wanglab/gogpt-training-data huggingface dataset:
Protein: NEDD8-activating enzyme E1 regulatory subunit (E1 N-terminus-related protein 2) (Ubiquitin-activating enzyme E1-like 1) (Ubiquitin-like activation protein 1) (Q12059)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBC12.
Interaction partners:
- NEDD8-activating enzyme E1 catalytic subunit
- NEDD8-conjugating enzyme UBC12
- NEDD8-like protein RUB1
- Cell division control protein 53
- Ubiquitin-conjugating enzyme E2-34 kDa
- COP9 signalosome complex subunit 5
- RING-box protein HRT1
Sequence:
MERYDRQLRLWGALGQDSLNRSRVCVVGPATPLLQEVFKNLVLAGISSLTWLKVECAVQSGSLFLAELKKDLEPLASKQLEYEENDLRKTLQQPQYDWTRFSVVILTCIGEQTAMLDLNEIRRQRGTKFPPVLNTFVSGFYGYIYLVLSETHFVLQAHPDSKKYDLRLQNPWPELINYVDTFDLSKMDTATFSGIPYTVLLMKCIAKLERDGNNGRITIDQMKKVLDQICLPLGNDVIYEPNYVEAKRYAYLACSQNDCCKELEDLLRNLEISDYGNDWHDTYNYEILTLLLTLKNIAKENGELSFQPLTGTLPDMESTTENYIRLKKLYEVKAKLDKSRVEESLARSKKIVSQDVLETFCSHYGEVRKILPPKSDLLGIFSTSNALLDALVMVQFWEQPAVTAEDKDEFIGLRVDDNYSVMAFFGGAVVQEAIKLITHHYVPIDNLFLYNGINNSSATYKI
Protein: 1,3-beta-glucan synthase component FKS1 (EC 2.4.1.34) (O93927)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Catalytic subunit of the 1,3-beta-glucan synthase (GS) complex. Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Involved in cell wall synthesis, maintenance and remodeling (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P38631}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSYPNPPPPPKGSASFSSSSSDPFNQTNQLPYDSQFPPQHAFAHPSAPNPGAGGAGVAPPGQGGQYAPYYDNEPEMGGRWEGGGMGRETWASESGWSQNEPNYPPSDYHGGPGYLPSRASTPTFEGSNAGHRPRDPYPAWTVDANIPLSKEEIEDVLIDLANKFGFQKDSSRNVYDFLMIQLDSRASRMSPNQALLTLHADYIGGEHANYRKWYFAAQLDLDDAIGAVQNPGLNRVRSVARRGGKTKNPLATAQEKSLESATSRWRTAMNNMSQYDRLRQVALYLLCWGEAAQVRFMPECLCFIFKCADDYYRSPECQNRQEAVPEGLYLRAVIKPLYRFLRDQGYEVVDGKFLRRERDHDKVIGYDDVNQLFWYPEGISRITLNDNTRLVDIPPAQRFMKFDRIDWNKVFFKTYLEKRSFFHLLVNFNRIWVLHISVFWFFTAYNAPSIYAPSGSTTATTPMAWSMTGLGGFVATLIMIAATLAEFSYIPTTWNNTSHLTRRLIFLLIILAITGGPSIYIAFFNQTGHVALILGIVQFFCSVVATIAFATLPSGRMFGDRVAGKSRKYLANQTFTASYPALGFYPRVASFLLWFLVFGCKFTESYFFLTLSFRDPMKVMNGMKVQNCHDKYFGNGLCTNQPAFALAVMFVMDLTLFFLDTFLWYVIWNTVFSIARSFAIGMSIWTPWKDIFARLPKRIYAKILATDDMEVKYKPKVLVSQVWNAVIISMYREHLLSIEHVQKLLYHQIQSDQPGKRTLRAPAFFISQSEKGSKAEFFPKGSEAERRICFFAQSLTTSIPAPIPVDAMPTFTVLVPHYSEKILLSLREIIREEDQNTRVTLLEYLKQLHPVEWDNFVRDTKILAEESDAFNGGNPFASDEKEEAKKADDIPFYTIGFKSAAPEYTLRTRIWASLRAQTLYRTVSGFMNYSKAIKLLYRVENPEVVQLFGGNTDQLERELERMARRKFKFVVSMQRYSKFNKEEHENAEFLLRAYPDLQIAYLDEEPPRKDGGESRIFSALIDGHSEIMPNGRRRPKFRIELPGNPILGDGKSDNQNHAIVFYRGEYLQLIDANQDNYLEECLKIRNVLGEFEEFKVSTQSPYAAQGHADFAKFPVAILGAREYIFSENIGILGDIAAGKEQTFGTLAARSLSYIGGKLHYGHPDFLNAIYMNTRGGVSKAQKGLHLNEDIFAGMLAFGRGGRIKHSEYYQCGKGRDLGFGTILNFQTKIGTGMGEQMLSREYYYLGTQLPIDRFLTFYYGHPGFHINNILVMMSVQVFMLALVFLGTLNKQLTVCRYSSGGDILPGQSGCYNLVPVFKWIKRCIISIFIVFWIAFVPLFVQELTERGTGRAILRLCKHFLSLSPVFEVFSTQIYMHSILNDLTFGGARYIATGRGFATTRISFSILYSRFAGPSIYLGMRTLVLLLFITLTVWVPHLIYFWITVVGLCVAPFLFNPHQFAIADFIIDYREFLRWMSRGNSRTHANSWVGYCRLSRTRVTGFKRKRLGLPSEKLSSDVPRAPWKAILIGEIIGPICLAILFVICYLFIKSFAVDGQIQPGLVRIAIIALGPIVWNMALLITLFLISVFLGPCLNSYTHQFGATMAALAHFGAVAGMLVFFELLWFLELWNTSHAVLGIIAVISVQRCIFKFLIAVFLSREFKHDETNRAWWTGVWFNRGLGSHALSQPAREFVVKTIEMGLYSADFIACHLLLALLTIPMFIPYFDRVHATMLFWLAPNQQIRPPIYSFRQRSQRRKIVFKYGLLYLIIQGIFIALIVVPIIFKDVAGLTPKSVPFNGII
Protein: Beta-agarase A (EC 3.2.1.81) [Cleaved into: Beta-agarase A catalytic chain (AgaAc)] (G0L322)
Organism: Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
Function: Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place.
Subcellular location: Secreted {ECO:0000269|PubMed:15456406}.
Interaction partners:
- Beta-porphyranase B
- Beta-porphyranase D
- Conserved hypothetical periplasmic protein
- 3,6-anhydro-alpha-L-galactosidase
- Glycoside hydrolase
- Glycoside hydrolase
- Conserved hypothetical lipoprotein
- Cytochrome P450
- Polysaccharide lyase, family PL9
- Kappa-carrageenase, family GH16
Sequence:
MKKNYLLLYFIFLLCGSIAAQDWNGIPVPANPGNGMTWQLQDNVSDSFNYTSSEGNRPTAFTSKWKPSYINGWTGPGSTIFNAPQAWTNGSQLAIQAQPAGNGKSYNGIITSKNKIQYPVYMEIKAKIMDQVLANAFWTLTDDETQEIDIMEGYGSDRGGTWFAQRMHLSHHTFIRNPFTDYQPMGDATWYYNGGTPWRSAYHRYGCYWKDPFTLEYYIDGVKVRTVTRAEIDPNNHLGGTGLNQATNIIIDCENQTDWRPAATQEELADDSKNIFWVDWIRVYKPVAVSGGGNNGNDGATEFQYDLGTDTSAVWPGYTRVSNTTRAGNFGWANTNDIGSRDRGASNGRNNINRDINFSSQTRFFTQDLSNGTYNVLITFGDTYARKNMNVAAEGQNKLTNINTNAGQYVSRSFDVNVNDGKLDLRFSVGNGGDVWSITRIWIRKVTSNSANLLAAKGLTLEDPVETTEFLYPNPAKTDDFVTVPNSEIGSSIIIYNSAGQVVKKVSVVSENQKISLEGFAKGMYFINLNGQSTKLIVQ
Protein: Propionate--CoA ligase (EC 6.2.1.1) (EC 6.2.1.17) (B1WC11)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGLPEERRKSGSGSRAREETGAEGRVRGWSPPPEVRRSAHVPSLQRYRELHRRSVEEPREFWGNIAKEFYWKTPCPGPFLQYNFDVTKGKIFTEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGVQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTDAFYRGEKLVNLKELADESLEKCREKGFPVRCCIVVKHLGRAELVMNDSPSQSPPVKRPCPDVQISWNEGVDLWWHELMQQAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDTSTVADPSVINHLFSHRCLTTQ
Protein: Protein PHYTOCHROME KINASE SUBSTRATE 1 (Q9SWI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be responsible for light-regulated cytoplasmic sequestration of phytochromes or may be a negative regulator of phytochrome B signaling. Component of the network that modulates the very low-fluence response (VLFR) branch of phyA signaling. Acts positively in PHOT1 signaling. Regulates phytochrome-mediated photomorphogenesis and hypocotyl phototropism. Involved in the control of leaf flattening and leaf positioning. Promotes negative root phototropism and negatively regulates root gravitropism. May act by controlling auxin homeostasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10348744, ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:20071603}; Peripheral membrane protein {ECO:0000269|PubMed:10348744, ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:20071603}.
Interaction partners:
- Phototropin-1
- Phytochrome A
- Phytochrome B
- Phototropin-2
- Root phototropism protein 2
- Protein PATRONUS 1
- CBL-interacting serine/threonine-protein kinase 20
- Root phototropism protein 3
Sequence:
MVTLTPSSASTPKTSFDFMKNNNSHSSLYVSSSSYLSSKEDALVTTKKLMEPSKTLNMSINPKQEEFGDEKKMVKKAPEDPEIGVFGAEKYFNGDMDSDQGSSVLSLTNPEVERTVVDSKQSAKKSTGTPSVRSESSWNSQSVLLQNKLVNSCNSSFKEKKNSNGQIQKVTNNKKSFLANLGCKCACSDGDSVDVEEKTSVKRSADPNISVITMRSSADMNTELIKIQKQEELSQRKSLEVFGSPVAIEKKSSVVQKKLPLPPWKSRTEEDDTKSEGSDSSSDLFEIEGLTGNPKPFLTRQGSDPASPTCYAPSEVSVEWSIVTASAADFSVMSECATSPVRRNRPTQIPRIPITAKSAPQRRKSSSSSGGNGFLMSCKSHKSVMVSGDLDRRSSMNKTQPSYVPRFPMETTKPKSFETRRRISNSSISHTQSSLLYSQ
Protein: BUB3-interacting and GLEBS motif-containing protein ZNF207 (BuGZ) (xBuGZ) (Zinc finger protein 207) (Q7ZXV8)
Organism: Xenopus laevis (African clawed frog)
Function: Kinetochore- and microtubule-binding protein that plays a key role in spindle assembly. Znf207/BuGZ is mainly composed of disordered low-complexity regions and undergoes phase transition or coacervation to form temperature-dependent liquid droplets. Coacervation promotes microtubule bundling and concentrates tubulin, promoting microtubule polymerization and assembly of spindle and spindle matrix by concentrating its building blocks.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O43670}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O43670}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26388440}. Note=Localizes primarily to the nucleus in interphase, concentrates at kinetochores prior to nuclear envelope breakdown and during early prometaphase, and disappears from kinetochores upon microtubule-binding. {ECO:0000250|UniProtKB:O43670}.
Interaction partners:
Sequence:
MGRKKKKQLKPWCWYCNRDFDDEKILIQHQKAKHFKCHICHKKLYTGPGLAIHCMQVHKETIDAVPNAIPGRTDIELEIYGMEGIPEKDMEERRRILEQKTQVDGQKKKTNQDDSDYDDDDDTAPSTSFQQMQTQQAFMPTMGQPGIPGLPGAPGMPPGITSLMPAVPPLISGIPHVMAGMHPHGMMSMGGMMHPHRPGIPPMMAGLPPGVPPPGLRPGIPPVTQAQPALSQAVVSRLPVPSTSAPALQSVPKPLFPSAGQAQAHISGPVGTDFKPLNNIPATTAEHPKPTFPAYTQSTMSTTSTTNSTASKPSTSITSKPATLTTTSATSKLVHPDEDISLEEKRAQLPKYQRNLPRPGQAPISNMGSTAVGPLGAMMAPRPGLPPQQHGMRHPLPPHGQYGAPLQGMAGYHPGTMPPFGQGPPMVPPFQGGPPRPLMGIRPPVMSQGGRY
Protein: SD01238p (Vismay, isoform A) (Q7K380)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MISPEQEEVNMVLDRHVRQNIKDLMHEAHVHASLLNNEGRDRFHSDSSLDQDSLHAVVGNDLSTEQGANQVQNYHDMMVDSEHHVDINGSLRKRRGNLPKSSVKILKRWLYEHRYNAYPSDAEKFTLSQEANLTVLQVCNWFINARRRILPEMIRREGNDPLHFTISRRGKKVSPNCSRSSALGANLTGPNPAHGSPASEVVVGATEEVDGAGEIHEGIANVLTNFEQYVQGPNGQMVKMEPEYEDSVIYRSEGEESAQGYESCGPNSEEEVRFETSHDWQSVIKTVFGTEEVSTSAGNNPGTSGSKASVQNTAIWNRNQTAKRDVNQQLTDFESELNIIQASEIQTIDPTNSNQQDIGDNLQADEVFTGAEAEAGQSQLSALSQGTSSDEEGKYKCLYYLVETAMAVRQNDDVQDDDFVYMGD
Protein: Visual pigment-like receptor peropsin (O14718)
Organism: Homo sapiens (Human)
Function: May play a role in rpe physiology either by detecting light directly or by monitoring the concentration of retinoids or other photoreceptor-derived compounds.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 3
Sequence:
MLRNNLGNSSDSKNEDGSVFSQTEHNIVATYLIMAGMISIISNIIVLGIFIKYKELRTPTNAIIINLAVTDIGVSSIGYPMSAASDLYGSWKFGYAGCQVYAGLNIFFGMASIGLLTVVAVDRYLTICLPDVGRRMTTNTYIGLILGAWINGLFWALMPIIGWASYAPDPTGATCTINWRKNDRSFVSYTMTVIAINFIVPLTVMFYCYYHVTLSIKHHTTSDCTESLNRDWSDQIDVTKMSVIMICMFLVAWSPYSIVCLWASFGDPKKIPPPMAIIAPLFAKSSTFYNPCIYVVANKKFRRAMLAMFKCQTHQTMPVTSILPMDVSQNPLASGRI
Protein: Gonadal soma derived factor variant 1 (Gonadal somatic cell derived factor precursor) (Gonadal somatic cell-derived factor) (B0ZE98)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Anti-Mullerian hormone
- Forkhead box protein L2
- Aromatase
- Doublesex- and mab-3-related transcription factor 1
- Cytochrome P450, family 11, subfamily C, polypeptide 1
- Transcription factor Sox-3
- Bone morphogenetic protein 15.
- Estradiol 17-beta-dehydrogenase 1
Sequence:
MLLRLVLLLLAFPLGEMFVLHPSPEDQSHSREQEIKKIILKSLHLPKEPSNSLSQLEHLRESLKNSIHSPPGNSSLPEDSGNSSCCRRSSQVLMKDLGWDGWVVLPESVAFVQCVSCGSGTSVQCCKPTAHHIVPFVYMDASGLVLSTVRLPRDCGCDLAEDTLDPAAMSPP
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4 (Hormone-regulated proliferation-associated protein of 20 kDa homolog) (Q9D1H6)
Organism: Mus musculus (Mouse)
Function: May be involved in cell proliferation and survival of hormone-dependent tumor cells. Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q9P032}; Lipid-anchor {ECO:0000250|UniProtKB:Q9P032}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- Complex I assembly factor TIMMDC1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex assembly factor 2
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Complex I intermediate-associated protein 30, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
Sequence:
MGARVTRALRNFNVEKRAEREISKRKPSMAPKHPSTRDLLQEHRSQYPEIEEVVSKKDNKLLSLLRDVYVDSKDPVPALPVKVEPRQEPKEFRLPIGNHFDKNITDIPKGKITVVEALTLLNNHKLSPETWTAEKIAQEYYLELKDVNSLLKYFVTFEVKILPPEDRKAIQSK
Protein: GEO12018p1 (IP04259p) (Sting-regulated gene 1) (Q9VC22)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
- FI09328p
- Uncharacterized protein, isoform A
- GH19118p
- Uncharacterized protein, isoform A
- RH15675p
Sequence:
MQLLAAILVLILASLAHGRPTFDKIAELLFGDPNHYPPARPVDPQLHPGPGPLIQEGYEQGYDYHYGGGYGYGGSHQQTHPGGYAYYPPRPVPAANDYYPPPWSVRPSPGYYSQPSHPASVHYPHKNQDLYGGGGGYKQRGY
Protein: Sex determination protein fox-1 (Feminizing locus on X protein 1) (Q10572)
Organism: Caenorhabditis elegans
Function: RNA-binding protein that regulates tissue-specific alternative splicing events by binding to 5'-UGCAUG-3' and 5'-GCACG-3' elements. Also binds to poly(A), poly(G), poly(C), or poly(U) stretches of RNA. Plays a role in the sex determination pathway and X chromosome dosage compensation, and together with sex-1 is involved in making the distinction between one and two X-chromosomes. Binds to 5'-GCAUG-3' and 5'-GCACG-3' elements in intron 6 of the pre-mRNA of the sex-determining factor xol-1 to promote its alternative splicing and together with sex-1 negatively regulates the expression of xol-1 to promote hermaphrodite development. Negatively regulates the expression of the active isoform of xol-1 (isoform b) by promoting intron 6 retention and the deletion of exon 7 coding sequences in hermaphrodite embryos. Furthermore, binding to the pre-mRNA of xol-1 can also direct the use of an alternative 3' splice site enabling the xol-1 transcript to be trans-spliced to unrelated genes on chromosome 2, which also leads to xol-1 exon 7 deletion. Does not seem to regulate the retention of introns 1 to 5 of xol-1 pre-mRNA. Plays a role in the association of the dosage compensation complex proteins dpy-27 and sdc-3 with the hermaphrodite X chromosomes. Binds to 5'-UGCAUG-3' elements in intron 7 of the pre-mRNA of unc-32 to promote its alternative splicing in neuronal tissues. Binds to 5'-UGCAUG-3' elements in intron 4 of the pre-mRNA of egl-15 to promote its alternative splicing in body wall muscle tissues. Promotes binding of RNA-binding protein sup-12 to target RNA. Plays a role in male mating behavior.
Subcellular location: Nucleus {ECO:0000269|PubMed:23468662, ECO:0000269|PubMed:9217163, ECO:0000305|PubMed:33372658}.
Interaction partners:
- XO lethal protein 1
- Steroid hormone receptor family member cnr14
- RRM domain-containing protein
- Signal element on autosome protein 2
- Putative RNA-binding protein
- Mec-8 protein
- K Homology domain-containing protein
- Homeobox protein ceh-39
- T-box transcription factor 18
- Myoblast growth factor receptor egl-15
Sequence:
MAELIEEVSTATHASLNACDPIVVNSEALPMQALYQLSATGAQQQNQQIPIGLSNSLLYQQLAAHQQIAAQQHQQQLAVSAAHQTQNNIMLATSAPSLINHMENSTDGKVKDDPNSDYDLQLSIQQQLAAAAQAAQMGQTQIGPQIVGQQGQPVVATTAGSTNGSAAVTQPDPSTSSGPDGPKRLHVSNIPFRFRDPDLKTMFEKFGVVSDVEIIFNERGSKGFGFVTMERPQDAERARQELHGSMIEGRKIEVNCATARVHSKKVKPTGGILDQMNPLMAQSALAAQAQMNRALLLRSPLVAQSLLGRGAALIPGMQQPAFQLQAALAGNPLAQLQGQPLLFNAAALQTNALQQSAFGMDPAAVQAALLANEQARFQLAAAAAQGRIPSSGNASAFGEQYLSNALATASLPSYQMNPALRTLNRFTPY
Protein: Uncharacterized protein (C8V1V6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- non-specific serine/threonine protein kinase
- Cytosolic regulator Pianissimo, putative
- Target of rapamycin complex subunit LST8
- Stress activated MAP kinase interacting protein, putative
- TORC1 growth control complex subunit Kog1, putative
Sequence:
MAGRASSGSQSSVAEQTNDRQEYLTIAWPAGLLGYCVNLSGIDSNHQIQISQHDNVCIVKNELLAVLITYSAPNLHRHCPLLEMLRSPVTVSPERSASRPPLPRSSSDFDDDPDRPGSSGSDASSVISNATAFQTTPHRRDRDRDREPDPSYSPRTVLRTPPTETSAAASASAQGPGHPPTSFMPHHDPTSRKPSGRVYPSDLHKRSRHHSQGFFEPSLPTASSSDATLSASRIAAQAAMQSQGQHSSSTIPQVPPKRAVQGHGSDNGSGSVSPPPPIPASQPQRPGSAGSPYQNSNATTGGHGVGQAAATTAANHVFPRLPPPGVEAHPNEREHKKTEKEKSKMKLFSKPKHIGISRDKDFKDRGLPSPNKISGLTRIVSASATNLADIYPSNNSSMYSLSNASASTVVPADKPSVPEKEKDKEKDKEKDKEKAHRHHHFLSRQKLKLKDLKDKDDHYNLPLSSAASNSRPSDPNAPQSLYSFTPASPSATTTSFSKSVGGLDLLHGGRALRDKKKEEKTLAEEQPEWLANSTVAGAATAGFAGPSSLGSTGGFLTEAVVRETLQGFGLHNMSPEDAWDFLKAKLLVIFDGEDVRIAIEDLNKLVIIHIQRCVQRRTPTAIVDDLRGLLEAGFATLNHTLNGVPDDKLVPHLVQIWMLMNIREAKNFWSLALDGEYPGCELEVRNLVLIAFRDMVIINRYDNLKATFSRLSLDSIKLGNSALSVTTKSSNNSNNGRPTTSASFDGGFGSYSSQSSTFLNTAGSFSSESPGYNRSRATSNTSSNPDQLIFQSFSSPSQRPTIIHRANNASDTSHVITETVGRMLQCMSVLASVQTNDTAQERIETLSKDLKHNWLGRGRTGRDRRGFVGTKIRPPIVAQASDNSTDSNMDELSSKRLQQELSVL
Protein: TERF1 (TRF1)-interacting nuclear factor 2 (TERF1-interacting nuclear factor 2) (F1R9M2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- ACD shelterin complex subunit and telomerase recruitment factor.
- Protection of telomeres protein 1
- Telomeric repeat-binding factor
- H/ACA ribonucleoprotein complex subunit 2-like protein
- H/ACA ribonucleoprotein complex subunit 3
- CST complex subunit CTC1
- Telomeric repeat-binding factor 2-interacting protein 1
- H/ACA ribonucleoprotein complex subunit DKC1
- Regulator of telomere elongation helicase 1
- Telomerase reverse transcriptase
Sequence:
MNRKTKTATRSLEKDQPLPMSALQLIAPPLRLLSAAMWKVMLQRDTVHYGKVEETITSLCETVPGLLDYRHQARLTMGLRALMILEELRQPDPPDAELVLQELKKLQMSSCIPNGKKKDQKVEEAKRNFQTLVQSLLKNPSARKQFYKEDFQLHYGRNYAASLEKLMWEFLIRLDQLLPVPDLAQTVSWLSAAPAVLEECARSASQPQLVRTLLQHEVCLGHLGSSSLLSSTGDAILSSLSLPLSGKVLQTIQSESTSASNRVTTPAQSTPRTTRRMAKQAQSQVAPVIGSISCVNLQINNEKVASESAKSASEVQRNTRTNLRSQSKKQVPEKEEEHYVGNLLFTVITQSSGSEVEEEEEEDGGKEDTSNTDESSERSFKLPQQTEVEQKNGSRVSGVTRKCSTKTNAEAAGSQDEGEISEILISCMKRNLRVVVPRLNISSNALPVQLNHLAEEKDGTSYSGQSNSKDRVRNRDSVQRKRRFPNSSPTPEKLLTLSVNKLAPACSPCIPLLKRLPVGTPETPSPLIKSSDDIIGDSDDERAGTVKRKVFNQQYCKTNNGTYVPTLREFWNPVFCPSSSPGSRH
Protein: Pectinesterase inhibitor 1 (Pectin methylesterase inhibitor 1) (AtPMEI1) (Q9LNF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inhibits pectin methylesterase (PME) from flowers and siliques. Inhibits PME from leaves.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:21223393}.
Interaction partners:
- Pectinesterase PPME1
- Pectinesterase inhibitor 5
- Pectinesterase inhibitor 4
- Pectinesterase inhibitor 10
- Pectinesterase inhibitor 3
- Pectinesterase inhibitor 12
- Pectinesterase inhibitor 11
- Pectinesterase 5
- Pectinesterase inhibitor 6
- AGAMOUS-like 98
Sequence:
MAANLRNNAFLSSLMFLLLIGSSYAITSSEMSTICDKTLNPSFCLKFLNTKFASPNLQALAKTTLDSTQARATQTLKKLQSIIDGGVDPRSKLAYRSCVDEYESAIGNLEEAFEHLASGDGMGMNMKVSAALDGADTCLDDVKRLRSVDSSVVNNSKTIKNLCGIALVISNMLPRN
Protein: Shugoshin (Meiotic protein S332) (Q24141)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a central role in chromosome cohesion during meiosis and mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. May act by protecting or Rad21 from cleavage by Sse/separase. Required during meiosis in both males and females.
Subcellular location: Chromosome, centromere {ECO:0000269|PubMed:10654079, ECO:0000269|PubMed:7585942, ECO:0000269|PubMed:9490715, ECO:0000269|PubMed:9869638}. Note=Localizes to the centromere of meiotic and mitotic chromosomes (PubMed:10654079, PubMed:9490715). During meiosis, it assembles onto centromeres during prometaphase I, remains attached until anaphase II, during which it is displaced from centromeres without being degraded (PubMed:9490715). Localization onto centromeres is independent of kinetochore formation and cohesin complex (PubMed:10985388). {ECO:0000269|PubMed:10654079, ECO:0000269|PubMed:10985388, ECO:0000269|PubMed:9490715}.
Interaction partners:
- separase
- Bub1-related kinase
- Borealin
- Aurora kinase B
- Protein ORD
- Inner centromere protein, isoform A
- Serine/threonine protein phosphatase 2A regulatory subunit
- Bub1 kinase, isoform A
- Protein wings apart-like
- Serine/threonine-protein phosphatase PP2A
Sequence:
MGSKVEQQYKLLNAELMDQVQKQRLEIGEYRKRVISLEREIMDIREEHVLQNHRQRMENISIVRSLMLSLNVDSDSLAVRQEPAPAAQINRPSGPRRSSREICKDMRRTCALARTTRPISPRRSSSVTSTVSSTSRRSSAEVQSEVVTTRIPEDRRANKPTPPPRRPAELVFDEDDSDDDFDEAVSPVEETQTEQNEENNRLFSIIEENGSEGESTDSSSSCEAIYCDTTFESSPPNAQVTVTPSGRALREVDTNIPVAVSLSRGKETGKGSWLAISVAVEDSPQEPSIQCPRLAVTRPSQSSGIFPDVNGLTPRRSLFNGIGKMAGSTSTPKSFLVEEMPSIRTRSRTAANKKSENTDMSSSFCNNSARPSRSCRPTSLVEPSLKNKLRNGSKGKAKAKK
Protein: Transmembrane and immunoglobulin domain-containing protein 1 (Q9D7L8)
Organism: Mus musculus (Mouse)
Function: May control cell-cell adhesion, cell migration and proliferation, cell morphology, and protects renal epithelial cells from oxidative cell injury to promote cell survival.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6UXZ0}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6UXZ0}. Cytoplasm {ECO:0000250|UniProtKB:Q6UXZ0}.
Interaction partners:
- Guanylin
- Clarin-3
Sequence:
MVWKITGPLQACQLLLVVLSLPQGRTSSVLTVNGRTENYILDTQHGVQASLECAVQNHTEDEELLWYREDGIVDLKNGNKINISSVCVSPINESDNGVRFTCKLQRDQTVSVTVVLNVTFPPLLSGNGFQTVEENSDVSLVCNVKSNPQAQMMWYKNNSALVLEKGRHQIHQTRESFQLSITKVKKSDNGTYSCIASSSLKMETMDFHLLVKDKVFVMPAEPIIAACVVVVLTMAFALFSRRKRIMKLCGKKNDPNSETAL
Protein: NAD-dependent protein deacetylase HST1 (EC 2.3.1.286) (Homologous to SIR2 protein 1) (Regulatory protein SIR2 homolog 1) (P53685)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: NAD-dependent histone deacetylase involved in telomeric silencing. Histone deacetylase proteins act via the formation of large multiprotein complexes that are responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Restores silencing at HMR in SIR2 mutants when overexpressed. Required to repress middle sporulation genes during vegetative growth. Acts as a sensor of NAD(+) levels and regulator of NAD(+) biosynthesis. Regulates the gene expression of de novo NAD(+) biosynthesis genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Note=But not nucleolar, and cytoplasmic.
Interaction partners:
- Suppressor of mar1-1 protein
- Repression factor of MSEs protein 1
- Probable DNA-binding protein SNT1
- SIR4-interacting protein SIF2
- SET domain-containing protein 3
- Protein HOS4
- Probable histone deacetylase HOS2
- Glutamine-dependent NAD
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
Sequence:
MNILLMQRIVSFILVVSQGRYFHVGELTMTMLKRPQEEESDNNATKKLKTRLTYPCILGKDKVTGKFIFPAITKDDVMNARLFLKDNDLKTFLEYFLPVEVNSIYIYFMIKLLGFDVKDKELFMALNSNITSNKERSSAELSSIHAKAEDEDELTDPLEKKHAVKLIKDLQKAINKVLSTRLRLPNFNTIDHFTATLRNAKKILVLTGAGVSTSLGIPDFRSSEGFYSKIRHLGLEDPQDVFNLDIFLQDPSVFYNIAHMVLPPENMYSPLHSFIKMLQDKGKLLRNYTQNIDNLESYAGIDPDKLVQCHGSFATASCVTCHWQIPGEKIFENIRNLELPLCPYCYQKRKQYFPMSNGNNTVQTNINFNSPILKSYGVLKPDMTFFGEALPSRFHKTIRKDILECDLLICIGTSLKVAPVSEIVNMVPSHVPQILINRDMVTHAEFDLNLLGFCDDVASLVAKKCHWDIPHKKWQDLKKIDYNCTEIDKGTYKIKKQPRKKQQ