wanglab/gogpt-training-data huggingface dataset:
Protein: Protein O-mannosyl-transferase 2 (EC 2.4.1.109) (Dolichyl-phosphate-mannose--protein mannosyltransferase 2) (Q9UKY4)
Organism: Homo sapiens (Human)
Function: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. Essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12460945, ECO:0000269|PubMed:14699049}; Multi-pass membrane protein {ECO:0000269|PubMed:12460945, ECO:0000269|PubMed:14699049}.
Interaction partners:
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Protein O-mannosyl-transferase 1
- Dystroglycan 1
- Ribitol 5-phosphate transferase FKRP
- Ribitol-5-phosphate transferase FKTN
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Ribitol-5-phosphate xylosyltransferase 1
- Xylosyl- and glucuronyltransferase LARGE1
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
Sequence:
MPPATGGGLAESELRPRRGRCGPQAARAAGRDVAAEAVARSPKRPAWGSRRFEAVGWWALLALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKYEHHSYMGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNSCADRPFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFAVHFMVLSKSGPGDGFFSSAFQARLSGNNLHNASIPEHLAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPLDPSFPVEFVRHGDIIRLEHKETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDHINPKLPNISLDVLQPSFPEILLESHMVMIRGNSGLKPKDNEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQRGARLPAEVAGLSQVLLRGGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPLARGIHVAGILSLLLGTAYSFYLFHPLAYGMVGPLAQDPQSPMAGLRWLDSWDF
Protein: Diuretic hormone 44 receptor 2, isoform A (IP10431p) (Q4V3E9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MADDDLRALVDSLDDASQEDLAKVIANFSVDMLQRASALIGAQQGSSGGQLQNRTLQCQQQQQREEEQASLEALASGGKRILQCPSSFDSVLCWPRTNAGSLAVLPCFEEFKGVHYDTTDNATRFCFPNGTWDHYSDYDRCHQNSGSIPVVPDFSPNVELPAIIYAGGYFLSFATLVVALIIFLSFKDLRCLRNTIHANLFLTYITSALLWILTLFLQVITTESSQAGCITLVIMFQYFYLTNFFWMFVEGLYLYTLVVQTFSSDNISFIIYALIGWGCPAVCILVWSIAKAFAPHLENEHFNGLEIDCAWMRESHIDWIFKVPASLALLVNLVFLIRIMWVLITKLRSAHTLETRQYYKASKALLVLIPLFGITYLLVLTGPEQGISRNLFEAIRAFLISTQGFFVALFYCFLNSEVRQTLRHGFTRWRESRNIHRNSSIKNRRHRASKDYSLRSRTESLRLTSTSPIPTGHYE
Protein: Transport protein particle (TRAPP) subunit, putative (Q38DI4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
- Transport protein particle
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Uncharacterized protein
- Trafficking protein particle complex subunit 11 C-terminal domain-containing protein
- COP9 signalosome complex subunit 4
- Trafficking protein particle complex subunit 11 domain-containing protein
- Trafficking protein particle complex subunit 11 domain-containing protein
Sequence:
MLNRDGTRSNRSSVRLTSDEGKVSLSAFSFLFSELCTRAHSTPTKARDIEEIEQRLTSLGAIVGAKLMMLSSLKDPLELQRRPTTIDEALKLLQEKFWTRWFGKAANDLQQEGESTRYFLVDSNPMVLQHVYPSPEYMDSEGQWSINYASFMGGIVEGALRAVGFDADVLTYHHPEPDKPQQSIFAISFAQHVHDRERRIRD
Protein: SAP DNA-binding domain-containing protein (Q54TP5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Probable serine/threonine-protein kinase qkgA
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase roco11
- EGF-like domain-containing protein
- GH84 domain-containing protein
- PA14 domain-containing protein
- PA14 domain-containing protein
- PA14 domain-containing protein
Sequence:
MNKRTRDKNDLDLNEEEGINNKKLKEDNDSSSNIVKSYENEFESFKLKKIGGELSIKKLQTILKDIGLPHSGRKVDLINRIEQYYNIKIKLEKEVEQQQNNNPFNKSQPILLIKNDYEIPFWKVFRNKSIFKNIFSNFKYSNIFNYSRLYSVNNIFNDFNNCIEIIRDKVKSNSYLAFKQIKDLDEYSIKTNETTDEDGLIKILDSFKEETQENRLFYTRFINNYCNKSIHPLILLGRIVKASNLLALKSFLNTEIYVKSKIQIKIEINKFSDLQILEFLINKYYRNNDDNNKKEKESEKESEKESEKEKEKEKESEKEKESEKEKESEKESEKDSEKDSEKEKEKEKEKEKEKEKEKEKEKEKEEKEELIQKDLNENEIDNLKKLKEGSEGNDNDKKKDEQDENLVFIESIRINDFNIFKELKLGELIHLAKTIYQNEKIVKLLELPTYHKVSIDFPEYIFFSLGEEFKNDYIIERIRESKLDFSNKIKEGLSFFNEIKEFQFTDKELNENLFMLLKPLTNWDRHFSKLNDKYNNNNNNNNNNNINNNSNEQGCELSLVKYNILELYNNKLRKNYQRLEEYFRFQRYEFAQKDFKEISSIHKEQIEIEKEIESLFQKENEFIEKQNEKDRLLESDEICKKKKIVLGYIFLLFNLSMPRRKPIEYYLSFKDEKKVIAYGTQMKDEFLNYGIPNNEILSRISEIGYGSNTRDRFKMIMNSKFLIEKPFKEHFINPLNSPLIIANVKSKDMLDLLFKNFNQQFFKDNNRNWKYCNSIEIIEYYEKLMQSLGRKFLFSFDFANRCTIECKGIDIYPKLLSRAISNPTLYNHSSNLAPKERLLKINDRTIVKQRAFLSLLELNYFKTITFDRSFTFNKYSYKISRWISDNCISNISKLNFNDNGYTKIKIQLPNKKRKNNNNNNNNNNNNNKNNNKNGKEEEIEEESTTYDGYGYNSDNSYDSDDYDDYDNYDNYDDYGDSDDSDDYLNFAHDDDSNYENDNEDEDHPQDYSNMAITTAATVTATATTTTAPTTTTATTATTTAPTATTTTTDNGKSDNGKEDDDDGIIMIILNQSQLIDILYNSNRLDDIFKFKRDYKFSNRNFFRKVGPHIPLSLVEILLKNSNFIKIGIDIQEFLNYLVLIGNLPIIKYLNLNFSHFFTKNQRTKDLKSLLSTAIRYDYPQIAEILFVYIKLTRYEFRKEVQTDFSLVDSLYYNNLW
Protein: Transcription initiation factor TFIID subunit 4B (Transcription initiation factor TFIID 105 kDa subunit) (TAF(II)105) (TAFII-105) (TAFII105) (G5E8Z2)
Organism: Mus musculus (Mouse)
Function: Cell type-specific subunit of the general transcription factor TFIID that may function as a gene-selective coactivator in certain cells. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators asond repressors. TAF4B is a transcriptional coactivator of the p65/RELA NF-kappa-B subunit. Involved in the activation of a subset of antiapoptotic genes including TNFAIP3. Through interaction with OCBA/POU2AF1, acts as a coactivator of B-cell-specific transcription. Plays a role in spermiogenesis and oogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q92750}. Cytoplasm {ECO:0000250|UniProtKB:Q92750}. Note=Export into the cytoplasm is mediated by a CRM1-independent nuclear export pathway and not by phosphorylation. {ECO:0000250|UniProtKB:Q92750}.
Interaction partners:
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 3
- TATA-box-binding protein
Sequence:
MPAGLTEPAGAAAPVVSSASGAVTMAPVAALPVRVEGTPVALGPVTKAPVSVCVESVAPQPLPAPVGTLVTKVVPVTALPKLGSPRLPAPQIVTVKTPGTTTIQLPANLQLPPGTVLIKSNSGQLMLVSPQQAVTGAKTTSNITPRPAVPANTQTVKICTVPNSSSQLMKKVTVAPVKNLTQIGTTVATTASSTSSGQPVALPSSVITVTPAKLVNTVSTLKSSSLGVLSTPSNDARLKAETSVAAQTALPPTVLENVKKCKNFLSMLIKLACSGSQSPEMGQNVKRLVEQLLDAEIEAEEFTRKLYIELKSAPQPHLVPFLKKSVVALRQLLPNSQSFIENCVKEVSGDVVISSCTMTTATSPVVTSTVSPVLVSGATAPRTLSVQQTLNPLAGPGVANTGVVTLHSVAPAAATGGTTAATVLLQTSKPLTTSVPNTVAAVSLQPENPVVSGAAVTLAIPSATFGEASATPLCLPSAKPAITSAGTKADKPAIGTPVQIVTQPSTLLPQAAGIPQTAKVKQLVVQQPSGSSVNHVTSISHSSPLSTQNCGQKTPVNAVMPTSSIIKQITLPGNKLLSLQAQRSSIQSNKIKENGPTCFRGEDDINDVTFMAEVNLDEENACILAAHSDFVGTLIQSCKEEPFLVIGALQKRILDIGKKHDITELNSDAVNLISHATQERLRGLLEKLTTIAQHRMTIYKGSENYILSTDTRSQLKFLEKLDQLEKQRKDLEEREMLLKAAKSRSNKEDPEQLRLKQKAKELQQLELAQIQYRDANLTALAAIGPRKKRPLESGNESFKDNPSTSGTSSLTATKPFRPRITRICLRDLIFCMEQEREMKYSRALYLALLK
Protein: Mediator of RNA polymerase II transcription subunit 13 (A0A8I5YBV3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364134}.
Interaction partners:
Sequence:
MSSSFVSNGASLEDCHCNLFCLADLTGIKWKRYVWQGPTSAPILFPVTEEDPILSSFSRCLKADVLGVWRRDQRPGRRELWIFWWGKDPNFADLIHHDLSEEEDGVWENGLSYECRTLLFKAVHNLLERCLMNRNFVRIGKWFVKPYEKDEKPINKSEHLSCSFTFFLHGDSNVCTSVEINQHQPVYLLSEEHVTLAQQSNSPFQVILSPFGLNGTLTGQAFKMSDSATKKLIGEWKQFYPISCGLKEMSEEKQEDMDWEDDSLAAVEVLVAGVRMIYPACFVLVPQSDIPTPSSVGSSHCSASCLGIHQVPASTRDPAMSSVTLTPPTSPEEVQSVDPQSAQKWVKFSSVSDGFSTDSTSHHGGKIPRKLANHVVDRVWQECNMNRLQNKRKYSATSSGLCEEETADKIGSWDFVEATQRTSCSCLRHKSLKTRNTGQQGQAPSLGQQQQILPKHKTNEKQEKSEKPQKRPLTPFHHRVSISDDIGMDTDSASQRLVISAADSQVRFTNIRTNDVAKTPQMHGTELANSPQPPPLSPHPCDVVDEGVTKTPSTPQSQHFYQMPTPDPLVPTKPMEDRIDSLSQSFPPPFQEAVEPTVYVGTAVSLEEDEANVAWKYYKVPKKKDVEFLPPQLPNDKFKDDPVGPFGQESVTSVTELMVQCKKPLKVSDEIVQQYQIKNQYLSAIASDTEQEPKIDPYAFVEGDEEFIFTDKKDRQNSEREAGKKHKVEDGTSAVTVLSHEEDAMSLFSPSKQDAPRPANHARPPSTSLIYDSDLAVSYTDLDNLFNSDEDELTPGSKKSASGSDDKASSKESKTGSLDPLSCISTADLHKMYPTPPSLEQHIMGFSPMNMNNKEYGSMDPTPGGTVLEGSSSSVGTQFRIEVEEGFCSPKPSEIKDFSYVYKPENCQVLVGCSMFAPLKTLPSHCLPPIKLPEECVYRQSWTVGKLDLLPSGPSMPFIKEGDGSNLDQDYGPAYTPQIHTSFGMPPSSAPPSNGGAGILPSPSTPRFPTPRTPRTPRTPRGAGGPASAQGSVKYENSDLYSPASTPSTCRPLNSVEPATVPSIPEAHSLYVNLILSESVMNLFKDCNFDSCCICVCNMNIKGADVGVYIPDPTQEAQYRCTCGFSAVMNRKFGNNSGLFLEDELDIIGRNTDCGKEAEKRFEALRASSVENVNGSLKESEKVPDELILLLQDQCTNLFSPFGAADHDPFPKAGISSNWVRVEERDCCSDCCLALEHGRQFMDNMSGGKVDEALVRSSCLHPWAKQNDASVQCSQDILRMLLSLQPVLQDAIQKKRTVRPWGVQGPLTWQQFHKMAGRGSYGTDESPEPLPIPTFLLGYDYDFLVLSPFALPYWEKLMLEPYGSQRDIAYVVLCPENEALLNGARSFFRDLTAIYESCRLGQHRPISRLLTDGIMKVGATASKKLSEKFVTEWFSQAADGNNEAFSKLKLYAQVCRYDLGPYLASQPLDSSLLSQPNLVAPPNQSLVTAPQMTNTGNANAPSATLASAASSTMTLTPGVAISTSVATANSTLTTTSSSSSSSMSSGVSSNKLPSFPPFGSMNTSGTGSMSAQGSTVQSGQLGGQQSSSLQAAGISGESASLPTQPHPDVSESTMDRDKVGIPTDGDSHAITYPPAIVVYIIDPFTYENKDESTSSSNVWTLGLLRCFLEMLQTLPPHIKSTVSVQIVPCQYLLQPVKHDDRQIYSQHLKSLAFSAFTQCRRPLPTSTNVKTLTGFGPGLAMETALKSPDRPECIRLYTPPFILAPVKDKQTELGETFGEAGQKYNVLFVGYCLSHDQRWILASCTDLYGELLETCIINIDVPNRARRKKGSARRFGLQKLWEWCLGLVQMSSLPWRVVIGRLGRIGHGELKDWSCLLSRRNLQSLSKRLKDMCRMCGISAADSPSILSACLVAMEPQGSFVIMPDSVSTGSVFGRSTTLNMQTPQLNTPQDTSCTHILVFPTSASVQVASATYTTENLDLAFNPNNDGADGMGIFDLLDTGDDLDPDIINILPASPTTSPVHSPGSHYPHGGDAGKGQGTDRLLSTESHDEVTNILQQPLALGYFVSTAKAGPLPDWFWSACPQAQYQCPLFLKRG
Protein: Lysine-specific demethylase JMJ18 (EC 1.14.11.-) (Jumonji domain-containing protein 18) (AtJMJ18) (Protein JUMONJI 18) (Lysine-specific histone demethylase JMJ18) ([histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ18) (F4I6G4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a specific activity for H3K4me3 and H3K4me2. No activity on H3K9me3/2, H3K27me3/2 and H3K36me3/2. Involved in the control of flowering time by demethylating H3K4me3 at the FLC locus and repressing its expression. The repression of FLC level and reduction in H3K4me3 at the FLC locus results in induction of the flowering activator FT, which is a downstream target of FLC.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:22536163}.
Interaction partners:
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit d, mitochondrial
- ATPase, F1 complex, OSCP/delta subunit protein
- ATP synthase subunit O, mitochondrial
- ATP synthase subunit delta, chloroplastic
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- ATP synthase subunit a.
- ATP synthase subunit a-2
- ATP synthase subunit a-1
- ATP synthase subunit a, chloroplastic
Sequence:
MENPPLESEIKEDMSLKNHPPDKDKDKDTIMEQPSSPRHRKVVARWLPDEAQRPIINDAPVFTPSLEEFVDPLAYIEKIRPLAEPYGICRIIPPSTWKPPCRLKEKSIWEQTKFPTRIQTVDLLQNREPMKKKPKSRKRKRRRNSRMGSSKRRSGSSPAESTSSPEAEEKFGFNSGSDFTLDEFEKYALHFKDSYFEKKDSGGDIVKWTPSVDDIEGEYWRIVEQPTDEVEVYYGADLENGVLGSGFYKRAEKFTGSDMEQYTLSGWNLNNLPRLPGSVLSFEDCDISGVLVPWLYVGMCFSSFCWHVEDHHLYSLNYHHFGEPKVWYGVPGSNATALEKAMRKHLPDLFEEQPDLLHGLVTQFSPSILKDEGVQAYRVVQNSGEYVLTFPRAYHAGFNCGFNCAEAVNVAPVDWLAHGQNAVELYSKETRKTSLSHDKLLLGAAYEAVKALWELSASEGKENTTNLRWKSFCGKNGTLTNAIQARLQMEEGRITALGRDSSSLKKMEKDFDSNCERECFSCFYDLHLSASGCKCSPEEYACLKHADDLCSCDVKDGFILLRYTMDELSSLVRALEGESDDLKIWASKVLGIEHSDEDQTKTSSVISEEKKLKEGSFDLNIDLEMDYQEDVKEEASTSGGELTASENLGVSVEPINLGFLIFGKLWCNKYAIFPKGFRSRVKFYNVLDPTRMSNYISEVLDAGLMGPLFRVTLEESPDESFFNVSAQQCWEMVMRRVKDTSTSLGLPILPQFESINGLQMFGFLSPSIVQAIEALDPNHRLVEYWNHKNQTSSDSKDHFISSNCSASLTKGKLFGVDLM
Protein: Putative calcium-transporting ATPase 11, plasma membrane-type (EC 7.2.2.10) (Ca(2+)-ATPase isoform 11) (Q9M2L4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol out of the cell or into organelles.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Vacuolar cation/proton exchanger 1
- Vacuolar cation/proton exchanger 3
- Vacuolar cation/proton exchanger 4
- Alpha carbonic anhydrase 2
- Alpha carbonic anhydrase 4
- Vacuolar cation/proton exchanger 2
- F-box/LRR-repeat protein 15
Sequence:
MSNLLKDFEVASKNPSLEARQRWRSSVGLVKNRARRFRMISNLDKLAENEKKRCQIQEKIRVVFYVQKAAFQFIDAGARPEYKLTDEVKKAGFYVEADELASMVRNHDTKSLTKIGGPEGIAQKVSVSLAEGVRSSELHIREKIYGENRYTEKPARSFLTFVWEALQDITLIILMVCAVVSIGVGVATEGFPKGMYDGTGILLSIILVVMVTAISDYKQSLQFRDLDREKKKIIIQVTRDGSRQEVSIHDLVVGDVVHLSIGDQVPADGIFISGYNLEIDESSLSGESEPSHVNKEKPFLLSGTKVQNGSAKMLVTTVGMRTEWGKLMDTLSEGGEDETPLQVKLNGVATIIGKIGLGFAVLTFVVLCIRFVVEKATAGSITEWSSEDALTLLDYFAIAVTIIVVAVPEGLPLAVTLSLAFAMKQLMSDRALVRHLAACETMGSSTCICTDKTGTLTTNHMVVNKVWICENIKERQEENFQLNLSEQVKNILIQAIFQNTGSEVVKDKEGKTQILGSPTERAILEFGLLLGGDVDTQRREHKILKIEPFNSDKKKMSVLTSHSGGKVRAFCKGASEIVLKMCEKVVDSNGESVPLSEEKIASISDVIEGFASEALRTLCLVYTDLDEAPRGDLPNGGYTLVAVVGIKDPVRPGVREAVQTCQAAGITVRMVTGDNISTAKAIAKECGILTAGGVAIEGSDFRNLPPHEMRAILPKIQVMARSLPLDKHTLVNNLRKMGEVVAVTGDGTNDAPALHEADIGLAMGIAGTEVAKENADVIIMDDNFATIVNVAKWGRAVYINIQKFVQFQLTVNVVALIINFVSACITGSAPLTAVQLLWVNMIMDTLGALALATEPPNEGLMKRQPIGRTASFITRAMWRNIIGQSIYQLIVLGILNFAGKQILNLNGPDSTIVLNTIIFNSFVFCQVFNEVNSREIEKINVFEGMFKSWVFVAVMTATVGFQVIIVEFLGAFASTVPLSWQHWLLCILIGSVSMILAVGLKCIPVESNRHHDGYELLPSGPSDSA
Protein: Cadherin-2 (Neural cadherin) (N-cadherin) (Parachute) (ZNCAD) (Q90275)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion (By similarity). Cadherins contribute to the sorting of heterogeneous cell types, and thereby play an important role during embryonic development. Required for normal neural tube morphogenesis. Required to allow mid- and hindbrain neurons to reach and maintain their appropriate positions within the neural tube by restricting neuronal motility within the embryonic mid- and hindbrain. Required for proper neurite branching. Required for pre- and postsynaptic organization (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:21115806}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction {ECO:0000269|PubMed:10456847}. Cell surface {ECO:0000250|UniProtKB:P15116}. Cell junction, desmosome {ECO:0000250|UniProtKB:P15116}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P15116}.
Interaction partners:
- Catenin beta-1
- Junction plakoglobin a.
- Actin alpha 1, skeletal muscle b.
- Cadherin 1, type 1, E-cadherin
- Protocadherin-19
- Gap junction alpha-1 protein
- Catenin alpha-2
- Catenin alpha-1
- Zinc finger protein SNAI2
- Tight junction protein 1a
Sequence:
MYPSGGVMLGLLAALQVAVQGTGAMPCQPGFTENEYNVMTADVITEGQVLLKVDFVDCGRGSGLRFESGDPADFRIDADGTVMAARTLQLTDRKGQSLEIKAKDENSQEQWMVHINFTQPKQVPVILFPRHSVLVKGDDSVNRVKRDWVIPPVNVLENSRKQFPEELVKIQSDKDKSNTLRYSVTGPGADQNPTGLFIIDPISGLLSVTKPLDREHIPNFHLRAHAVDINGNQMENPIDIIINVIDMNDNRPEFTHQIWNGTVDEGAKPGTFVMTVTSQDKDDPNTANGMLRYKILSQTPESPSSNMFTINNKTGKIITVAAGLDREKVPQYTLIIQATDMEGNPTYGLSNTATAVIRLLDVNDNAPEFTRETFHGEVPENRVNVIVTNLTVTDKDEPGTPAWNAVYRIISGDPTGRFSIPTDPVTNEGLVTVVKPVDFEMNRSFMLTVVADNEVPLASGIHRTRQSTATVSIRVIDVNESPNFDPNPKQIKLEEGLPQWSMLTTFTAHDPDRYMQQTISYSKLYDPANWLEIDPNNGRISTIAVLDRESPYVKNNLYNATFMASDNGVPRASGTGTLQIYLLDINDNAPRVFPQEAEVCERPEPNAINITAVDGDLNPNAGPYAFELPNRPSDIRRNWTLTRISGDHAQLSLKISYLESGIYELPISITDSGNLPMSNTTYLRIKVCQCDHHGDCVDMERIMAAGLGTGAIIAILICIIILLVLVLMFVMWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTLEPDMIKPVGIRRLDERPMHSEPNYPIRSAAPHPGDIGEFIHEGLKAADTDPTAPPYDSLLVFDYEGSGSTAGSLSSLHSSSSGGDQDYDYLNDWGPRFRKLADMYGGNDD
Protein: DNA primase (EC 2.7.7.-) (DNA priming protein) (P04520)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Synthesizes short RNA primers for the lagging strand DNA replication. The primase synthesizes short RNA primers on the lagging strand that the polymerase elongates using dNTPs. Recognizes two trinucleotide sequences 5'-GTT-3' and 5'-GCT-3' in vitro, but uses only the first as the priming site in vivo.
Interaction partners:
Sequence:
MSSIPWIDNEFAYRALAHLPKFTQVNNSSTFKLRFRCPVCGDSKTDQNKARGWYYGDNNEGNIHCYNCNYHAPIGIYLKEFEPDLYREYIFEIRKEKGKSRPIEKPKELPKQPEKKIIKSLPSCVRLDKLAEDHPIIKYVKARCIPKDKWKYLWFTTEWPKLVNSIAPGTYKKEISEPRLVIPIYNANGKAESFQGRALKKDAPQKYITIEAYPEATKIYGVERVKDGDVYVLEGPIDSLFIENGIAITGGQLDLEVVPFKDRRVWVLDNEPRHPDTIKRMTKLVDAGERVMFWDKSPWKSKDVNDMIRKEGATPEQIMEYMKNNIAQGLMAKMRLSKYAKI
Protein: Ribosome biogenesis protein NSA2 homolog (G5EFH0)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU367114}.
Interaction partners:
- Nucleolar GTP-binding protein 1
- Pescadillo homolog
- Large ribosomal subunit protein eL31
- Probable ribosome biogenesis protein RLP24
- Large ribosomal subunit protein uL30
- Nucleolar GTP-binding protein 2
- Brix domain-containing protein F44G4.1
- Guanine nucleotide-binding protein-like 3 homolog
- Ribosome biogenesis protein BOP1 homolog
- 60S ribosome subunit biogenesis protein NIP7 homolog
Sequence:
MPQNEHIELHRKRHGRRLDHEERQRKKLARAAHDRSQMAKTLRGHKAKLYHKKRYSEKVEMRKLLKQHEEKDQKNTVEQPDKGAVPAYLLDRQQQTSGTVLSNMIKQKRKQKAGKFNVPIPQVRAVSDAEAFKVVKTGKTNRKGWKRMVTKVTFVGESFTRKPAKFERFIRPMGLRFKKAHVTHPELQTTFHLPIVGVKKNPSSQMYTSLGVITKGTILEVNVSELGMVTQGGKVVWGKFAQVTNNPENDGCINAVLLI
Protein: Ubiquitin-like protein ATG12 (Autophagy-related protein 12) (P38316)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes. ATG12-ATG5 rearranges the ATG3 catalytic center and enhances its E2 activity.
Subcellular location: Preautophagosomal structure membrane {ECO:0000269|PubMed:10712513, ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:23064152, ECO:0000269|PubMed:23549786, ECO:0000269|PubMed:9759731}; Peripheral membrane protein {ECO:0000269|PubMed:10712513, ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:23064152, ECO:0000269|PubMed:23549786, ECO:0000269|PubMed:9759731}. Note=Localizes to the isolation membrane (IM), a membrane sac which is generated from the pre-autophagosomal structure (PAS). Ultimately, the IM expands to become a mature autophagosome. Also localizes to a dot at the junction between the IM and the vacuolar membrane, termed the vacuole-IM contact site (VICS).
Interaction partners:
- Autophagy-related protein 8
- Ubiquitin-like-conjugating enzyme ATG10
- Autophagy protein 16
- Autophagy-related protein 3
- Ubiquitin-like modifier-activating enzyme ATG7
- Serine/threonine-protein kinase ATG1
- Autophagy protein 5
- Putative lipase ATG15
- Autophagy-related protein 18
- Cysteine protease ATG4
Sequence:
MSRILESENETESDESSIISTNNGTAMERSRNNQELRSSPHTVQNRLELFSRRLSQLGLASDISVDQQVEDSSSGTYEQEETIKTNAQTSKQKSHKDEKNIQKIQIKFQPIGSIGQLKPSVCKISMSQSFAMVILFLKRRLKMDHVYCYINNSFAPSPQQNIGELWMQFKTNDELIVSYCASVAFG
Protein: LD29322p (Q9VH64)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Vitellogenin receptor Yl
- DNA repair protein SWI5 homolog
- ATP synthase F
- FI02878p
Sequence:
MVRSALVVAAIALSVLIALQGVDADKKQSKKYSKEANDPHFQQVKQEKYDPDFKSIQRPFRMAKLNLVWAKAQNRLTEPKLKSLYMELKIHDKEEIAWKQLNSQHKDKDGLKADELRRKLIGIMSSYDLLEHFDDTQDTEKLKPYKKFHDAEERHRNKSLFKDKKLNRLWEKAEISGFTAEELKSLKQEFDHHQDKVDVYYSLLENIGTVDTDKHENAINTEDLDTYNLISNDVNENDIKTHAQNVKSFENDLNTLRGHHTGIKDHYDRLERLVSSGPHSQDFIEPKVQGLWRVAQASNFTVKELESIKTELHHFESRLLKLRHLHAEHALQKEKYKGEKVKDKSSRFEEMEDQLKKQTRKVEKLQENIEKTIFKHTEL
Protein: Large ribosomal subunit protein mL54 (Q9S799)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Class I peptide chain release factor
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein bL27c
- AT5g15220/F8M21_110
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Small ribosomal subunit protein bS18c
- Small ribosomal subunit protein bS18c
Sequence:
MNRIGLIRGSSSKDVVRRTFAAAASKAKKGGKGGGASDAPKGSSLTKEIKSTTVVGANTLKDGSDPKILPDSDYPDWLWHLLDKRPALSELRRKNVETLPYDDLKRFVKLDTRGKIKENNSIKAKN
Protein: Uncharacterized membrane protein YahN (P75693)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Arginine exporter protein ArgO
- Aromatic amino acid exporter YddG
- Lysine exporter LysO
- L-alanine exporter AlaE
Sequence:
MMQLVHLFMDEITMDPLHAVYLTVGLFVITFFNPGANLFVVVQTSLASGRRAGVLTGLGVALGDAFYSGLGLFGLATLITQCEEIFSLIRIVGGAYLLWFAWCSMRRQSTPQMSTLQQPISAPWYVFFRRGLITDLSNPQTVLFFISIFSVTLNAETPTWARLMAWAGIVLASIIWRVFLSQAFSLPAVRRAYGRMQRVASRVIGAIIGVFALRLIYEGVTQR
Protein: Glutathione S-transferase, putative (EC 2.5.1.18) (Q4WGM0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Glutathione reductase
- Glutathione synthetase
- glutathione-specific gamma-glutamylcyclotransferase
Sequence:
MSLKPIVLWSHVMGPNPLKVVFILEQLGIPYEQKYLATDQVKKEPFVNINPNGRVPAIEDPNTGITLWESGAILEYLVETYDKQNTISFPTGSPEYFQAKQWLHFQMSGQGPYFGQAVWFTIYHPEKVDSAKERYYNEIRRVCGVLNKYLQNREYLVGDKFSYVDAAFVPWFRIIPAITGDAIELGKDFPNLDAWLKRLHALPAISKAFKIQEAAKAAQENTWINELNCV
Protein: Futalosine hydrolase (FL hydrolase) (EC 3.2.2.26) (Futalosine nucleosidase) (Menaquinone biosynthetic enzyme MqnB) (Q5SKT7)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Catalyzes the hydrolysis of futalosine (FL) to dehypoxanthine futalosine (DHFL) and hypoxanthine, a step in the biosynthesis of menaquinone (MK, vitamin K2). Is highly specific to futalosine since it does not accept aminodeoxyfutalosine (AFL), or any structurally related nucleotides and nucleosides as substrate.
Interaction partners:
Sequence:
MWLLLSPTRLEAPFLEGEPFAFLAWRGLKGTGFVYLETGIGKVNAAMALAAYAARNPVEKALLFGLAGAYPGGPSLGEAVLVEEEVEADLGLKEGLAPLGFPALALGERRYFNRFPLDPGLTGELARGLGLKVAVGLTRDLVSETPEEALALARRWGASLENMEGAAFARACLALGVRGAELRALSNPAGVRDKAHWRTKEALSALARAVRRLLAEEGGARRPPG
Protein: Homogentisate 1,2-dioxygenase (EC 1.13.11.5) (Homogentisate oxygenase) (Homogentisic acid oxidase) (Homogentisicase) (Q9ZRA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 4-hydroxyphenylpyruvate dioxygenase
- Glutathione S-transferase Z2
- Glutathione S-transferase Z1
- Fumarylacetoacetase
- Oxaloacetate tautomerase FAHD1, mitochondrial
- At5g13560
- Oxaloacetate tautomerase FAHD2, mitochondrial
- Aspartate aminotransferase, cytoplasmic isozyme 2
- Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial
- Alpha-aminoadipic semialdehyde synthase
Sequence:
MEEKKKELEELKYQSGFGNHFSSEAIAGALPLDQNSPLLCPYGLYAEQISGTSFTSPRKLNQRSWLYRVKPSVTHEPFKPRVPAHKKLVSEFDASNSRTNPTQLRWRPEDIPDSEIDFVDGLFTICGAGSSFLRHGFAIHMYVANTGMKDSAFCNADGDFLLVPQTGRLWIETECGRLLVTPGEIAVIPQGFRFSIDLPDGKSRGYVAEIYGAHFQLPDLGPIGANGLAASRDFLAPTAWFEDGLRPEYTIVQKFGGELFTAKQDFSPFNVVAWHGNYVPYKYDLKKFCPYNTVLLDHGDPSINTVLTAPTDKPGVALLDFVIFPPRWLVAEHTFRPPYYHRNCMSEFMGLIYGAYEAKADGFLPGGASLHSCMTPHGPDTTTYEATIARVNAMAPSKLTGTMAFMFESALIPRVCHWALESPFLDHDYYQCWIGLKSHFSRISLDKTNVESTEKEPGASE