQSSRSMITVNVTEEFHQWRIFCLVAGLIVILLAPVVSSWLPFYYTSSMAVGVFLVVLIIIFQVMRLLPTGRKNVMYLAFYGSVVGAGSFILHQFSMMVNMILVNFGLSEDMYNPVAILVLVGVVITGAAFGFWTVRKFVVSKDGGGVDASVAQFVKWAMRSVAATFILQSSLDTPMAMGAFVLASLFGFLVSKTKSFVGKSHWLVSAGERRPIMHGRAEFLSRPGGGGLWKSAKSVPSYSGSPSYDVIVSSPSSVNRRIPIGNQDYYSTFHTTPNRKRMSKREYDELTQETTREAMAGLAASPGFSDWLVEHADRIKLLPTDSSYDDELGSESDSTGEQSWTRFFW
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (H0Y6Y4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEEPMDTDQGNSMLSAIQSEVAKNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKFEKHFEKTLLGK
Protein: Meiotic activator RIM4 (Regulator of IME2 protein 4) (P38741)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Positive regulator of sporulation-specific genes and of sporulation. Required for premeiotic DNA synthesis and meiotic chromosomal segregation. May act in a nutritional signaling pathway.
Interaction partners:
- Meiosis induction protein kinase IME2/SME1
- Proteasome subunit beta type-7
- Minichromosome maintenance protein 5
- Meiosis-inducing protein 1
- G2/mitotic-specific cyclin-3
Sequence:
MKTEISTADSLRDPPSNGLKADSELVIREDIDQFLPSEVSSLGSDHQNDGEDSDTDSDNFLQDPEDDVDEESTGRGTVTTTSTSTESRGRPSSCIFVASLAAALSDDELCLSVTENFKKYGDLARVKVLRDNANRPYAFVQYNNDHDAKHALIRAQGTLLNGRRLRCEPAKVNRTLYLKNQQSIDFNEISQICEKFGGLEQIVPDRTDNQYTRRYTYPISSANSWFVQFVYRDDAIRAYANLRTDPNWIIEWAQNINVPKNYNLLHKSKFKSSKYHQNNGIINNDGSNNNDNNNSNNNNREDSRRNGDVIEEECGHVHGSDSEEKLTSDGIYDDEDKDSEITIDKRSIFVGQLDKETTREELNRRFSTHGKIQDINLIFKPTNIFAFIKYETEEAAAAALESENHAIFLNKTMHVQYKEVGGRHNRKFSGKNGGSNFNHHQFFSTRSGKTFTGPELNLAPPPINMYRKMSGGSQQESETMMPYMPMGPMPMGPPPPNAASLSDFDMFPPSYSTFMKGMMPLRRKSMPNSWSSPSSKSVNSENESVNGGDENSELPSEIPESSGRYNAANSFTTYNNSSAGNSNNNNNNNNSNSNKSQYKKRYARRSSYGYNEVPPKPYYFQPYYYHPMQYHMGPMGPLHPSQGSAGNHHPYMMVYPMSPPPPSGLDGSMIPPPINVSQSHAANHGSTHVHANEFISNDTGDINEDNKAYSLDY
Protein: DNA replication licensing factor MCM3 (EC 3.6.4.12) (Minichromosome maintenance protein 3) (AtMCM3) (Q9FL33)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cell division control protein 6 homolog B
- Mini-chromosome maintenance complex-binding protein
- Minichromosome maintenance 10
- DNA replication licensing factor MCM5
- DNA replication complex GINS protein SLD5
- Origin of replication complex subunit 2
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM7
- Origin of replication complex subunit 5
- DNA polymerase epsilon subunit B
Sequence:
MDVPEETRLRHKRDFIQFLDSMYMEEIKALVHQKRHRLIINISDIHHHFREVASRILKNPNEYMQSFCDAATEATRAIDPKYLKEGELVLVGFEGYFVSRVVTPRELLSDFIGSMVCVEGIVTKCSLVRPKVVKSVHFCPSTGEFTNRDYRDITSHAGLPTGSVYPTRDDKGNLLVTEYGLCKYKDHQTLSIQEVPENAAPGQLPRSVDVIAEDDLVDSCKPGDRVSVFGIYKALPGKSKGSVNGVFRTILIANNIALLNKEANAPIYTKQDLDNIKNIARRDDAFDLLARSLAPSIYGHAWIKKAVVLLMLGGVEKNLKNGTHLRGDINMMMVGDPSVAKSQLLRAIMNIAPLAISTTGRGSSGVGLTAAVTSDQETGERRLEAGAMVLADKGIVCIDEFDKMNDQDRVAIHEVMEQQTVTIAKAGIHASLNARCSVVAAANPIYGTYDRSLTPTKNIGLPDSLLSRFDLLFIVLDQMDAGIDSMISEHVLRMHRYKNDRGEAGPDGSLPYAREDNAESEMFVKYNQTLHGKKKRGQTHDKTLTIKFLKKYIHYAKHRITPKLTDEASERIAEAYADLRNAGSDTKTGGTLPITARTLETIIRLATAHAKMKLSSEVTKADAEAALKLMNFAIYHQELTEMDDREQEERQREQAEQERTPSGRRGNQRRNNEDGAENDTANVDSETADPMEVDEPSVEQFSGTVSAARIETFERVFGQHMRTHRLDDISIADIETVVNNNGVGASRYSADEIMALLEKLQDDNKVMISDGKVHII
Protein: Nematode cuticle collagen N-terminal domain-containing protein (O01904)
Organism: Caenorhabditis elegans
Interaction partners:
- Cuticle collagen bli-1
- CPG4 domain-containing protein
- Dual oxidase 1
- Cuticle collagen 49
- Nematode cuticle collagen N-terminal domain-containing protein
- Dual oxidase maturation factor 1
Sequence:
MDEKELNHEASMLRKVAFLGICISTVSTLTCIIAIPLLYNYMQHVQTNLHSEIDFCRHRTVGLFIQYERMQSASGIKGRRIIVKKQAGYDFAESNTNAESGFSSSKSSLAPGGQCCSCKTGPSGPPGPPGEDGRDGRDGKPGLNGEDGTDAKDSAPRRDAAAPCYDCPVGPPGPPGNIGSKGQPGRNGKDGLPGVPGLPGQPGEPGDDGEPGEDGDPGQPGDNGEPGKCDEVNVAQGPPGSPGPPGLPGPDGLPGTPGNPGQDGEQGPAGEPGRDGKDGQPGRPGQPGPPGEPGTGGGCEHCPTPRTAPGY
Protein: Inositol polyphosphate multikinase alpha (EC 2.7.1.140) (EC 2.7.1.151) (Inositol polyphosphate 6-/3-/5-kinase alpha) (AtIpk2-alpha) (AtIpk2alpha) (Q9LY23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inositol phosphate kinase with a broad substrate specificity. Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3), inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4), inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4) and inositol 1,2,3,4,6-pentakisphosphate (Ins(1,2,3,4,6)P5) but not inositol 1,4-bisphosphate (Ins(1,4)P2), inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), inositol 1,2,6-trisphosphate (Ins(1,2,6)P3), inositol 3,4,5,6-tetrakisphosphate (Ins(3,4,5,6)P4), inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5), inositol 1,2,4,5,6-pentakisphosphate (Ins(1,2,4,5,6)P5) or inositol hexakisphosphate (InsP6). Regulates pollen and root development probably through the regulation of InsP3-mediated calcium accumulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:15618435}. Cell membrane {ECO:0000269|PubMed:15618435}.
Interaction partners:
- Inositol-pentakisphosphate 2-kinase
- Inositol-tetrakisphosphate 1-kinase 1
- Inositol-pentakisphosphate 2-kinase
- Inositol-pentakisphosphate 2-kinase
- Inositol 1,3,4-trisphosphate 5/6-kinase 4
- Inositol-tetrakisphosphate 1-kinase 2
- Inositol-tetrakisphosphate 1-kinase 3
- Phosphoinositide phospholipase C 1
- Phosphoinositide phospholipase C 4
- Phosphoinositide phospholipase C 3
Sequence:
MQLKVPEHQVAGHIAKDGKPGPLVDDKGRFFKPLQGDSRGEIEVKFYESFSSNTEVPEHIHRYFPVYHGTQAVEGSDGAAMMVLENLLAEYTKPSVMDVKMGSRTWYPDASEEYIQKCLKKDTGTTTVSSGFRISGFEVYDHKESSFWKPERKLLRGLDVDGARLTLRKFVSSNSLSDTGSKPDSAFASSVYGGSHGILTQLLELKTWFENQTLYHFNSCSILMVYENESILKGNDDDARPQVKLVDFAHVLDGNGVIDHNFLGGLCSFINFIREILQSPDESADS
Protein: Transcription termination factor MTERF6, chloroplastic/mitochondrial (Mitochondrial transcription termination factor 6) (Protein PIGMENT DEFECTIVE 191) (Q9SZL6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription termination factor essential for chloroplast development. Required for maturation of 16S rRNA, 18S rRNA and 23S rRNA in the chloroplast. Binds to a specific region within the tRNA(Ile)(GAU) gene at a position adjacent to and downstream of the 16S rRNA gene. Required for the maturation of tRNA(Ile)(GAU). Binds to double-stranded DNA.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:26152711}. Mitochondrion {ECO:0000269|PubMed:21464319, ECO:0000269|PubMed:26152711}.
Interaction partners:
- Transcription termination factor MTERF15, mitochondrial
- Transcription termination factor MTEF18, mitochondrial
- Rho-N domain-containing protein 1
- DNA-directed RNA polymerase subunit alpha
- Holliday junction resolvase MOC1, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 14
- PLASTID TRANSCRIPTIONALLY ACTIVE protein 6, chloroplastic
- Plastid transcriptionally active 3
- Thioredoxin-like protein CITRX, chloroplastic
Sequence:
MEVTNTSSIMWFFRDKGFDDPSIDKMLRKCKQLEKAQSDVASENWDYLSNIVGIQERKLPYIVSRCPKILTLRLDERLIPMVECLSSLGRNPREVASAITKFPPILSHSVEEKLCPLLAFFQALGVPETQLGKMILFNPRLISYSIDTKLTVIVSFLASLGLDQDGMIGKVLVKNPFLMGYSVDKRLRPTTEFLKSSVGLSEDGIKSVVMNFPQLLCRDVNKILKPNYDYLKECGFGDSQIATMVTGYPQILIKSVKNSLQPRIRFLVQVMGRGMDEVASYPEFFHHGLKKKVESRFKLVKKNNIDCSLREMLDCNTKKFHEKFGFSEVTASF
Protein: Ureidoglycolate lyase (EC 4.3.2.3) (Degradation of allantoin protein 3) (Ureidoglycolatase) (Ureidoglycolate hydrolase) (P32459)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as secondary nitrogen source when primary sources are limiting.
Interaction partners:
- Allantoicase
- Allantoinase
- Urea amidolyase
- Malate synthase 2
- Protein DAL82
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
Sequence:
MVTVVAETLTKESFEEYGTIISPDEEISRMQNLEKGANQGTAIKLLQVSQVENKSTSKVPNWNLFRCFPQPHLNRVFTQGSNQAISHSIKVLEKHPCSTQTFVPMGRTSAEVAYLVVVAKEIGNKPDLSTLRAFTCLGNQAVTYGLGTWHAPMIVLGKEEHLDFSVLIYESLDPDRPEKDCVEEHYSDGDVCIII
Protein: Olfactory receptor 4M1 (Olfactory receptor OR14-7) (Q8NGD0)
Organism: Homo sapiens (Human)
Function: Olfactory receptor that acts as a receptor of Asprosin hormone at the surface of hepatocytes to promote hepatocyte glucose release. Also binds Asprosin in the arcuate nucleus of the hypothalamus, thereby stimulating appetite by promoting orexigenic AgRP neuronal activity (By similarity). In testis, Asprosin-binding promotes sperm progressive motility and enhances male fertility (By similarity). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase, resulting in an elevation of intracellular cAMP (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:31230984}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU363047}.
Interaction partners:
- Beta-arrestin-2
- Guanine nucleotide-binding protein G
Sequence:
METANYTKVTEFVLTGLSQTREVQLVLFVIFLSFYLFILPGNILIICTIRLDPHLTSPMYFLLANLALLDIWYSSITAPKMLIDFFVERKIISFGGCIAQLFFLHFVGASEMFLLTVMAYDRYAAICRPLHYATIMNRRLCCILVALSWMGGFIHSIIQVALIVRLPFCGPNELDSYFCDITQVVRIACANTFPEELVMICSSGLISVVCFIALLMSYAFLLALLKKHSGSGENTNRAMSTCYSHITIVVLMFGPSIYIYARPFDSFSLDKVVSVFHTVIFPLLNPIIYTLRNKEVKAAMRKVVTKYILCEEK