wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized methyltransferase At2g41040, chloroplastic (EC 2.1.1.-) (Q0WPT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}.
Interaction partners:
Sequence:
MAMAALTSSSSAITLLNKPFLPNRSSFFSSDSQSPLLRFSASTSVRSRFPSAAISAVAPKSDINKNETPKIEIEETQVFACPVCYEPLMRKGPSGINLQAIYRSGFKCGQCNKTYSSKDEYLDLTVTADLDDYNEVKPITTELFRSPLVSFLYERGWRQAFKRSGFPGPDEEFRMAEEYFKEAEGGLLVDVSCGSGLFSRKFAQSGKYSGVIALDYSENMLRQCKEFIKNDNTFDNSTNIAVVRADVSRLPFPSGSVDAVHAGAALHCWPSPTNAIAEICRVLRSGGVFVGTTFLRYSPSTPWIIRPFQSRILQSYNYLMQDEIKDVCTSCGLTDYEDYIQDSFIMFTARKP
Protein: Adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 1 (D3ZWA8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Cytoplasmic vesicle, phagosome {ECO:0000256|ARBA:ARBA00004262}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004220}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Adiponectin receptor 1
- Adiponectin receptor 2
- DCC-interacting protein 13-beta
- RAC-alpha serine/threonine-protein kinase
- PDZ domain-containing protein GIPC1
- Caspase-3
- Netrin receptor DCC
- RAC-beta serine/threonine-protein kinase
- Inositol polyphosphate 5-phosphatase OCRL
- RAC-gamma serine/threonine-protein kinase
Sequence:
MPGIDKLPIEETLEDSPQTRSLLGVFEEDATAISNYMNQLYQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPISQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNGQLEEFLANIGTSVQNVRREMDGDVETMQQTIEDLEVASDPLYLPDPDPTKFPVNRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISKQIYLSENPEETAARVNQSALEAVTPSPSFQQRHESLRPGGQSRPPTARTSSSGSLGSESTNLAALSLDSLVAPDTPIQFDIISPVCEDQPGQAKAFGQGGRRTNPFGESGGSTKSETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPYVVLYATHQENKRLFGFVLRTSGGRSESNLSSVCYIFESNNEGEKICDSVGLAKQIALHAELDRRASEKQKEIERVKEKQQKELSKQKEIEKDLEEQSRLIAASSRPSQSGSEGQLVLSSSQSEESDLGEEGKKRESEA
Protein: Trafficking protein particle complex II-specific subunit 120 homolog (AtTRS120) (TRAPP II-specific subunit 120 homolog) (Protein VASCULAR NETWORK DEFECTIVE 4) (Q9FY61)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specific subunit of the TRAPP II complex, a highly conserved vesicle tethering complex that is required for the proper transport of proteins in post-Golgi trafficking pathways to the growing cell plate in mitotic active cells. Required for the polarized and selective transport of PIN2 and probably PIN1 to the plasma membrane. Not required for ER-to-Golgi as well as biosynthetic and endocytic vacuolar transport.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:24443495}. Early endosome {ECO:0000269|PubMed:24443495}.
Interaction partners:
- Trafficking protein particle complex subunit
- Trafficking protein particle complex II-specific subunit 130 homolog
- SNARE-like superfamily protein
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit
- Transport protein particle
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit-like protein
- Tetratricopeptide repeat
Sequence:
MEPDVSIETLSIIRIAVLPIGTIPPTLLRDYHSMLLRHHTIALSAISSFYTEHQKSPFTNQPWDSGSLRFKFVLGGSPPSPWEDFQSNRKMLAVIGLCHCPSSPDLDSVTEKFNVACKSYSSALVRRCFAFSPGDSQLEDGDKKGENLILFPPSDKQTQEFHLQTMMQDIAASLLMEFEKWVLQAESAGTILKTPLDSQASLNSEEVIKAKKRRLGRAQKTIGDYSLLAGSPVDANAHYSTALELARLTGDYFWYAGALEGSVCALLVDRMGQRDVALEDEVRYRYTNVILHYRKSFIQEIAQRVSPLSFELEATLKLARFLCRRELAKEVVELLTNAADGAKSLIDASDRLILYVEVARLFGALGYQRKAAFFCRQVAQLYLQQDNRLAAISAMQVLSMTTDAYRIQSRASMSKVSVNNETGRLPDAGKMHHHSIVSLFESHWSTLQMVVLREILLSAVRAGDPLAAWSAAARLLRWHYPLITPSGQNGLANSLANSADRLPSGTRCADPALPFVRLFSFPLHSSQVDIVKRNPAREDWWTGSAPSGPFIYTPFSKGDANESSKQELIWVVGEPVQVLVELANPCCFDLRIDSIYLSAHSSNFDAFPVSVDIPPNSAKVITLSGIPTAVGPVTIPGCTVHCFGVITEHVFRDVDNLLLGAAQGLVFSDPFRSCGSAKLRHVFVPNISVAPPLPLLVANVVGGDGAIILYEGEIREVCINFANAGTVPIVQAHVSLSGKNQDAVISIADEALQSALPLKPGAQVTLPVTLKAWHVGPTDSDNTMSSGRNAAGNTGRPKDGTSPSLLIHYAGPLSNNGDSQEKESIVPPGRRLVVPLQICVLQGLSFVKARLLSMEIPAHVSDNLRDEDIERESNADSLVKINPFRGSWGLRFLELELSNPTDVVFEISVFVQLENSAKEDDSSPVQDSPEYEYPKTRIDRDYSARVLIPLEHFKLPVLDGSFFTKDPPPGSPSSSRNPSFSEKNTKAEINTLIKNLISKIKVRWQSGRNSSGELDIKDAIQTALQTTVMDVLLPDPLTFGFRLVRNGLEKDPETKAESPFSKGSVLSHEVTPMEVLVRNNTSEAIKLNLSVTCRDVAGQNCTEGADATVLWAGALSGISMEVAPLQEARHCFSLFFLVPGEYTMVAAAVIEDANNVLRARAGTASPNEPIFCRGPPFHVCVAGGAL
Protein: Methyltransferase (Q385R2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Small ribosomal subunit protein mS29
- 30S Ribosomal protein S17, putative
- PROP1-like PPR domain-containing protein
- Uncharacterized protein
- tRNA pseudouridine synthase A-like protein
- Rhodanese domain-containing protein
- Uncharacterized protein
- Dehydrogenase-like protein
- Kinteoplast poly
- Small ribosomal subunit protein uS5 C-terminal domain-containing protein
Sequence:
MFFRFHSTTLQTCLTSGVARSSVAVAVPLRAGCTRREMSSGGDGVLEGAMHKPGESGLQAGSSTTIAGKETWSQFSTKMRYGRRRIRVIDVAAKMSYEYQMLRKMCKRRPAMRQWAVRDDFCDMNPGVVIMSPSMQAAFMKVFRMKEKGLIRQCLRDIVPVIEYRNREEPARLPTNPADMIPEGEPDTLNQKKRELFERREKGENFADLRLHDKRSQAKLRFRIRQRLLKFQRQLAVANAIASRSVLYSTNDAIGYFLFRGAAMYAGMHRVFFELSKQLPHFVPKTMLDFGAGTGTAILVAKEVYDPGSLAYPLYRSLRQTMQGNDSSRTHQLSELRYDLKRLQRNNEEKKKVRFMAVAALLERGEVDPADLPEDLKREIAEVATAAATAKKDRLVREAHARYRDVVDGTEWESGDPLGEVRASTEDPEDVIDGEQGDGGDDGEAAKGRPKTWWEKLIDVENETARTRAARRLRPLQEVTAVEPSPGMMEIGTMVLHDDVPNVTWKRYLLPEDEAIQHDLVVAAYSLSEIATSENRRRIVQQLWKMTKGVLVFVEFANLNNFNILMEARDWILEEKDVGLWDWQPTIVAPCPHEHRCPLRHCKTGVKRKRMRICSTEAHYRSTFVEVWARHMPLKVGIEPISYLILARNELVPERAERRREQLKKAEEMKRRERDVKQQQLHEASLAVKDVVFERLSDEALHRVQSGVPQPLTDIDEVREASTSATSTSLLKDLKDGATSTGEIGHMPTDVPRLVKTGNTRHNRLIFPLQFPPATHKFNRAFVDAGYQRQRAITPAEMLVVRQEVEQLQQRVMRAAPKYLRVVRDPRCHGKVQADFCTPEGDLVSGRVYRRFYGDRNRVSAHSTMRWQHIGGWKLLKRIRRGSLFPHNVPLYAVTKHAQIDFPNTLLDTKHSTVEQTAMQYNDPMSLVEMPDDGLTREELKQKRRLQRDVELQKKVEEKLEDIFGVNAKDWKMDDLGGGRLDARREISEQQWADAVRRAKIRTVQHTKNALPFAAKKRAAQRALQVRRRNVRLEMSGNRRR
Protein: Lipid A biosynthesis acyltransferase (EC 2.3.1.241) (Kdo(2)-lipid IV(A) acyltransferase) (Q9HYZ8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01942}; Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01942}.
Interaction partners:
- 3-deoxy-D-manno-octulosonic acid transferase
- UDP-3-O-acylglucosamine N-acyltransferase
- Lipid-A-disaccharide synthase
- Tetraacyldisaccharide 4'-kinase
- UDP-3-O-acyl-N-acetylglucosamine deacetylase
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
- Probable 2-OH-lauroyltransferase
- UDP-2,3-diacylglucosamine hydrolase
- Arabinose 5-phosphate isomerase KdsD
- Lipopolysaccharide heptosyltransferase 1
Sequence:
MDRPRFSSAFLHPRYWPLWFGLGLLWLVVQLPYPVLLMLGRGLGALMYRLVGSRREIAARNLELCFPEKSPAERERLLKENFASSGIAFFEMAMSWWWPKARLARLAHIEGLEHLREAQAQGEGVILMALHFTTLEIGAALLGQVHTIDGMYREHDNPVFDYVQRRGRERHNLDATAIEREDVRSMLKVLRGGRAIWYAPDQDYGAKQSLFVPLFGIPAATVTATTKFARLGRARVLPFTQSRLADGSGYRLTIHPPLEDFPGESEEADCLRINQWVERCVRQQPEQYLWAHRRFKTRPPGEAKLYPKRRKR
Protein: Protein verrocchio (Q9VTZ2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:27835648}. Chromosome {ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:27835648}. Chromosome, telomere {ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:27835648}. Note=Localizes to euchromatic telomeres of polytene chromosomes (PubMed:26110638). Telomere localization is not dependent on peo/pendolino (PubMed:26110638). Telomere localization is dependent on cav/HOAP, tea and moi/modigliani (PubMed:27835648). {ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:27835648}.
Interaction partners:
- Protein modigliani
- Protein telomere ends associated
- Telomere-binding protein cav
Sequence:
MDFNQSFEDIESQLDNFVIRKNQQSEKSTGKCGPEVHDNVPLTISQIERATQDPENENVFITDDVHPIHFCTCIIYAFVTGNGTHNESFMKFMIDDGTGSLEASITKKPFNGRVISSLYSEASSLASSEAYKSIAVSMMRLLQVSMEYIDPTRISRGHSLFLRGRPNRFRGKMGLDAFQFFIDSGRSRNMEIGFVDYLTDWQRRHKTMQNTTNK
Protein: Apolipoprotein C-II (Apo-CII) (ApoC-II) (Apolipoprotein C2) (Q05020)
Organism: Mus musculus (Mouse)
Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P02655}.
Interaction partners:
- Apolipoprotein C-I
- Apolipoprotein C-III
- Apolipoprotein E
- Apolipoprotein A-I
- Lipoprotein lipase
- Apolipoprotein A-II
- Apolipoprotein A-V
- Apolipoprotein B-100
- Apolipoprotein A-IV
- Apolipoprotein C-IV
Sequence:
MGSRFFLALFLVILMLGNEVQGNQEDDSGSLALLGTVQGSLLSYWTSAKEVAKDLYQKTYPISMDEKLRDMYSKSSAAMSTYAGIFTDQLLTLLRGE
Protein: Putative amidase PB8B6.03 (EC 3.5.1.4) (Q8TFF9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Alpha-glucosidase
- Putative amidase C869.01
- Putative amidase C550.07
- Putative aldehyde dehydrogenase-like protein C922.07c
- Putative aldehyde dehydrogenase-like protein C9E9.09c
- Pentafunctional AROM polypeptide
- Putative lysine N-acyltransferase C17G9.06c
- Probable circularly permuted 1,3-beta-glucanase P23A10.11c YJL171C
- Phospholipase D1
- Uncharacterized protein C16G5.19
Sequence:
MDTPTWEVVAALKRNQVLNSIPKEWRKPNIRKEMISSGYVNTYEYLNLILPPEENAITNLSMLELATNIAKGNYTSYNVTKAFCHRAALAHQILNCCIEIFFDEALKKAKELDDVFQKTSKVVGPFHGIPISLKDQVDLPGKDSSIGYVSLVGKPKTEIALLAKILQDKGAIFYVKTTVPMAMMAPQTVSNLHGYTYNALNINLSSGGSSGGEGALLGSGASCCGIGTDIGGSIRIPSCFQGLYALKPSTGRISYLNVTNSYSGQELIPSVIGPMARSLKDIEFFTETVIASEAWKIDSKLLPIPWKNQSHLKSKKLIFGVLKTDGIVKPHPPIIRALNEVVAVLEKSGYEVIEISIPFQKDMLDTVVKVFSADARFEINNESQKTGEPVVSVVKRFVSDKIFKKPITVNEWWDLGNQVYKIRQMFLELWNNTAIQTLSGNSIDAIIAPIWASTSFLPESKADHLYTSLFNICDCPCVVFPFTKVDANIDLSDVSYKPLNEEDKENNDMYDPVLFDNMPVCLQVVTKKLEEEKCLAAASSIMDCLTN
Protein: Structural maintenance of chromosomes protein 1 (Chromosome segregation protein smc1) (Cohesin complex subunit psm1) (O94383)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate.
Subcellular location: Nucleus {ECO:0000269|PubMed:11069892}. Chromosome {ECO:0000269|PubMed:11069892}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. At anaphase, the rad21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.
Interaction partners:
- Cohesin subunit psc3
- Cohesin subunit rad21
- Sister chromatid cohesion protein mis4
- Structural maintenance of chromosomes protein 3
- Meiotic recombination protein rec11
- Sister chromatid cohesion protein pds5
- Meiotic recombination protein rec8
- Separin
- Serine/threonine-protein kinase plo1
- MAU2 chromatid cohesion factor homolog
Sequence:
MGRLLRLEVENFKSYRGHQIIGPFEDFTSIIGPNGAGKSNLMDAISFVLGVKSSHLRSTNVKELIYRGKILQRDNTDFTDSSNPTTAYVKLMYELDNGEQREYKRAITPSGATEYKIDEEIVTFSEYCGSLQKENILVRARNFLVFQGDVETIASQSPLELSKLVEQISGSLEYKSEYDKSKDEQDKAVNLSAHSFNKKRGINAELRQYQEQKTEAERYQSQKEKRDSAQLVYLLWKLFHLEKSISSNMAEVTRLKADSIQLIERRDENTKEIEKLKEKEGSIRRNLLAFDRKVRKQEKLIASKRPELISIAEKALESKSNLRKIQRKAAEIEKDYSDQASTLQVLENQLTSLSAAEKEFLKDMQEKEQLKGLRLLPEDKEEYEGLRSEADKLNSNLLFKLQTLNRNIKVTSQSKDSLTSIVGDLESKIKSLHESVSSLDTERADLLAKINEKIESLELEKHDQQKKRLTYSELFHKTQELNEELQSCLQKILEASADRNESKQDAKKREALYALKRIYPEVKGRIIDLCTPTQKKYESAIAAALGKNFDAIVVETQAVAKECIDYIKEQRIGIMTFFPMDTIAASPVNQKFRGTHKGARLAIDVLNFESEYERVMISAVGNTLICDSMTVARDLSYNKRLNAKTVTLEGTVIHKTGLITGGSSNNRSAKHWDDHDFDLLTQTKDRLMHQIGEIEYQKSSCVITESDTVKLHSLESEISLLKDKYTVVSRSVEDKKKEIGHYESLIKEKQPHLSELEMELRNFVKSRDELQIQVEKVEEKIFSGFCKRIGISDIHTYDEIHRTFTQSFTQKQLEFTKQKSLLENRISFEKQRVSDTRLRLERMHKFIEKDQESIDNYEQNREALESEVATAEAELELLKEDFASENSKTEKILLAASEKKLVGKRLVSELTKLSGNITLLESEIDRYVSEWHAILRKCKLEDIDVPLREGSLTSIPIDDVSNSGDITMGEEPSEPVINFEKFGVEVDYDELDEELRNDGSESMASVLQEKLREYSEELDQMSPNLRAIERLETVETRLAKLDEEFAAARKAAKNAKERFNAVKQKRLQKFQAAFSHISEQIDPIYKELTKSPAFPLGGTAYLTLDDLDEPYLGGIKFHAMPPMKRFRDMDQLSGGEKTMAALALLFAIHSYQPSPFFVLDEIDAALDQTNVTKIANYIRQHASSGFQFVVISLKNQLFSKSEALVGIYRDQQENSSRTLSINLEGYVE
Protein: Protein-serine O-palmitoleoyltransferase porcupine (EC 2.3.1.250) (Protein MG61) (Q9H237)
Organism: Homo sapiens (Human)
Function: Protein-serine O-palmitoleoyltransferase that acts as a key regulator of the Wnt signaling pathway by mediating the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1(9Z)), to Wnt proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9JJJ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9JJJ7}.
Interaction partners:
- Proto-oncogene Wnt-1
- Proto-oncogene Wnt-3
- Protein Wnt-7a
- Protein Wnt-3a
- Protein Wnt-5a
- Protein Wnt-2
- Protein Wnt-5b
- Protein Wnt-2b
- Protein Wnt-7b
- Protein Wnt-4
Sequence:
MATFSRQEFFQQLLQGCLLPTAQQGLDQIWLLLAICLACRLLWRLGLPSYLKHASTVAGGFFSLYHFFQLHMVWVVLLSLLCYLVLFLCRHSSHRGVFLSVTILIYLLMGEMHMVDTVTWHKMRGAQMIVAMKAVSLGFDLDRGEVGTVPSPVEFMGYLYFVGTIVFGPWISFHSYLQAVQGRPLSCRWLQKVARSLALALLCLVLSTCVGPYLFPYFIPLNGDRLLRNKKRKARGTMVRWLRAYESAVSFHFSNYFVGFLSEATATLAGAGFTEEKDHLEWDLTVSKPLNVELPRSMVEVVTSWNLPMSYWLNNYVFKNALRLGTFSAVLVTYAASALLHGFSFHLAAVLLSLAFITYVEHVLRKRLARILSACVLSKRCPPDCSHQHRLGLGVRALNLLFGALAIFHLAYLGSLFDVDVDDTTEEQGYGMAYTVHKWSELSWASHWVTFGCWIFYRLIG
Protein: RE72245p (Q6AWQ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHNLITGPHLLSNPHDISGLPIYRKMSRQSTCRLVLLLAFTLALIHASHSNTVGPKIHFIHDDLTENELNSGEEVSPTESLPKISTPKVKDLPVETTTRSPTKKTTSSGTEKSLSEEAWNDLMEAAKHSQALADDPHFNKMLNTTVAAGEKNSTDTDDSEYYDYDDDYNYFDEETVTISPSPKKAKSNPKLQPIVDATITKSKSKSNDQKTKESANDIDSDSQYDYDEGLDDDDDEDDAADDLLTDDEQVVFSEDVPCPRFCQCARNVNSYLVATCSRLDMGIQKFGSDITDLVVTNVGPKYPILMGPNFFQNLGLKNVASIKIANCTLEYLHAEAFHGLNELYAVNLTDVGLAIINPDTFVGNKKLRMLTISGNDLSVMSSIHYLLKSSSIEELDFSRNNLMELNPKAFSHLSNVVYINLSQNSLKKLPEKAFEKVTLLEELDLSYNSLTELPRDIFNGTTLSILHLKYNTFNGDLHFGTKDLQQLDLSFNSIVQVHHSMFDKMPGLTNLNLKGNGIKKIQPDSFLTLKNLRHIDLSINDLDQISGMLFFKNSELDVIRLNDNPRLSQLPTDGFLSYSGEFTVYYLDISNCAIGPLGHKAFSTMPHLTTLKLAWNNINHLPREIFTELHKLIDLDLSNNLITRMDDLIFMDNGELTKLSLAGNPISRLSVRLFLPLHQLRCLDVNDCELTTLLSDRDLGAGYKIFDSLRSFNASGNLIKKITSEDVKSFKNLRSLDITNNPLKCTPDFQEFISYVTLQMQMTPKRLPVLANLEDDATIVQLETLAQAGWSSLAHEVCKHAEGSDLLDEKKADSAEAKLEKRLKESVKKLNEDEAKLLSVLDKSVLDKSRLSSMQKIMKGSVNTETAKPEEDADEENLNNGGEDKEDDSSDYDSEEDDDDDDEDDDDDNNDDDRFEEAKKNAKAKADANKAFDTFVNKELKPVLKTDGIQAEEVDMSQETRDKFLLEKLGFDSESEESDEYTEKMIFHGELSYDLVVPLIVVSFCLLMIVLSIARVIYVVLRKRGERYRMALLASKNSFVYQKLSEDIVKPTSKEQKEPKHLKQPKVHRYAPINQV
Protein: Alginate lyase (EC 4.2.2.3) (Poly(beta-D-mannuronate) lyase) (Q06749)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the depolymerization of alginate by cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues via a beta-elimination mechanism. May serve to degrade mislocalized alginate that is trapped in the periplasmic space. Acts preferentially on non-acetylated alginate or its precursor mannuronan. Is able to catalyze cleavage adjacent to either mannuronate or guluronate residues in alginate. Exhaustive digestion of alginate by AlgL generates dimeric and trimeric products. In addition to its enzymatic function, AlgL appears to be required for alginate export, maybe as part of a multi-protein alginate-secretion complex.
Subcellular location: Periplasm {ECO:0000255|HAMAP-Rule:MF_00557, ECO:0000269|PubMed:8370530, ECO:0000305|PubMed:8335634}.
Interaction partners:
- Alginate biosynthesis protein AlgX
- Alginate biosynthesis protein AlgK
- Mannuronan C5-epimerase
- Mannuronan synthase
- Probable alginate O-acetylase AlgJ
- Mannuronan synthase
- Alginate production protein AlgE
- Probable alginate O-acetylase AlgI
- GDP-mannose 6-dehydrogenase
- Alginate biosynthesis protein AlgA
Sequence:
MKTSHLIRIALPGALAAALLASQVSQAADLVPPPGYYAAVGERKGSAGSCPAVPPPYTGSLVFTSKYEGSDSARATLNVKAEKTFRSQIKDITDMERGATKLVTQYMRSGRDGDLACALNWMSAWARAGALQSDDFNHTGKSMRKWALGSLSGAYMRLKFSSSRPLAAHAEQSREIEDWFARLGTQVVRDWSGLPLKKINNHSYWAAWSVMSTAVVTNRRDLFDWAVSEFKVAANQVDEQGFLPNELKRRQRALAYHNYALPPLAMIAAFAQVNGVDLRQENHGALQRLAERVMKGVDDEETFEEKTGEDQDMTDLKVDNKYAWLEPYCALYRCEPKMLEAKKDREPFNSFRLGGEVTRVFSREGGS
Protein: Carbohydrate sulfotransferase 7 (EC 2.8.2.-) (EC 2.8.2.17) (Chondroitin 6-sulfotransferase 2) (C6ST-2) (mC6ST-2) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5) (GST-5) (N-acetylglucosamine 6-O-sulfotransferase 4) (GlcNAc6ST-4) (Gn6st-4) (Q9EP78)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues. Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Also acts on core 2 mucin-type oligosaccharide and N-acetyllactosamine oligomer with a lower efficiency. Has weak or no activity toward keratan sulfate and oligosaccharides containing the Galbeta1-4GlcNAc. Catalyzes 6-O-sulfation of beta-benzyl GlcNAc but not alpha- or beta-benzyl GalNAc.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Carbohydrate sulfotransferase 3
- Carbohydrate sulfotransferase 12
- Chondroitin sulfate N-acetylgalactosaminyltransferase 2
- Carbohydrate sulfotransferase
- Carbohydrate sulfotransferase 14
- Carbohydrate sulfotransferase 11
- Carbohydrate sulfotransferase 15
Sequence:
MKGRRRRRREYCKFTLLLALYTLLLLLVPSVLDSHSEQDKGRNCPGLQRSLGVWSLEAAAAGEREQGAEVRSLAEGNPDRSPGSPGNLSAVGEAVTQEKQHIYVHATWRTGSSFLGELFNQHPDVFYLYEPMWHLWQALYPGDAESLQGALRDMLRSLFRCDFSVLRLYAQPGDPGERAPDSANLTTAMLFRWRTNKVICSPPLCPAAPRARADVGLVEDKACESTCPPVSLRALEAECRKYPVVVIKDVRLLDLGVLVPLLRDPGLNLKVVQLFRDPRAVHNSRLKSRQGLLRESIQVLRTRQRGDHFHRVLLAHGVDARPGGQARALPSAPRADFFLTSALEVICEAWLRDLLFTRGAPAWLRRRYLRLRYEDLVWQPQAQLRRLLRFSGLRTLAALDAFAFNMTRGSAYGADRPFHLSARDAREAVHAWRERLSQEQVRQVETACAPAMRLLAYPRSGDERDRKTVREGETPLETKANWAV
Protein: Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.360) (Histone H3-K79 methyltransferase) (Q581Z0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU271113}.
Interaction partners:
- Histone H3 variant
- Histone H3, putative
- Histone H4
- Histone H4
Sequence:
MPGLLISRKRTRSEASGKPIGEIKCVAENRVQALKPPLGELVPKGELGAGTPHEPYNLPLRGNPNKSGCHHCLADQCHCVFFERLLDATFRRLDIKRITEVSGSRHLCAKSLLPTFVSRMVRLMEITSEDTFYDLGCGNGSILFQVAFLTGARCVGIEISEHNAKVAKKAWEVIRPELEGSSGRSMPEVNIITSDMTKILADERLFESERGKTVILLSNLLFPKSLTHYLSERFRRVPSGTRILCFDDLYPHSRSVAAIRDPEAFRLFAMTDYRWQECSVEWCTRDGPFFIHRRR
Protein: Caspase-14 (CASP-14) (EC 3.4.22.-) (Mini-ICE) (MICE) [Cleaved into: Caspase-14 subunit p17, mature form; Caspase-14 subunit p10, mature form; Caspase-14 subunit p20, intermediate form; Caspase-14 subunit p8, intermediate form] (O89094)
Organism: Mus musculus (Mouse)
Function: Non-apoptotic caspase which is involved in epidermal differentiation. Seems to play a role in keratinocyte differentiation and is required for cornification. Regulates maturation of the epidermis by proteolytically processing filaggrin. In vitro is equally active on the synthetic caspase substrates WEHD-ACF and IETD-AFC. Involved in processing of prosaposin in the epidermis. May be involved in retinal pigment epithelium cell barrier function (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11175259}. Nucleus {ECO:0000269|PubMed:11175259}.
Interaction partners:
- Filaggrin
- Bleomycin hydrolase
- Protein-glutamine gamma-glutamyltransferase E
- Loricrin
Sequence:
MESEMSDPQPLQEERYDMSGARLALTLCVTKAREGSEVDMEALERMFRYLKFESTMKRDPTAQQFLEELDEFQQTIDNWEEPVSCAFVVLMAHGEEGLLKGEDEKMVRLEDLFEVLNNKNCKALRGKPKVYIIQACRGEHRDPGEELRGNEELGGDEELGGDEVAVLKNNPQSIPTYTDTLHIYSTVEGYLSYRHDEKGSGFIQTLTDVFIHKKGSILELTEEITRLMANTEVMQEGKPRKVNPEVQSTLRKKLYLQ
Protein: AT3G48140 protein (B12D protein) (B12D-like protein) (Q42338)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASRWLRPEVYPLFAATGVAVGICAFSLIRNITGNPEVRCTKENRAAGILDNHAEGEKYKENFLRKFVRNKKPEIMPGLNKFFTDPTY
Protein: Protein wntless homolog (Abnormal cell migration protein 14) (Q7YWX7)
Organism: Caenorhabditis elegans
Function: Probable sorting receptor which regulates endocytosis and secretion of the wnt ligand egl-20. Recycling of mig-14 from the plasma membrane to the Golgi apparatus by the retromer complex is essential for its function. Its endosomal trafficking is regulated by its association with sorting nexin snx-3 on early endosomes and the mtm-6/mtm-9 myotubularin complex. Required in embryonic development for endoderm specification and the correct positioning and orientation of the mitotic spindles and division planes in blastomere cells. Functions during vulval development, playing a role in vulval precursor cell fate specification. During development, specifically regulates the migration of HSN neurons, the left Q neuroblast (QL) and its descendants and the distal tip cells of the gonads. Positioning of Q neuroblasts may be both dependent and independent of hox gene mab-5. Involved in establishing ALM and PLM neuronal cell polarity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18160346, ECO:0000269|PubMed:18160347}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:19763082, ECO:0000269|PubMed:21076391}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18160347, ECO:0000269|PubMed:19763082}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000269|PubMed:26115433}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:26115433}; Multi-pass membrane protein {ECO:0000255}. Note=Traffics between endosomal cell membrane and the Golgi apparatus membrane and the cell membrane to mediate wnt/egl-20 secretion (PubMed:18160347, PubMed:21076391). Co-localizes with snx-3 on intracellular punctae and early endosomes to facilitate recycling and wnt/egl-20 secretion (PubMed:21076391). Localizes to the basolateral cell membrane of intestine cells, but not the apical cell membrane (PubMed:26115433). {ECO:0000269|PubMed:18160347, ECO:0000269|PubMed:21076391, ECO:0000269|PubMed:26115433}.
Interaction partners:
- Protein Wnt
- Protein Wnt-2
- Protein Wnt-1
- Abnormal cell lineage protein 44
- Protein-serine O-palmitoleoyltransferase porcupine
- Sorting nexin-3
- Protein mom-2
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 29
- Protein mom-5
Sequence:
MAGGAVIENLSNRKLFVIFAGLLVIQIMFFLIGAWYAPSPSSYMEFEMITCRDETKGLSGEWIHRDNCQQISELSEYTPSSFDLREIVFIAKMPHTRDGIELEYSPWFQFLLGVLHVDVEYSEHFKYVAHAPLELEVRMGYRDKESKKNEWKELVTSNVTRILECTIAEDEKKAGGTYDCDMLDLFELGSSSYPFYLINIRIPINQQACQFDNKSANCQIGKLTGLRLIEIHQNGGFTLVWLWTKTFMTPVVAICLWWYYNRINQLARNPLLLERAILLLGLSLVILDFPIEWISLTYRIPFLLLISDLRQGLFYTVLFSFWLIFAGEHLIDDNTRNNLKSYRFNLSFIITASLGLLIYDLIERGIQLYDPFYSVWSSPTGSQIAYFAIFISAISTVAYFIFLFFKIARVWSTIKSKRSAQIYQTSENRRLKVEGVIYRFKFLMLFTLLCSAFTIAAYFMKQYGEAQLHGDEARDGFLTGSTSAFFTGAFGMCNIYVLLLLAMYAPSHKHYRGASQLIDENDDDEIMEDPSNQHTESNAMTTFLKPSTD