wanglab/gogpt-training-data huggingface dataset:
Protein: Pecanex-like protein 4 (Hepatitis C virus F protein-binding protein 2) (HCV F protein-binding protein 2) (Pecanex homolog protein 4) (Q63HM2)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSPDVPLLNDYKQDFFLKRFPQTVLGGPRFKLGYCAPPYIYVNQIILFLMPWVWGGVGTLLYQLGILKDYYTAALSGGLMLFTAFVIQFTSLYAKNKSTTVERILTTDILAEEDEHEFTSCTGAETVKFLIPGKKYVANTVFHSILAGLACGLGTWYLLPNRITLLYGSTGGTALLFFFGWMTLCIAEYSLIVNTATETATFQTQDTYEIIPLMRPLYIFFFVSVDLAHRFVVNMPALEHMNQILHILFVFLPFLWALGTLPPPDALLLWAMEQVLEFGLGGSSMSTHLRLLVMFIMSAGTAIASYFIPSTVGVVLFMTGFGFLLSLNLSDMGHKIGTKSKDLPSGPEKHFSWKECLFYIIILVLALLETSLLHHFAGFSQISKSNSQAIVGYGLMILLIILWILREIQSVYIIGIFRNPFYPKDVQTVTVFFEKQTRLMKIGIVRRILLTLVSPFAMIAFLSLDSSLQGLHSVSVCIGFTRAFRMVWQNTENALLETVIVSTVHLISSTDIWWNRSLDTGLRLLLVGIIRDRLIQFISKLQFAVTVLLTSWTEKKQRRKTTATLCILNIVFSPFVLVIIVFSTLLSSPLLPLFTLPVFLVGFPRPIQSWPGAAGTTACVCADTVYYYQMVPRLTAVLQTAMAAGSLGLLLPGSHYLGRFQDRLMWIMILECGYTYCSINIKGLELQETSCHTAEARRVDEVFEDAFEQEYTRVCSLNEHFGNVLTPCTVLPVKLYSDARNVLSGIIDSHENLKEFKGDLIKVLVWILVQYCSKRPGMKENVHNTENKGKAPLMLPALNTLPPPKSPEDIDSLNSETFNDWSDDNIFDDEPTIKKVIEEKHQLKDLPGTNLFIPGSVESQRVGDHSTGTVPENDLYKAVLLGYPAVDKGKQEDMPYIPLMEFSCSHSHLVCLPAEWRTSCMPSSKMKEMSSLFPEDWYQFVLRQLECYHSEEKASNVLEEIAKDKVLKDFYVHTVMTCYFSLFGIDNMAPSPGHILRVYGGVLPWSVALDWLTEKPELFQLALKAFRYTLKLMIDKASLGPIEDFRELIKYLEEYERDWYIGLVSDEKWKEAILQEKPYLFSLGYDSNMGIYTGRVLSLQELLIQVGKLNPEAVRGQWANLSWELLYATNDDEERYSIQAHPLLLRNLTVQAAEPPLGYPIYSSKPLHIHLY
Protein: ALF transcription elongation factor 4 (A0A8I6GGV9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNREDRNVLRMKERERRNQEIQQGEDAFPPSSPLFAEPYKVTSKEDKLSSRIQSMLGNYDEMKDYIGDRSIPKLVAIPKPAVPTTTDEKANPNFFEQRHGGSHQSSKWTPVGPAPSTSQSQKRSSGLQSGHSSQRSSAGGSGASGSGQRHDRDSYSSSRKKGQHGSEHSKSRSSSPGKPQAVSSLSSSHSRSHGNDHHSKEHQRSKSPRDPDANWDSPSRVPFSSGQHSSQSFPPSLMSKSSSMLQKPTAYVRPMDGQESVEPKLSSEHYSSQSHGSNMTELKPSSKAHLTKLKIPSRPLDASVSGDVSCVDEILKEMTHSWPPPLTAIHTPCKTEPSKFPFPTKVMGLCCHYKGNICHFYFISFSNSEPSHHNSEGADNSRDDSSSHSGSESSSGSDSESESSSSDSEANEPSQSASPEPEPPPTNKWQLDNWLNKVNPHKVSPASSVDSNIPSSQAYKKEGREQGTASNYTDPGGAKEASSATPGRDSKTIQKGSESGRGRQKSPAQSDSTTQRRTVGKKQPKKTEKSAAEEPRGGLKIESETPVDMATSMPSSRHKAATKGSRKPNIKKESKSSPRPTAEKKKYKSASKSSQKSREIIETDSSSSDSDERESLPPSSQTPKYPESNRTPVKPSSAEEDDSFFRQRMFSPMEEKELLSPLSDPDDRYPLIVKIDLNLLTRIPGKPYKETEPPKGEKKNVPEKHSREVQKQASEKASNKGKRKHKNDDDNRASESKKPKTEDKNSSAHKPSSSKESSKQSSTKEKDLLPSPAGPVPSKDSKTEHGSRKRTVSQSSSLKSSSTSNKENSGSSKSTSSTAKQKKTEGKVSSSSKEAKEKAPNSSSNCPPSTPTPDSSKPRRTKLAFDDRNYSADHYLQEAKKLKHNADALSDRFEKAVYYLDAVVSFIECGNALEKNAQESKSPFPMYSDTVELIKYTMKLKNYLAPDATAADKRLTVLCLRCQSLLYLRLFKLKKENALKYSKTLTEHLKNSYSNSQAPSPGLGSKAVGMPSPVSPKLSPGNSGSYSSGGSSASASGSSVTIPQKIHQMAASYVQVTSNFLYATEIWDQAEQLSKEQKEFFAELDKVMGPLIFNASIMTDLARYTRQGLHWLRQDAKLIS
Protein: Putative flavin-containing monoamine oxidase AofH (EC 1.4.3.-) (P9WQ15)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable O-methyltransferase Rv1703c
- Probable helicase HelZ
- Probable alcohol dehydrogenase adh
- aldehyde dehydrogenase
- Probable aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Probable aldehyde dehydrogenase NAD dependent AldA
- Probable alcohol dehydrogenase AdhA
- Probable zinc-type alcohol dehydrogenase
- Alcohol dehydrogenase B
Sequence:
MRLTRAVTNPPWTVDVVVVGAGFAGLAAARELTRQGHEVLVFEGRDRVGGRSLTGRVAGVPADMGGSFIGPTQDAVLALATELGIPTTPTHRDGRNVIQWRGSARSYRGTIPKLSLTGLIDIGRLRWQFERIARGVPVAAPWDARRARELDDVSLGEWLRLVRATSSSRNLMAIMTRVTWGCEPDDVSMLHAARYVRAAGGLDRLLDVKNGAQQDRVPGGTQQIAQAAAAQLGARVLLNAAVRRIDRHGAGVTVTSDQGQAEAGFVIVAIPPAHRVAIEFDPPLPPEYQQLAHHWPQGRLSKAYAAYSTPFWRASGYSGQALSDEAPVFITFDVSPHADGPGILMGFVDARGFDSLPIEERRRDALRCFASLFGDEALDPLDYVDYRWGTEEFAPGGPTAAVPPGSWTKYGHWLREPVGPIHWASTETADEWTGYFDGAVRSGQRAAAEVAALL
Protein: Centriolar satellite-associated tubulin polyglutamylase complex regulator 1 (Q9H6J7)
Organism: Homo sapiens (Human)
Function: Regulator of the tubulin polyglutamylase complex (TPGC) that controls cytoskeletal organization, nuclear shape, and cilium disassembly by balancing microtubule and actin assembly. Regulates the assembly and stability of the TPGC and thereby modulates polyglutamylation of the microtubule, which antagonizes MAP4 binding.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:34782749}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:34782749}. Note=Associated with microtubules. {ECO:0000269|PubMed:34782749}.
Interaction partners:
- Leucine-rich repeat-containing protein 49
- Polyglutamylase complex subunit TTLL1
- Tubulin polyglutamylase complex subunit 2
- Nicolin-1
- Tubulin polyglutamylase complex subunit 1
- Eukaryotic translation initiation factor 3 subunit F
Sequence:
MLSPERLALPDYEYLAQRHVLTYMEDAVCQLLENREDISQYGIARFFTEYFNSVCQGTHILFREFSFVQATPHNRVSFLRAFWRCFRTVGKNGDLLTMKEYHCLLQLLCPDFPLELTQKAARIVLMDDAMDCLMSFSDFLFAFQIQFYYSEFLDSVAAIYEDLLSGKNPNTVIVPTSSSGQHRQRPALGGAGTLEGVEASLFYQCLENLCDRHKYSCPPPALVKEALSNVQRLTFYGFLMALSKHRGINQALGALPDKGDLMHDPAMDEELERLLAQVPGLVNSVTASPEASCLPSRTPPRVGSPWRPLHHSRKVDGESDGSTEETDESET
Protein: Kallikrein-4 (EC 3.4.21.-) (Enamel matrix serine proteinase 1) (Kallikrein-like protein 1) (KLK-L1) (Prostase) (Serine protease 17) (Q9Y5K2)
Organism: Homo sapiens (Human)
Function: Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Plasma protease C1 inhibitor
- Kininogen-1
- Alpha-2-macroglobulin
- Matrix metalloproteinase-20
- Serine protease inhibitor Kazal-type 5
- Antithrombin-III
- WD repeat-containing protein 72
- B2 bradykinin receptor
- Kallistatin
- Angiotensin-converting enzyme
Sequence:
MATAGNPWGWFLGYLILGVAGSLVSGSCSQIINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIGLGLHSLEADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIRSISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSKLYDPLYHPSMFCAGGGHDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQVGVPGVYTNLCKFTEWIEKTVQAS
Protein: MTOR-associated protein MEAK7 (MEAK7) (TBC/LysM-associated domain-containing protein 1) (TLD domain-containing protein 1) (Q8K0P3)
Organism: Mus musculus (Mouse)
Function: Activates an alternative mTOR signaling through RPS6KB2 activation and EIF4EBP1 repression to regulate cell proliferation and migration. Recruits MTOR at the lysosome, essential for MTOR signaling at the lysosome.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q6P9B6}. Cytoplasm {ECO:0000250|UniProtKB:Q6P9B6}. Lysosome {ECO:0000250|UniProtKB:Q6P9B6}.
Interaction partners:
- Ribonuclease kappa
- V-type proton ATPase subunit e 1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit H
- V-type proton ATPase subunit D
- V-type proton ATPase subunit G 1
- V-type proton ATPase subunit S1
- Renin receptor
Sequence:
MGNAKSLSGQKMASRFLPEEQAEVDKLFDVLSSSEGGVATGTFSLEAMKSHVKEALPPAMVTRLYNGMQRVKPTDRTLGSCRSVSREQFTAFLSQLLRGSCEEKGLMVMNMISDAEGPTKTRDVQKFTEDLVASVAHVLTHRHELRGWTCRKSEVPPDSMQAMVAQLLSEMKFQDGYKFQGPQCLDQVCDQAMIEEWVFHVPHVGMFLSVVVHRGLCLLGSSFDPSTLVPECLADQGGRFESILDVLSVIYLSSHLAPEHRQRWRLLFSTQLHGQSFSQLCSHITSQGPSLLVLEDRDGYVFGGFASCSWEVKPQFQGDNRCFLFSIAPRMATHLHTGYNNHFMYLNYGQQTMPNGLGMGGQHHYFGLWVAADFGKGHSKAKPACTTYNSPQLSAQEDFLFDKMEVWGLGNLLEEYEGKNKKSVLDSNPEARSLLEISGRARHSEGLREVPRDED
Protein: Solute carrier family 7 member 12 (Asc-type amino acid transporter 2) (Asc-2) (X-amino acid transporter 1) (XAT-1) (Q8VIE6)
Organism: Mus musculus (Mouse)
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:11591708}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000269|PubMed:11591708}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:11591708}.
Interaction partners:
- Amino acid transporter heavy chain SLC3A1
- Cationic amino acid transporter 3
- High affinity cationic amino acid transporter 1
Sequence:
MQLLRALGVFHVSMILFSATLGTGIFVTPKAVLKYSSLNIPVSLSIWAGCGLLSIMSALCNAEIATTYPLSGASYYFLKRTLGSSVAFLSLWIKLFAHFLGIGAQCLLIATSVIQCFYSGCPAPELPTKCLALAILWSFGIVSARGIKTVAWFNTVSSFIKLSVLCLISLTVLLVNGKKENVSRFENALDAELPNASQIADAILQVSYSYLGSSVLIVIAGEIKRPTETIPKTLIYGISIVTVLYLLTNISYLAVLTSQEIIFSDSVGVTWMNRVFPSIQWISSFLISAFLLGSVSCGIVSASRVFYSASQEGEFPSIYSMLNDHHSPAVADIQIVILSSVAIISSSIIYLVKYVSLGSFCINLLQMIGLLKIRYQNPDIPRPYKVWLPFIFGSIALSLFLIFTPVIQSPSIEHVYQVVFLFCGFLCYWLQANLNGHATCFDTITCYCQLLFNISPSEDPEEQKN
Protein: Kelch-like protein 12 (Q5U374)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of Wnt signaling pathway and ER-Golgi transport. The BCR(KLHL12) complex is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division (By similarity). Negatively regulates the Wnt signaling pathway, possibly via the targeted ubiquitination and subsequent proteolysis of dvl2 and dvl3. Regulates convergent-extension movements during early embryonic development.
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle {ECO:0000250|UniProtKB:Q53G59}.
Interaction partners:
- Cullin-3A
- Cullin 3
- Peflin
- Protein transport protein Sec31A
- Kelch like family member 12.
- Protein SEC13 homolog
- Protein transport protein Sec24D
- Protein transport protein Sec23A
- Protein transport protein Sec24C
- Protein transport protein Sec31A
Sequence:
MAPKDIMTNSHAKSILNAMNALRKSNTLCDITLRVEGTDFPAHRIVLAACSDYFCAMFTSELAEKGKSFVDIQGLTASTMEILLDFVYTETVLVTVENVQELLPAACLLQLKGVKRACCDFLNSQLDPSNCLGIRDFAETHNCLDLMQAAELFSQKHFAEVVQQEEFMLLSQSEVEKLIKCDEIQVDSEEPVFEAVLNWVKHNRKEREPYLPDLLEYVRMPLLTPRYITDVIDAEPLIRCSLPCRDLVDEAKKFHLRPELRSEMQSPRTQARLGAKEVLLVIGGFGSQQSPIDIVEKYDPKTREWSFLPNIARKRRYVATVALNDRVYVIGGYDGRSRLSSVECLDYTADEDGVWYSVATMNVRRGLAGATTLGDMIYVAGGFDGSRRHTSMERYDPNIDQWSMLGDMQTAREGAGLVVASGLIYCLGGYDGLNILNSVERYDPHTGHWTSVTPMANKRSGAGVALLNDHIYVVGGFDGTAHLSSVEVYNIRTDYWTTVANMTTPRCYVGATVLRGRLYAIAGYDGNSLLSSIECYDPVIDSWEVVTSMATQRCDAGVCVLREK
Protein: Beta-monoglucosyldiacylglycerol synthase (Beta-MGS) (MGlcDAG synthase) (EC 2.4.1.336) (UDP-glucose:1,2-diacylglycerol 3-beta-D-glucosyltransferase) (Q8YMK0)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Function: Glucosyltransferase involved in the biosynthesis of the non-bilayer-forming membrane lipid beta-monoglucosyldiacylglycerol which contributes to regulate the properties and stability of the membrane. Catalyzes the transfer of a glucosyl residue from UDP-Glc to diacylglycerol (DAG) acceptor to form the corresponding beta-glucosyl-DAG (1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol). It can only use UDP-Glc as sugar donor. Two types of DAG (dipalmitoyl-DAG (DPDAG) and 1-oleoyl-2-palmitoyl-DAG (OPDAG)) can be used as sugar acceptors, but OPDAG is preferred.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Alr1909 protein
- Alr1352 protein
- Diacylglycerol kinase
- Polysaccharide deacetylase
- Alr1793 protein
Sequence:
MPANSWPDNDSYKELDPLNSLLSDVSTTEESVVETRDLSLPSRFQGRRGKAALVLTIVWSGTIALHLVSWGSIFILGLTTVLGIHALGVVFARPRHYQKEIQGSLPFVSILVAAKNEEAVIAKLAKNLCNLEYPNGQYEVWIIDDNSTDKTPHILAELAKEYDKLKVLRRSAQATGGKSGALNQVLPLTQGEIIAVFDADAQVASDMLLHVVPLFQREKVGAVQVRKAIANAKENFWTKGQMAEMSLDIWFQQQRTALGGIGELRGNGQFVRRQALDSCGGWNEETITDDLDLTFRLHLDKWDIECLFYPAVQEEGVTTAIALWHQRNRWAEGGYQRYLDYWDLILKNRMGTRKTWDMLMFMLTMYILPTAAIPDLLMALTRHRPPMLGPVTGLSVTMSVVGMFAGLRRIRQEQKFQVHTPFVLLLQTMRGTLYMLHWLVVMSSTTARMSFRPKRLKWVKTVHTGTGE
Protein: Ubiquitin-conjugating enzyme E2 (EC 2.3.2.23) (Q8I607)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Ubiquitin-60S ribosomal protein L40
- Ubiquitin-conjugating enzyme E2, putative
- RING-type E3 ubiquitin transferase
- Ubiquitin-activating enzyme E1
- E3 ubiquitin-protein ligase CHIP
- Polyubiquitin
- Ubiquitin-activating enzyme
- Ribosomal protein S27a, putative
- CCR4-NOT transcription complex subunit 4, putative
- Anaphase-promoting complex subunit 11, putative
Sequence:
MALKRITKELQDLNKDPPTNCSAGPIGDDLFFWQATIMGPGDSPYENGVYFLNIKFPPDYPFKPPKIIFTTKIYHPNINTAGAICLDILKDQWSPALTISKVLLSISSLLTDPNADDPLVPEIAHVYKTDRTKYHQTAKAWTQKYAQ
Protein: Adenylosuccinate synthetase (AMPSase) (AdSS) (EC 6.3.4.4) (IMP--aspartate ligase) (A0A8I6G9X7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03125}.
Interaction partners:
Sequence:
MSGTRASNDRPPGTGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADIVSRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKGRPPMAFQAPQQHPLCVFSIGTTKKGIGPTYSSKAARTGLRICDLLSDFDEFSARFKNLAHQHQSMFPTLEIDVEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGDLLQNRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVLSEIKVGISYKLNGKRIPYFPANQEILQKVEVEYETLPGWKADTTGARKWEDLPPQAQSYVRFVENHLGVWAGLAGQRTPGLCLPSPGIIRVLHQASIVTWALGIKLRFLWL
Protein: ribose-phosphate diphosphokinase (EC 2.7.6.1) (C8V1P9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Ribose-phosphate pyrophosphokinase
- ribose-phosphate diphosphokinase
- Multifunctional tryptophan biosynthesis protein
- 3-methyl-2-oxobutanoate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta
Sequence:
MRGVQIFSGNSHPLLTETVCERLGTSPAKVELGKFSNGETNVNVGVSVRNQDVYIIQSGSEKINDSVMELLIMISACKGGSAKSITAVMPYFPYSRQSKKKSHRGSITARMLANLLTVAGVDHVITLDLHASQMQGFFSKPVDNLFAEPFIARWIRNNVPGWKEAVVVSKNAGGTKRVTSLADTLKLNFGIVTTDRRRQKPGPTLADSTVFFEALDQETTPLPKEQDPFIARTHIENPDALQSRESQADLNELDSLRPETPSGARRPSELEAVNEYTDVRVRDVITGRLVQGHLVDDDYPPSGPTSMAVSGDATPGQLPSQESEAIPDSMVDSVVSTTSSMPGDHALGGSFDAADSSDEEEGSTKRNVEQEKTITLVGDVRDRTVFLVDDMIDKSGSWIAAAETVVKRGGAKKVYCIATHGLFGDSSLEQLEACESINYIVVTNTFPISPQVARKSRKLIIIDISSLLSESIRRHHYGESVSALFHLND
Protein: Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B (EC 2.4.1.145) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVb) (GlcNAc-T IVb) (GnT-IVb) (N-acetylglucosaminyltransferase IVb) (UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVb) (Q812F8)
Organism: Mus musculus (Mouse)
Function: Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains. Prefers complex-type N-glycans over hybrid-types. Has lower affinities for donors or acceptors than MGAT4A, suggesting that, under physiological conditions, it is not the main contributor in N-glycan biosynthesis.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9D4R2}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9D4R2}. Note=A processed soluble form also exists. {ECO:0000250|UniProtKB:Q9UQ53}.
Interaction partners:
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B
- Alpha-
- Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4D
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
Sequence:
MRLRNGTFLTLLLFCLCAFLSLSWYAALSGQKGDVVDIYQREFLALRDRLHAAEQESLKRSKELNLVLEEIKRAVSERQALRDGEGNRTWGRLTEDPRLKPWNVSHRHVLHLPTVFHHLPHLLAKESSLQPAVRVGQGRTGVSVVMGIPSVRREVHSYLTDTLHSLISELSPQEKEDSVIVVLIAETDPQYTSAVTENIKALFPTEIHSGLLEVISPSPHFYPDFSRLRESFGDPKERVRWRTKQNLDYCFLMMYAQSKGIYYVQLEDDIVAKPNYLSTMKNFALQQPSEDWMILEFSQLGFIGKMFKSLDLSLIVEFILMFYRDKPIDWLLDHILWVKVCNPEKDAKHCDRQKANLRIRFKPSLFQHVGTHSSLAGKIQKLKDKDFGKHALRKEHVNPPAEVSTSLKTYQHFTLEKAYLREDFFWAFTPAAGDFIRFRFFQPLRLERFFFRSGNIEHPEDKLFNTSVEVLPFDNPQSEKEALQEGRSATLRYPRSPDGYLQIGSFYKGVAEGEVDPAFGPLEALRLSIQTDSPVWVILSEIFLKKAD
Protein: Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.-) (Q55AK6)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Poly [ADP-ribose] polymerase
- Probable phosphatidate cytidylyltransferase
- 2'-phosphotransferase
Sequence:
MNNNNNNNNNNNNNNINNNNNNNINNNNNNNINNNNNNNNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKNINKLKNINSEKNNNKNKNINKKACDNSDNNNNNVKETLESYFSNIAPDSLLDNITGIILINPHIVQCSGHTYSYSTLEKCNSKEPLTNQPFKIEECILNRGKQNEIESFFETQFEKINNDFIKEKKIETLIPILKLIPFIISDNRSSCLNAKRNFEKTLSNDSTVNPLMNEIKKLNETQYNSWRELTKQQQQQQQQQQQQQQQQQQQQQQQQKQKQLPQLPQQQKHQPQQQQQQQQQQQQQQQKQLPQLPQLPQLPQQQQQQLQQQQQQQQQQQQQQQQQQQQQQQQQQQFINSKLIDSNNNLIVDKRFHIYIKIHLLRQWKQSIIPSKIIEKDGTFKVEGQLSSESQESILLQIGNLRRERVKFNSLFFETHKNLIYKYSKAIKTYLTHFQIDENNNTNQHQQQQHNNQNQKQKSNNKNNNQIFFLITGESSKVILVKNFIEDFKNLKKFVPMNEQQMRGRYDWSSLNTKDYVMHYQNGGIKMEANSKENLEIVSAIVMNLLNKSKVEHVYEVEKEIEILFLEQKSILKLINQKFTNSTRIIGTNKISIKSLETVYIQIKKIIDEALNGFYEKTIDLSGDDLFIKSKVLSNILKSLQEQCNNNNDELVSIKISPSKSDDTQIDFKNVLVYGNKNQVEKIEKSIISSKNSIHFQKYNSPNLKEILIVATSNLMKIKEIEKQYNATILINSEEIIICVPCIEKFKLVTADIDSLISTTPSETKTIQLSKLSSLKLKNLIESLEIKSQQIGIRYYYNKEELNVKISGDPENIKIIYLELLKEKYSYENSIETRAITIDKIRHDILFDLKKVGKLQKETFTLVELKVENETIISLNLSNGKIIRIIKGDITKQKTHAIVNPANEKLKNLGGAAFSIQEAAGATFKEFCESYYEKNGPIGTGCSVYGSKFKMGNIFVINTVGPKNDNPNKARILHMSIHSSLRSATALNCQSISIPAISTGIFGYDPKEAVPIIIKSAIEFLLTNETTLNEVNFVDLNQSTANIFENSLIKFSDNGTLFHNKNSSINKNTTTQPNKSILNTNYEPIKPKSLNYEWTWRENDGKDIPYDYDQSIQIEKAYNSRLRLVSIIGDLNQKKNGSTYTVYFIDHNNPSSWYQLNDKLQYTKRLVKRNIINNNINNNNKNNKNTTPTTINNNNNNNNDGNGFFGQLLKLLNPKTNNNNNKNNPNNNNPNNNIPNNNNNNNNNNNNNNNNNNNNNNNNKNNNNNDDDDDDDGVVVKSKNKYQIIVKGNINDIRSFVKELEDLVIKYKYSENIINIQIPIDSLSFIKDKCLSYGVEINYDTKTSNVNLEGLKEQVLDIKSQILEFKNNNKIIYPNRWDHKKECCLVEIEKGGKEWLEIRTRMSETLPGVIINKVEFVQNRSSYEDYYYKKNKIEAHNNGKSVSVYVCVCVCVCVCGELYLFHGTSATQPESIYNSKNCFDWRFSKESCMWGNGSYFAYNASYSHRYSYKTPQKLNQIFIATVLIGDSITSEPDSSLKLPPLKDSTNKNVRYDSVKGNPLGSDIYIVYDNQQSYPYYLVTYTYN
Protein: Collagenase 3 (EC 3.4.24.-) (Matrix metalloproteinase-13) (MMP-13) (UMRCASE) (P23097)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000250}.
Interaction partners:
- Metalloproteinase inhibitor 2
- Aggrecan core protein
- Cathepsin K
- A disintegrin and metalloproteinase with thrombospondin motifs 5
- Metalloproteinase inhibitor 1
- A disintegrin and metalloproteinase with thrombospondin motifs 4
- Stromelysin-1
- Collagen alpha-1
- Collagen type X alpha 1 chain
- Metalloproteinase inhibitor 3
Sequence:
ATFFLLSWTHCWSLPLPYGDDDDDDLSEEDLEFAEHYLKSYYHPVTLAGILKKSTVTSTVDRLREMQSFFGLDVTGKLDDPTLDIMRKPRCGVPDVGVYNVFPRTLKWSQTNLTYRIVNYTPDISHSEVEKAFRKAFKVWSDVTPLNFTRIHDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNLGGDAHFDDDETWTSSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPEKCDPALSLDAITSLRGETMIFKDRFFWRLHPQQVEPELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGYDIMEGYPRKISDLGFPKEVKRLSAAVHFEDTGKTLFFSGNHVWSYDDANQTMDKDYPRLIEEEFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSLLWC
Protein: Activity-dependent neuroprotective protein 2a (ADNP homeobox protein 2a) (A4QP16)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May be involved in transcriptional regulation. Required for progression through late erythroid differentiation. May be involved in vasculogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MYQIPVKNLTKLRRPRKRVKSILCDIGMQQCQDMLETYKCFDAGDASFDNTEWDDFTDGHVGKKKKKYPYRSQSLCCSLCWYSSRSVPTFRSHIHRCHWKNLDGACLLMCPYCPFVSSPKVTEQHIQFFHMLPSRAHQSHPSHTLAHTPKTISVTVSADAADDRYTCATCGYHDSLLYVMKKHVLVNHFATLLDRYFGLGSESAPMAGPQIRDGTPVKYHCKLCKLPAETIEHLLYHILSSEKHKELHWQIMPCIIEKECMNQMVGLQNLLNLAPKSMQPVTLFARPNYMPQQTQQTNGNGTVLLAGPSNAAALFCSPGAGQMFLSPQTQALLSGTTVAALQNAPHPQSPGGMSQVLPTSPVVKPLNMVMPNMPQNTPKTLPLTMTVPRLPPPQQGPQVLLPPGVQVNLPGEMGVHSPFLVTQGLQLNQSVPRAPLITSQSVRFIPTGNKVNGVPTYTLAPVQVTVPVHGGPPQMVLAQNQISQPPNSAVVTPGLMPPVQRAMNKNSRPNELAVQAPFLKKHDNQTVKCLRCKILLTEQGIFQHLLHGLKCLFCPQMFYSFKQIMEHSKKEHSLKVKDNRLYIKEQFSLDCDDEGNLIFSTFNLNTDVPKDLLDNRELNLALVTSTKDKIYIKMYPDKAEYTTMLKSAPNACPFCQVKLQNPEDYELHLQTKHHIVPTIHAILKTPAYKCIYCFGVYTEKSTPKTISIHVQRCRCAPKAVKEAERKLNPDTSESHDGDVCSSVQMPASEVTFQGAPEFPKPKKEAVTPRNRRRNTKASKTGTLVPETPVTLVLEPMGMERTSFEDRKDFLSQYFHRKPYVTKTEIELLASRLWINKADVKAHFNSKLTKCLKAIQKKRVCVRLGFKMIEVNKLKHNLFIPEVKPVKRKDPNEVNLSSLVPGVTVKTEQVDATTQHPLFIPEVPVTIKKEEEVCEIDHGFIIQEVTVKQEEVDEMEDALCTNG
Protein: B9 domain-containing protein 1 (Q388F8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
Interaction partners:
- B9 domain-containing protein 2
- C2 domain-containing protein
- Meckelin
- Transmembrane protein
- FAM86 N-terminal domain-containing protein
- Tectonic domain-containing protein
- Complex 1 LYR protein domain-containing protein
Sequence:
MEESVYKPLGSDRQYIEYPPKETDEESDDGLGERTFRNLHYEQLRANPRQPPRLDPFPSSRSTAFPSRSAGFDIIVQGVLEGAECHEADVLFARTYWVYGPDWTTHNSLSGGDTRLGEVPLVRSLGQQCQSEVVTQLSVVSADPFSRFTWSAPFECSLQSTNPHGWPQLVVTLHTVKGAIPQRSKASEDQTSGSRSGEQCVSYSRCFIPMQNGMHRKRLPLLQLRPSTTKQSFISWLTGQRPELRDPMFLCTGEDRCVLTAAPLTGHVSLTLSVTISGLRECGIGT
Protein: Histone H5 (P02259)
Organism: Gallus gallus (Chicken)
Function: Histone H5 performs the same function as H1, being necessary for the condensation of nucleosome chains into higher order structures, and replaces histone H1 in certain cells.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
Sequence:
MTESLVLSPAPAKPKRVKASRRSASHPTYSEMIAAAIRAEKSRGGSSRQSIQKYIKSHYKVGHNADLQIKLSIRRLLAAGVLKQTKGVGASGSFRLAKSDKAKRSPGKKKKAVRRSTSPKKAARPRKARSPAKKPKATARKARKKSRASPKKAKKPKTVKAKSRKASKAKKVKRSKPRAKSGARKSPKKK
Protein: Earthbound 1 (GH13810p) (Q9W0N9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00320}.
Interaction partners:
- IP10578p
- Dorsal interacting protein 4
- DNA-binding protein Ewg
Sequence:
MRIREKRKLQRELRVEKRVEREKKEHKEASKTQDNNNKAKATDTEVLTPAPAPAPAPPAAPTSTASPTPTSTHTPSLPAAEKVAFDNRIKRKNVLALNEKVAALREYDRLPVYKHVGRLFNCSPDQIKRIVQQRAEILNAWDQRTRRSQDAKTMETKTVRVSMLGKAVYDWIRRMMYYKDFSISDGLIQKMALQFKSSMNLAHFFPHQEWCDKFRRTYSIQHSDTRLLKIGYTQGYSVQIKDIVKDVMSESMPESGPRNGEEDDEEVSLGSPVSSHPRSYVEDEDDEVDVDGGGISGEDDLEEEPDVKPSLSELNFARALKPLPPLVRLPLQANTPPGTTQKVLLATPIVPTQAGGQPMTMTIIPLATLAQSITKIPAPQQQDKGPVVPPPKLEIKQEKEIKVEPKDPEELLAKQPEAELQENDDRAQREKDLEIPPTVHIKVEPEAELESELDQDPADLDEDANNGRSSVTSLAEVLAANVEDEMEYIEQMRQRKVSSPAAVENSLNPRQGTKRRYESAQDDNNNGGSGQESGSSVISCADARKYLKLLEEFALYKENYRLIELITRADEVMREMDDNVP