wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleoporin nup60 (Nuclear pore protein nup60) (O74500)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (By similarity).
Subcellular location: Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Nucleoplasmic side {ECO:0000250}.
Interaction partners:
- Importin subunit beta-1
- Nucleoporin pom152
- Importin subunit alpha-2
- Meiotically up-regulated gene 31 protein
- mRNA export factor gle1
- mRNA export factor mex67
- Probable importin subunit beta-4
- Nucleoporin nup124
- Tropomyosin
- Myosin regulatory light chain 1
Sequence:
MSSGPIRTLHKGKAARNRTPYDRIAASKDGNHSNGPQTPSKSIFQRAKEWLTPSSWKKAISIFSSPVVNKHEDSFDSKTDEEYLQNVSTTTEDVSMLINTPVTEKYEQEHRDTSAQATPSIVEQSPNQMLANFFSKKGKTPLNEIEKEGIISILNKSASPSSSVISPAASLNRFQTPRAAAISKRESGVSSEPRARTSSLTPGNTPNSAKQWSAFRSTFSPLREQDQLSTISPNSLLPAQRLSYYGPTLSTPYNRRLRHKRHSTTPISLSNSIAPSLSFQPKKARYESANVSFNDTSFTNVPTSSPLHQSTTANHPEKTPSRAAASLLSILDSKEKNTPSITAKAGSPQSAPSKASYISPYARPGITTSRRRHDQIRPSSEKSEPEKKEPSAFETLEKSSNVQTYKPSLMPEFLEKASTHGSFAKQKEGEQTSLSEKTALSEPENKTPVFSFKAPSATTDKPSPPVSSIFSFNAPSAASTKPSPAVSSTFSFNAPTTTPSATSFSIINKEKPARSPNETIDVDLEEEGSGISAEVEVANEGEDLQKNATEVKASTSEKPVFRFEAVTDEKNSEVSSSNQASSSTMISQPNTGFSFGSFNKPAGQEEKPQQRSLFSASFTTQKPELPAAKIEPEVQMTNVAIDQRSFEQAEKSPISVSESTSLVEVEKPSAEGTNEHKQDATMTLEKTDKQGSLEEEPFPKFSFTVLPKENGENLSTMESTQELPKFSFSVLKEEKN
Protein: Hibris (Q9V787)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MQFWITLTFAVHLATTICHVMAAVTAPTPAAQVAAPPVQKFHLTPHDLQILEGTDTLLRCEVSNRAGKVQWTKDGFALGFSAVIPGFPRYSVLVDAKQNAYNLQIKNATLEDDAEYQCQVGPAAGNPAIRANAKLSIVAAPSSIVIEGYARNARVEVEERQNLTLHCIAENANPAAEIVWFQGEVPVSTAPIVTVNQTAPKRFTTSSTLHLQPRAEDDYKEFSCEARHKALPPDVPMRAQVQLSVLYPPGAPFFEGYSQGETLHRGQEVQIACRSRGGNPPAQLTWYRNGVAISSPQRTSGRLSENVYKFTAAAEDNGANLVCEAKNLLATTPLRAELNLTVLYAPKDVYLSGANQAKVGDSVQLSCVTAPSNPQARISWSINGRPLDNSTYKTTSSSDGGWVSSSNISLTIDSQSRTFIAVCHALNTELTQNVVGSHTVNVLYPPSPPLLTGYNDGDILISGSILKLQCSSAGGNPPPTLQWYKNDKIINAPSKLVDSKITSELSLLVNASDNNAIYKCKVQNAAIDIPLFATKTLGVHFPPETVKISVVPKNLVPGIRAKLICDSSSSNPPAKISWWKDGIPVEGLNLANRPGLWGGSVSTLEMYVNITQDLDGIVYTCQSHNEVLQRSVHETISLDILYPPKFETPQSTTFVGVEGAPFHVELLASGNPMVITYTWTKDGLPISSNSLSGQRLISDGPRLNISRLSRNDAGVYICEALNSQGTALLEIQVAVEYAPTITAVSEGRSFVAGEPAVLACHIRARPLEAAHVRWSRDGYDLATRTISSFENGTALLQIASVERSDIGNFTCIVDNQRGAPAAQNVLLVVQTAPEIDHSPGFTRYAARLGVRAQLICRSLASPQPSFIWRRHGKDLKMQRRNKFKSVERQVDALNFESALLIENTSPDDYGQYECVVRNSLGQASTTLEFSKPSRPDAPLQLRVGNVSDTGVDLNWTPGFDGGMQTYFRLRLKQHGEDKYKYVDAKPGHQNISLDGLKPGATYYFSVMAANEAGGSKFMPDIKLTLSKGSQPHSAEYTEKDELPNVMIIGITSAAMVLLVLNAALVAWFVIRRQNKSQSEAEPSNDDVYSKDDSQSVYKLPITALQADVQKKAAASTYLVENVDIIQSTAYPPKYQESSMCTPPYPLCNPDFTRTLPNPKRHSQRNSATGMIEGMQMRSKDDHMLISNGLYIPSPSPASSLVIKGSYISSPSPAPPADGSYFNMSDKYMSYPPVTY
Protein: Uncharacterized protein (Q57Y08)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDNTEETSRVTDQEERTLTETELPAPAEHVLEGDNSASEENRLHAFLIPLEDGEQFARANLQHRWYRGLTKMLWDEELERNGILIVERGESGRNNQSADEEEEEDDDGTDDCVAKMKREFRIKREQDKIVYEEDSTRTETLREEQNAISLIVTLMEEAMDRSILMNEAETMFALILDVLKPRVHYRYIYAWGVVTCCSFKPLKSEMDRLRPSDRHKPPYMRKSLPTCRVPLEPIYYLPDGGKKMRAMNELNDVRAIGWV
Protein: Hepatic triacylglycerol lipase (HL) (Hepatic lipase) (EC 3.1.1.3) (Lipase member C) (Lysophospholipase) (EC 3.1.1.5) (Phospholipase A1) (EC 3.1.1.32) (P27656)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles (By similarity). Also exhibits lysophospholipase activity (By similarity). Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates (By similarity). In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P11150}.
Interaction partners:
- Apolipoprotein B-100
- Lipoprotein lipase
- Patatin-like phospholipase domain-containing protein 2
- Diacylglycerol O-acyltransferase 2
- Diacylglycerol O-acyltransferase 1
- 1-acylglycerol-3-phosphate O-acyltransferase Pnpla3
- Gastric triacylglycerol lipase
- Bile salt-activated lipase
- Apolipoprotein A-I
- 2-acylglycerol O-acyltransferase 1
Sequence:
MGNPLQISIFLVFCIFIQSSACGQGVGTEPFGRSLGATEASKPLKKPETRFLLFQDENDRLGCRLRPQHPETLQECGFNSSQPLIMIIHGWSVDGLLENWIWKIVSALKSRQSQPVNVGLVDWISLAYQHYTIAVQNTRIVGQDVAALLLWLEESAKFSRSKVHLIGYSLGAHVSGFAGSSMDGKNKIGRITGLDPAGPMFEGTSPNERLSPDDANFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSFQPGCHFLELYKHIAEHGLNAITQTIKCAHERSVHLFIDSLQHSDLQSIGFQCSDMGSFSQGLCLSCKKGRCNTLGYDIRKDRSGKSKRLFLITRAQSPFKVYHYQFKIQFINQIEKPVEPTFTMSLLGTKEEIKRIPITLGEGITSNKTYSFLITLDKDIGELILLKFKWENSAVWANVWNTVQTIMLWGIEPHHSGLILKTIWVKAGETQQRMTFCPENLDDLQLHPSQEKVFVNCEVKSKRLTESKEQMSQETHAKK
Protein: Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.8.5) (2-methyl branched chain acyl-CoA dehydrogenase) (2-methylbutyryl-coenzyme A dehydrogenase) (Q9VVU1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable enoyl-CoA hydratase, mitochondrial
- acetyl-CoA C-acyltransferase
- HL08109p)
- Trifunctional enzyme subunit alpha, mitochondrial
- Acetyl-CoA acetyltransferase 1, isoform A)
- Acetyl-CoA acetyltransferase 2
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- glutaryl-CoA dehydrogenase
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MMNSLKKLPVRMLANAARQQSAAMSSATGLPPPLTFLTDDEKMMKETVAKLAQEQIQPLVKKMDFEHKFDPSVVKAVFENGLMGIEIDTELGGSGCNFMTNIVVVEELSKIDPAVAAFVDIHNTLVNSLMIKFGNAEQKAKYLPKLAQEYAGSFALTEPGAGSDAFSLKTVAKKDGSHYVINGSKMWISNSDVAGVFLIFANAKPEDGYRGITTFIVDRETPGLIVNKPEDKLGIRASGTCQLTFDNVRVPEENILGTFGHGYKYAAGFLNEGRIGIAAQMVGLAQGTFDATIPYLLERKQFGDAIYNFQSMQHQIATVATEIEAARLMTYNAARLQEQGVPFQKEAAMAKYYASEVAQRAAIKCVDWMGGVGFTRDFPQEKYYRDVKIGAIYEGTTNMQLSTIAKCIKKDYAA
Protein: Protein-lysine 6-oxidase (EC 1.4.3.13) (Lysyl oxidase) [Cleaved into: Protein-lysine 6-oxidase, long form; Protein-lysine 6-oxidase, short form] (P16636)
Organism: Rattus norvegicus (Rat)
Function: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P28301}. Secreted, extracellular space.
Interaction partners:
- Fibulin-5
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Metalloendopeptidase
- Collagen alpha-1
- Collagen alpha-1
- Prostaglandin G/H synthase 2
- Fibrillin-1
- Elastin
- Snail homolog 1
- C-C motif chemokine 2
Sequence:
MRFAWTVLFLGQLQFCPLLRCAPQAPREPPAAPGAWRQTIQWENNGQVFSLLSLGAQYQPQRRRDSSATAPRADGNAAAQPRTPILLLRDNRTASARARTPSPSGVAAGRPRPAARHWFQVGFSPSGAGDGASRRAANRTASPQPPQLSNLRPPSHVDRMVGDDPYNPYKYSDDNPYYNYYDTYERPRSGSRHRPGYGTGYFQYGLPDLVPDPYYIQASTYVQKMSMYNLRCAAEENCLASSAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDASTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYAADIDCQWIDITDVQPGNYILKVSVNPSYLVPESDYSNNVVRCEIRYTGHHAYASGCTISPY
Protein: Subtilisin propeptide-like protein (PfSUB1-ProM) (C0H4D0)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Acts as a specific inhibitor of subtilisin-like protease SUB1.
Subcellular location: Secreted {ECO:0000305|PubMed:31942933}. Parasitophorous vacuole lumen {ECO:0000305|PubMed:31942933}. Cell membrane {ECO:0000305|PubMed:31942933}; Peripheral membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
Interaction partners:
Sequence:
MKFLFAFNFFSLYIYLYEFLCIHLCGSQVTPAGTVLNSNSALISRRINRRKMKNCNNNDLLKVLKMETTYNELPAHNLLMSSKNDINKLFDYINKNEELSKLMNSCGTYVYLKYLGVVIFSIKENVQISHLSEFIQYLLNKNVCIEFNQNVML
Protein: Small ribosomal subunit protein eS28z/eS28y (40S ribosomal protein S28-1) (Q9SR73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein eS26x
- Small ribosomal subunit protein uS2z
- Small ribosomal subunit protein eS6z
- U3 small nucleolar ribonucleoprotein protein IMP3
- Large ribosomal subunit protein eL38z/eL38y
- Small ribosomal subunit protein eS21z
- Small ribosomal subunit protein uS17z
- Small ribosomal subunit protein eS10z
Sequence:
MDSQIKHAVVVKVMGRTGSRGQVTQVRVKFTDSDRYIMRNVKGPVREGDILTLLESEREARRLR
Protein: Scribble planar cell polarity protein (A0A8I6APB3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLKCIPLWRCNRHVESVDKRHCSLQVVPEEIYRYSRSLEELLLDANQLRELPKPFFRLLNLRKLGLSDNEIQRLPPEVANFMQLVELDVSRNDIPEIPESIKFCKALEIADFSGNPLSRLPDGFTQLRSLAHLALNDVSLQALPGDVGNLANLVTLELRENLLKSLPASLSFLVKLEQLDLGGNDLEVLPDTLGALPNLRELWLDRNQLSALPPELGNLRRLVCLDVSENRLEELPVELGGLALLTDLLLSQNLLQRLPEGIGQLKQLSILKVDQNRLCEVTEAIGDCENLSELILTENLLTALPRSLGKLTKLTNLNVDRNHLEVLPPEIGGCVALSVLSLRDNRLAVLPPELAHTAELHVLDVAGNRLRSLPFALTHLNLKALWLAENQAQPMLRFQTEDDAQTGEKVLTCYLLPQQPLPSLEDPGQQSSPSESCSDAPLSRVSVIQFEDPLEGEEDAEEAAAEKRGLQRRATPHPSELKVMKRGIEERRNEAFVCKPDPSPPSPSEEERRLSAESALSGNSVPSASTASDGEPETLPAEVQGLGQQEAMPGQEEYPEEDYNEPTVHFAEDTLIPREDGEGEEGQPEAPWPLPSGRQRLIRKDTPHYKKHFKISKLPQPEAVVALLQGVQTDREGPTAGWHNGPHTPWAPRAHEEEEEEENRDEEEGEASMEEDDKEEAVASAPSVKGVSFDQANNLLIEPARIEEEELTLTIVRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAAHAGVRVGDKLLEVNGVALQDAEHHEAVEALRGAGAAVQMRVWRERMVEPENAVTITPLRPEDDYSPREWRGGGLRLPLLQPETPVPLRQRHAACLVRSEKGLGFSIAGGKGSTPYRAGDAGIFISRIAEGGAAHRAGTLQVGDRVLSINGVDMTEARHDHAVSLLTAASTTISLLLERETGGAYPPSPPPHSSSTPTATVAATMTTAIPGEPLLPRLSPSLLATALEGPYPVEEICLPRAGGPLGLSIVGGSDHSSHPFGVQDPGVFISKVLPRGLAARCGLRVGDRILAVNGQDVREATHQEAVSALLRPCLELCLLVRRDPPPPGMRELCIQKAPGEKLGISIRGGAKGHAGNPCDPTDEGIFISKVSPTGAAGRDGRLRVGLRLLEVNQQSLLGLTHAEAVQLLRSVGDTLTVLVCDGFDTSTTTALEVSPGVIANPFAAGLGHRNSLESISSIDRELSPEGPGKEKELASQTLPWEPESAETTGRNQEPLKLDYRVLAAVPSAGSLQRGPCATTGGKMTEAPSSPGSQQPPSPDELPANVKQAYRAFAAVPTVHPPENSATQPPTPGPAASPEQLSFRERQKYFELEVRVPQAEGPPKRVSLVGADDLRKMQEEEARKLQQKRAQMLREEAVTSGPDTGLASDRESLDDEQEAEQPWAGPSHAGGLSPSSPTPLGGSAPVRTAKAERRHQERLRMQSPELPAPERALSPAERRALEAEKRALWRAARMKSLEQDALRAQMVLSKSQEGRGKRGPLERLAEAPSPAPTPSPTPLEDFGLQTSTSPGRLSPDFVEELRTLDPSPSPGPQEEDGEVALVLLGRPSPGTVGPEDMTLCSSRRAMRPGRRGLGPVPS
Protein: E3 ubiquitin-protein ligase MIEL1 (EC 2.3.2.27) (MYB30-interacting E3 ligase 1) (Pirh2-like protein 1) (AtPILP1) (RING-type E3 ubiquitin transferase MIEL1) (Q8VZK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that acts as a regulator of cell death and defense. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Attenuates the activation of defense and related cell death responses in the absence of pathogens by mediating ubiquitination and subsequent proteasomal degradation of MYB30.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23403577}. Nucleus {ECO:0000269|PubMed:23403577}.
Interaction partners:
- Transcription factor MYB30
- Phosphatidylinositol 4-kinase gamma 2
- Transcription factor MYB96
- E3 ubiquitin-protein ligase RHA2B
- E3 ubiquitin-protein ligase RING1-like
Sequence:
MEASPNDRLHFGKMGFGCKHYKRRCQIRAPCCNEVFDCRHCHNESTSTLRNIYDRHDLVRQDVKQVICSVCDTEQPAAQVCSNCGVNMGEYFCSICIFYDDDTEKQQFHCDDCGICRVGGRENFFHCKKCGSCYAVGLRNNHRCVENSMRHHCPICYEYLFDSLKDTNVMKCGHTMHVECYNEMIKRDKFCCPICSRSVIDMSKTWQRLDEEIEATAMPSDYRDKKVWILCNDCNDTTEVHFHIIGQKCGHCRSYNTRAIAPPVLPQ
Protein: Large ribosomal subunit protein bL12 (50S ribosomal protein L7/L12) (BL9) (Vegetative protein 341) (VEG341) (P02394)
Organism: Bacillus subtilis (strain 168)
Function: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Interaction partners:
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS10
Sequence:
MALNIEEIIASVKEATVLELNDLVKAIEEEFGVTAAAPVAVAGGAAAGGAAEEQSEFDLILAGAGSQKIKVIKVVREITGLGLKEAKELVDNTPKPLKEGIAKEEAEELKAKLEEVGASVEVK
Protein: Arginine/serine-rich coiled-coil protein 2 (Q7L4I2)
Organism: Homo sapiens (Human)
Interaction partners:
- RNA-binding protein 25
- AT-rich interactive domain-containing protein 4B
Sequence:
MAASDTERDGLAPEKTSPDRDKKKEQSEVSVSPRASKHHYSRSRSRSRERKRKSDNEGRKHRSRSRSKEGRRHESKDKSSKKHKSEEHNDKEHSSDKGRERLNSSENGEDRHKRKERKSSRGRSHSRSRSRERRHRSRSRERKKSRSRSRERKKSRSRSRERKKSRSRSRERKRRIRSRSRSRSRHRHRTRSRSRTRSRSRDRKKRIEKPRRFSRSLSRTPSPPPFRGRNTAMDAQEALARRLERAKKLQEQREKEMVEKQKQQEIAAAAATGGSVLNVAALLASGTQVTPQIAMAAQMAALQAKALAETGIAVPSYYNPAAVNPMKFAEQEKKRKMLWQGKKEGDKSQSAEIWEKLNFGNKDQNVKFRKLMGIKSEDEAGCSSVDEESYKTLKQQEEVFRNLDAQYEMARSQTHTQRGMGLGFTSSMRGMDAV
Protein: Putative methyltransferase Rv1407 (EC 2.1.1.-) (P9WGX3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May act as RNA methyltransferase.
Interaction partners:
- Methionyl-tRNA formyltransferase
- dTDP-4-amino-4,6-dideoxyglucose formyltransferase
- Phenylalanine--tRNA ligase beta subunit
- Riboflavin biosynthesis protein RibD
- Uncharacterized protein Rv1405c
- Small ribosomal subunit protein uS10
- Serine/threonine protein phosphatase PstP
- tRNA pseudouridine synthase B
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL13
Sequence:
MTPRSRGPRRRPLDPARRAAFETLRAVSARDAYANLVLPALLAQRGIGGRDAAFATELTYGTCRARGLLDAVIGAAAERSPQAIDPVLLDLLRLGTYQLLRTRVDAHAAVSTTVEQAGIEFDSARAGFVNGVLRTIAGRDERSWVGELAPDAQNDPIGHAAFVHAHPRWIAQAFADALGAAVGELEAVLASDDERPAVHLAARPGVLTAGELARAVRGTVGRYSPFAVYLPRGDPGRLAPVRDGQALVQDEGSQLVARALTLAPVDGDTGRWLDLCAGPGGKTALLAGLGLQCAARVTAVEPSPHRADLVAQNTRGLPVELLRVDGRHTDLDPGFDRVLVDAPCTGLGALRRRPEARWRRQPADVAALAKLQRELLSAAIALTRPGGVVLYATCSPHLAETVGAVADALRRHPVHALDTRPLFEPVIAGLGEGPHVQLWPHRHGTDAMFAAALRRLT
Protein: Galanin receptor type 2 (GAL2-R) (GALR-2) (O88854)
Organism: Mus musculus (Mouse)
Function: Receptor for the hormone galanin, GALP and spexin-1. The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Galanin peptides
- Spexin
- Galanin receptor type 1
- Galanin receptor type 3
- Galanin-like peptide
- Somatostatin receptor type 1
Sequence:
MNGSDSQGAEDSSQEGGGGWQPEAVLVPLFFALIFLVGAVGNALVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDDWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLALLFSGPYLSYYSQSQLANLTVCHPAWSAPRRRAMDLCTFVFSYLLPVLVLSLTYARTLHYLWRTVDPVAAGSGSQRAKRKVTRMIVIVAVLFCLCWMPHHALILCVWFGRFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRKICAGLLRRAPRRASGRVCILAPGNHSGGMLEPESTDLTQVSEAAGPLVPAPALPNCTTLSRTLDPAC
Protein: Phosphoacetylglucosamine mutase (PAGM) (EC 5.4.2.3) (Acetylglucosamine phosphomutase) (N-acetylglucosamine-phosphate mutase) (Q9VTZ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- UDP-N-acetylglucosamine diphosphorylase
- Probable glucosamine 6-phosphate N-acetyltransferase
- N-acetyl-D-glucosamine kinase
- N-acetylglucosamine-6-phosphate deacetylase
- glutamine--fructose-6-phosphate transaminase
- chitin synthase
- Glucose-6-phosphate isomerase
- Phosphoglucomutase 1
- Trehalase
- Trehalase
Sequence:
MSINLRTVYAFAREMYPKTSKETIQYGTAGFRGKAEFLDSVMFRMGVLATLRSRYRGGSVIGVMITASHNPEPDNGVKLVDPKGEMLEASWEAIATDLVNVSDQELEQQVAKIIKDNNIDVTTSSQVFVGMDNRYHSPRLLKAVADGVIALKGNVKEYGIVTTPMLHYFVVAANTKEAYGKPTEEGYYDKLIKAFELLRNGRLENGNYRNSIIYDGANGVGARKMLQFIKRMKGTLNVTVINQGIGVGKINEDCGADYVKVQQSPPKSMPEDVKPYTRCVSVDGDADRVVYFFTDDKGEFHLLDGDRIATLIAGYLMELVTQSEISLRLGLVQTAYANGASTDYIVDQLKFPVSCVPTGVKHLHHKALEYDIGVYFEANGHGTIVFSDNAKATIAQVAQTKESAKTLLLLIDLINETVGDAISDMLLVETILNHKGWDVQDWISSYNDLPNRQLKVKVQDRNVIETTDAERVCVKPEGLQTEINQVVAKYKRGRSFVRPSGTEDVVRVYAEAATKEDTDNLAYEVGLLVQKLAGGVGPPLTKPNSSAHL
Protein: Homeobox protein ceh-36 (Q93352)
Organism: Caenorhabditis elegans
Function: Probable transcription factor, acting as a progenitor identity factor regulating the development of lineally-related embryonic cells including glial, excretory and neuronal cells. Mediates chemosensory function of ASE and AWC neurons. In ASE neurons, required to diversify the fate of the ASEL neurons from the ASER neurons. Acts cell-autonomously to establish a neuronal left right asymmetry, possibly promoting asymmetric expression of the helix-loop-helix proteins ngn-1 and hlh-2. In cooperation with the transcription factor sox-2, required for the differentiation of AWC olfactory neurons. May regulate the expression of sox-2 in AWC olfactory neurons.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeobox protein mls-2
- Transcription factor che-1
- Nuclear hormone receptor family member odr-7
- Receptor-type guanylate cyclase gcy-5
- Serpentine receptor class r-10
- LIM/homeobox protein lim-4
- Receptor-type guanylate cyclase gcy-10
- Cyclic nucleotide-binding domain-containing protein
- Homeobox domain-containing protein
Sequence:
MTTNFYTAFPTLGYTAYPQFAFAAATTAPSLTSATTSSTTMAPMAPNSESGRRAGRRERTSFNRGQLDQLEKVFRETQYPDVHRREALAKAINLPDGRVQVITVWFKNRRAKDRNNKKMDGVHPGSTSSRSSNGSPHNESKPDTKSLGIHIPGTPEFNAHSAAKYEANSAVLSQLQQQQQQQLQQPKSELEDSKPLADTKYDSTQSLLPQAQAAAYASYATTAPYPYNYNSYFPSNFYYQQYGSNDYTPNITAYSPL
Protein: LP05062p (Q960I7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTSSANHNAAGYGAPTPSGSYVENTIIIQYDPYVQEVWDQARKLRCTWYDFYEKAVTFRPFQVDMLHAVTANFLGDNLQCWMQIQVGKGPWASEVSGIVKIGQTMTMVLAIKDDENKFDMLVRNCVAHDGKRAPIQLVDQNGCVVRPKIMSKFQKIKNFGPSASVVSFAYFQAFKFPDSMNVHFQCVIQVCRYNCPEPKCGPGLPGGEYGLPQIGANGLSEEYGPPEAYERNDFALGGPGVLPPAAYPDPRHPASDATGAYSENQPDVVPSPQAQTSAAVPTADSGTVSGPASSQSPQPQPTGSNELGLPPPPLPGQSGQYSTVKRKDDLSAGGNLVSLGGRPRSVEGLDDLRGVRRRRDTMDIVVKPQRIYKRNAQEMTDVNTSRIIQVVAPGDVNFALNSNASNETVVIQSARSADAETICMSVPSFVGGLVMLLLVLAVASLVAAFLFVRVRHFDRKGAGMAYVN
Protein: GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (GMP synthetase) (Glutamine amidotransferase) (Q4V7C6)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of xanthine monophosphate (XMP) to GMP in the presence of glutamine and ATP through an adenyl-XMP intermediate.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:3436958}.
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase 2
- Inosine-5'-monophosphate dehydrogenase 1
- Adenine phosphoribosyltransferase
- GMP reductase
- GMP reductase 1
- Guanylate kinase
- Ubiquitin carboxyl-terminal hydrolase 7
- Inosine triphosphate pyrophosphatase
- Trifunctional purine biosynthetic protein adenosine-3
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MALCNGDSKPENAGGDLKDGCHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISMDNTCSLFRGLQKEEIVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGVQFHPEVGLTENGKVILKNFLYDIAGCSGNFTVQNRELECIREIKEKVGTSKVLVLLSGGVDSTVCTALLNRALNQDQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMSLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVRILGRELDLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMEITSQHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLIPRMCHNINRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILRESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGVPATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Protein: Mitochondrial ribosomal protein S18 (Q38AS2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Pentacotripeptide-repeat region of PRORP domain-containing protein
- Uncharacterized protein
- Ribosomal protein S9
- LysM domain-containing protein
- Opioid growth factor receptor
- Uncharacterized protein
- Uncharacterized protein
- Enoyl-CoA hydratase/isomerase domain-containing protein
- Small ribosomal subunit protein mS41
Sequence:
MNRTGGSVYAHALSQFAVCRQPWNEYIGLLTKQDSTPYHTEPQEKPAYRGRKQGREGWLFGQQVQLHYHRFPDEQLITNLSRWRTGETVGDIAMQQFRNAQPFDIEDKDPQGVQRPSPEVYMKLNYKNPATISRFLTRTGHMYPADILPLNPEAVVKLRVAKAQAIRIGLYPRFGNPFWFRSQKFRPKAYQENYDPTTYSTKRTVEHFAYNWVQTDRIRRYFRELEAVHTSGSASARGSGGGTTAEHKQQDQFYSPENQPISLHRNNISYMEDVGRSVKNPTVPGLMSTKGMKKKFHNLYSSTSTKRMGFSNPTLGIKKV
Protein: Sca1 complex protein phr (Pleckstrin homology domain-containing protein) (Q1ZXQ0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the Sca1 complex, a regulator of cell motility, chemotaxis and signal relay. The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells where it regulates F-actin dynamics and signal relay by controlling the activation of rasC and the downstream target of rapamycin complex 2 (TORC2)-Akt/protein kinase B (PKB) pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20493808}. Note=The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells (PubMed:20493808). Membrane localization of the Sca1 complex is regulated by scaA phosphorylation by PKB and PKB-related PKBR1 (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Ras guanine nucleotide exchange factor H
- Ras guanine nucleotide exchange factor A
- Protein phosphatase 2A catalytic subunit B
- Protein phosphatase 2A scaffold subunit
- Dipeptidyl aminopeptidase
- Sca1 complex scaffold protein scaA
- Large ribosomal subunit protein uL10
Sequence:
MLLLNYTQNFQLITFLLFPFINTFDYNCLKPTTTTTTSPTSSKLGFLNRSKSNSNININELKNKFLEQQQEGSISNIAGVATTQQNPSIVINSSSSSSSSSSHHPHHQKTPSNSSSNFNLIKASFNQIGVAFNNNISPRSNRKEKEKDKDKDHQDNSNINNINNINNNINNNINNNNNNNNNNNNNNNMHNPTSSSPSINNNLKGKNVASIIAANGANLNNSLSNLHQHVNNNSNNNLTNSFNSVSHNNISISSGGSALSYNYTQQLNQNGGSNNGSTSNSTSNSANNSLLSLASSINGNIGSDENGSNVMYGGDIASSYHSMSIDPLKSSTNTETIEIMVVGDELSNKARFISSFLNNGIGEDPTLEISTKKSIAIQSGAYNVNINTTVGQEEFWGINDVYYRSSQGFIFVYNVNSRESFLSFLKFRDKIIHEKGTENILMAMVGLTSPLINQESGEESCIREVTQQEAKRMADLYSCSFVELNSFGLDCEHQIQSIVTDLLGRITSGLSSTNNNNSGNNSNNNNGNSNGNSSNNNSNNNSTNNLNNSAILNESIAQSIEVLMLGDIFVGKTQIIQRLLGNPFQNAYKETTEWNRNVYQMTVNDVRYLLKIVDTCGLDIEETLNRERLVSTQGFIFVYSIASRESFLMIEQLRKKLSSIKSETKIPSVLIANKGDSLIRQVTFDEGSKMAQHLGSHYFEVSSMFSDDESIGRPFEQLLIDIQKSGNASGFEPSEIKKKGYLFKEGKKLKSMSKYFFKASRGNLSYCKNESNKSKVKSIQLSEQIQLAIPHNVHEKKDVWPFSIILDPVSKHSINLIASTEEERNAWIKAIKFNCFLEDITSNIIDDVVKSMVSEIASGVAGSGSNNGNNNGHLKRSDTTQQLNNSGSFINGINANKPVPNFSNLSISGGGSSNNSNNSTPMSSPYGSSNNFSSHLSQSTSSMSMSPQQQLQSVLLSSSNLSSSMNSSFSYSSSISSSYTDSMSGSPPDSNGQVFPQSPQLKKTLFQRTTSFSKGSKLK
Protein: Upstream transcription factor 2, c-fos interacting (M0QY46)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XPGLDPAASATAAAAASHDKGPEAEEGVELQEGGDGPGAEEQTAVAITSVQQAAFGDHNIQYQFRTETNGGQVTYRVVQVTDGQLDGQGDTAGAVSVVSTAAFAGGQQAVTQVGVDGAAQRPGPAAASVPPGPAAPFPLVGALPPLGGGGREWRGDTGSALGEPRGWGRC