wanglab/gogpt-training-data huggingface dataset:
Protein: N-acetylgalactosaminyltransferase 7 (EC 2.4.1.41) (Protein-UDP acetylgalactosaminyltransferase 7) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7) (pp-GaNTase 7) (dGalNAc-T2) (Q8MV48)
Organism: Drosophila melanogaster (Fruit fly)
Function: Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. Prefers the monoglycosylated Muc5AC-3 as substrate. Might have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Polypeptide N-acetylgalactosaminyltransferase 5
Sequence:
MRVSTIRSGRICRLALCLLVLLPLLYLLANWSDHHKRVQEAYHTRFGGPKFAHQRLEGRPREVPKLVDGLGNFEPKDVKPRSGPGENGEAHSLSPDKKHMSDASEMEYGMNIACSDEISMHRSVRDTRLEECRHWDYPFDLPRTSVIIVFHNEGFSVLMRTVHSVIDRSPTHMLHEIILVDDFSDKENLRSQLDEYVLQFKGLVKVIRNKEREGLIRTRSRGAMEATGEVIVFLDAHCEVNTNWLPPLLAPIYRDRTVMTVPIIDGIDHKNFEYRPVYGTDNHFRGIFEWGMLYKENEVPRREQRRRAHNSEPYRSPTHAGGLFAINREYFLELGAYDPGLLVWGGENFELSFKIWQCGGSIEWVPCSRVGHVYRGFMPYNFGKLASKKKGPLITINYKRVIETWFDDTHKEYFYTREPLARYLDMGDISEQLALKKRLNCKSFQWFMDHIAYDVYDKFPGLPANLHWGELRSVASDGCLDSMGHQPPAIMGLTYCHGGGNNQLVRLNAAGQLGVGERCVEADRQGIKLAVCRLGTVDGPWQYNEHTKHLMHRVHKKCMALHPATQQLSLGHCDVNDSYQQWWFKEIRPRW
Protein: Lipase maturation factor 1 (Transmembrane protein 112) (Q96S06)
Organism: Homo sapiens (Human)
Function: Involved in the maturation of specific proteins in the endoplasmic reticulum. Required for maturation and transport of active lipoprotein lipase (LPL) through the secretory pathway. Each LMF1 molecule chaperones 50 or more molecules of LPL.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24909692}; Multi-pass membrane protein {ECO:0000269|PubMed:24909692}.
Interaction partners:
- Hepatic triacylglycerol lipase
- Lipoprotein lipase
- Apolipoprotein C-II
- Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
- Apolipoprotein A-V
Sequence:
MRPDSPTMAAPAESLRRRKTGYSDPEPESPPAPGRGPAGSPAHLHTGTFWLTRIVLLKALAFVYFVAFLVAFHQNKQLIGDRGLLPCRVFLKNFQQYFQDRTSWEVFSYMPTILWLMDWSDMNSNLDLLALLGLGISSFVLITGCANMLLMAALWGLYMSLVNVGHVWYSFGWESQLLETGFLGIFLCPLWTLSRLPQHTPTSRIVLWGFRWLIFRIMLGAGLIKIRGDRCWRDLTCMDFHYETQPMPNPVAYYLHHSPWWFHRFETLSNHFIELLVPFFLFLGRRACIIHGVLQILFQAVLIVSGNLSFLNWLTMVPSLACFDDATLGFLFPSGPGSLKDRVLQMQRDIRGARPEPRFGSVVRRAANVSLGVLLAWLSVPVVLNLLSSRQVMNTHFNSLHIVNTYGAFGSITKERAEVILQGTASSNASAPDAMWEDYEFKCKPGDPSRRPCLISPYHYRLDWLMWFAAFQTYEHNDWIIHLAGKLLASDAEALSLLAHNPFAGRPPPRWVRGEHYRYKFSRPGGRHAAEGKWWVRKRIGAYFPPLSLEELRPYFRDRGWPLPGPL
Protein: Beta-D-xylosidase 3 (AtBXL3) (EC 3.2.1.-) (Alpha-L-arabinofuranosidase) (EC 3.2.1.55) (Q9LXD6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the hydrolysis of arabinan. Can hydrolyze (1,3)-alpha-, (1,2)-alpha-linked side group residues and non-reducing terminal L-arabinofuranose residues of debranched (1,5)-alpha-L-arabinan backbone. Acts also as a beta-D-xylosidase, releasing D-xylose from arabinoxylan and xylan.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- Cellulose synthase-like protein D5
- Putative alpha-xylosidase 2
- Glucuronokinase 1
- Probable glucuronokinase 2
- Aldo-keto reductase family 4 member C10
- GDSL esterase/lipase EXL2
- GDSL esterase/lipase At4g16230
- Xylulose kinase 2
- Putative mannan endo-1,4-beta-mannosidase P
Sequence:
MASRNRALFSVSTLFLCFIVCISEQSNNQSSPVFACDVTGNPSLAGLRFCNAGLSIKARVTDLVGRLTLEEKIGFLTSKAIGVSRLGIPSYKWWSEALHGVSNVGGGSRFTGQVPGATSFPQVILTAASFNVSLFQAIGKVVSTEARAMYNVGSAGLTFWSPNVNIFRDPRWGRGQETPGEDPTLSSKYAVAYVKGLQETDGGDPNRLKVAACCKHYTAYDIDNWRNVNRLTFNAVVNQQDLADTFQPPFKSCVVDGHVASVMCSYNQVNGKPTCADPDLLSGVIRGQWQLNGYIVSDCDSVDVLFRKQHYAKTPEEAVAKSLLAGLDLNCDHFNGQHAMGAVKAGLVNETAIDKAISNNFATLMRLGFFDGDPKKQLYGGLGPKDVCTADNQELARDGARQGIVLLKNSAGSLPLSPSAIKTLAVIGPNANATETMIGNYHGVPCKYTTPLQGLAETVSSTYQLGCNVACVDADIGSAVDLAASADAVVLVVGADQSIEREGHDRVDLYLPGKQQELVTRVAMAARGPVVLVIMSGGGFDITFAKNDKKITSIMWVGYPGEAGGLAIADVIFGRHNPSGNLPMTWYPQSYVEKVPMSNMNMRPDKSKGYPGRSYRFYTGETVYAFADALTYTKFDHQLIKAPRLVSLSLDENHPCRSSECQSLDAIGPHCENAVEGGSDFEVHLNVKNTGDRAGSHTVFLFTTSPQVHGSPIKQLLGFEKIRLGKSEEAVVRFNVNVCKDLSVVDETGKRKIALGHHLLHVGSLKHSLNISV
Protein: Small ribosomal subunit protein mS39 (28S ribosomal protein S39, mitochondrial) (MRP-S39) (Pentatricopeptide repeat domain-containing protein 3, mitochondrial) (Q14C51)
Organism: Mus musculus (Mouse)
Function: Mitochondrial RNA-binding protein that has a role in mitochondrial translation.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS11m
Sequence:
MAAAAVAARRLSFRSGLVLLQTTRGTGVCEPKVCCRFYAGTESLPKVEGSDITGIEEIVIPKKKTWDKVAVLQALASTVNRDPTAAPYVFHDDPYLIPTSALESRSFLLAKKSGETAAKFIINSYPKYFQKDIAEPHIPCLMPEYFEPQIEDVSEAALEERIRLRKVRASVDMFDQLLQAGTTVSLETTNSLLDLLCYYGDQEPPADYPFQQTEHLENLEEAAEENNQTSKMESGPWKAQNNAERIFALMPEKNARSYCTMIRGMVKHRAYAQALNVYTELLNNRLSADVYTFNALIEAKTFILNEKFEEKWNDILDLLKHMVAQKVKPNLQTFNTILKGLRKCYSLGRIPALQILREMKHIGIEPSLATYHHIIHLFYPRDLSAIKMPSLIIYDIMNELEGRTFSPQDLDDGRFFQLAMSVCSSLRDLELAYQVHRLLNTGDNRKLVGHDPLRKVYYSKFFSLICSLEQIDVTLKWYKDLIPSVFLPHYQIFIGLLQALDVANRLELVPQIWKDSKEYSHTFRDALREEVLMLMARDKHPPELQVAFADCAADIKSTYEDQSARQPAFDWPANPLQYIAVLFLRGGRSQEAWKMLELFKKHKKIPRNELLEEFMDTAKASGSTALAIEVVKLASAFSLPIGESLAQRVVMDFTVDPEQKEALGNLTELNSSDGESSSDSDSDDK
Protein: Peroxisomal targeting signal 1 receptor (PTS1-BP) (Peroxin-5) (Peroxisomal C-terminal targeting signal import receptor) (Peroxisome receptor 1) (J3KPV0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Peroxisome matrix {ECO:0000256|ARBA:ARBA00004253}.
Interaction partners:
Sequence:
MAMRELVEAECGGANPLMKLAGHFTQDKALRQEGLRPGPWPPGAPASEAVSVLEVESPGAASEAASKPLGVASEDELVAEFLQDQNAPLVSRAPQTFKMDDLLAEMQQIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVTQDYNETDWSQEFISEVTDPLSVSPARWAEEYLEQSEEKLWLGEPEGTATDRWYDEYHPEEDLQHTASDFVAKVDDPKLANSEGTSDAWVDQFTRPVNTSALDMEFERAKSAIELQAELEEMAKRDAEAHPWLSDYDDLTSATYDKGYQFEEENPLRDHPQPFEEGLRRLQEGDLPNAVLLFEAAVQQDPKHMEAWQYLGTTQAENEQELLAISALRRCLELKPDNQTALMALAVSFTNESLQRQACETLRDWLRYTPAYAHLV
Protein: Potassium voltage-gated channel subfamily KQT member 1 (IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1) (KQT-like 1) (Voltage-gated potassium channel subunit Kv7.1) (A0A286YA22)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004187}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}.
Interaction partners:
Sequence:
MTSPAHSTATEASWTAGAADLQMTEALHLRNDGVRFPSSVPVDPAVITQHPPSHLHPRMSVYSATRPTLSRSFLQGRVYNFLERPTGWKCFVYHFTVFLIVLSCLILSVLSTIDEYQALANKTLFWMELVLVMFFGVEYVVRLWSAGCRSKYVGILGRLRFARKPISVIDLIVVVASIIVLAFGSNGQVFATSAVRGVRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVDDHGNSGFGSYADALWWGVVTVTTIGYGDKVPQTWIGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQASWRCFALLNPDSATYKLFVKRNLSSSGSSPKLKVKMRRKMKISDRNNGQNSPAVPSITYDSFDDGRDSRQETLTSLQQSERAPSWNSLSSFQFSTPPATKPGVFEVSSRPTLQRSSSIADDMETEPEREIVLIPVAHVSQLRDSHRAAIRVIQRMYYFVARKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDHSLGKQSLFQTSSERLKDKGTNTIGSRLNRMDEKITHMDRTLNSIAESLNLMLARERRGDLARGKEQRSTMRRQSATFSLSVLDSSEQLSTTTAIHEDS
Protein: Probable ADP-ribosylation factor-binding protein C25H2.16c (P87157)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May play a role in the regulation of membrane traffic through the trans-Golgi network.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cell fusion protein cfr1
- Polyubiquitin
- ENTH domain-containing protein C794.11c
- AP-1 complex subunit mu-1
Sequence:
MSSAKRRLYSLIQNATEPYAFEPDLAVNLDIADLINQTGGNLPREAAFAIVRKVNDRNPTVAYLALNLLDICVKNCGYAFRLQIASKEFLNELVRRFPERPPSRLNKIQVMILSLIEEWRKTICRVDRYKEDLGFIRDMHRLLSYKGYTFPEIDKENLAVLSQKSVLKTAEELEKEDREAMSAKLQELIRRGTPADLAEANKLMKVMAGYDTEQKQKYKEHVLVDLEKVKRKAALFGEMLNEVSESDKLASGDLYDELAYSLKAAQRKVDKILEEMSPEDDSYVTVSDLKSLIASLLTQYDHLLEGDFSSARTVAADNNSLLQATTESAKSNSKTSANASNTQSAMDLLIDLDIGSDAQSPSLPASSSQMPTSSFNMESLSQSLLGTVEAPAEVGAISLTESFNSPVSNSSPNVPINNFTSTCAFENSHLNFQITPKSKTRDQVVLLATYTNLSPYDTVENLQSFIAVPKKYNLVLQPQSGTNLSPLQKDGIYQEMIVTKLLDVTELPVRFKLTYKVNGRSQEYTGQSSIRLL
Protein: Transcription factor bHLH145 (Basic helix-loop-helix protein 145) (AtbHLH145) (bHLH 145) (Transcription factor EN 131) (bHLH transcription factor bHLH145) (Q9FGB0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Protein HIRA
- Pentatricopeptide repeat-containing protein At1g07590
- Protein LIGHT-DEPENDENT SHORT HYPOCOTYLS 10
- Heavy metal-associated isoprenylated plant protein 16
- Metallothionein-like protein 1A
- UDP-glycosyltransferase 85A3
Sequence:
MGQDRGFGFPTQRLCSLSSLALSHLGKQDLNLVSKTCGDTTDMFSTRGSYQVSTQVSQSYFDGYCGWVHGSSHLQQQFLPPQNQCMKQVPLQVDGVISKAEEQCSQKRFLVFDQSGDQTTLLLASDIRKSFETLKQHACPDMKEELQRSNKDLFVCHGMQGNSEPDLKEDSEELNALLYSEDESGYCSEEDEVTSADHSPSIVVSGREDQKTFLGSYGQPLNAKKRKILETSNESMRDAESSCGSCDNTRISFLKRSKLSSNKIGEEKIFETVSLLRSVVPGEELVDPILVIDRAIDYLKSLKMEAKNREA
Protein: SIGLEC family-like protein 1 (Q8N7X8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLPLLQLVPAKLLNSSCSLEKTLQCSCSFHGIPTPSVQWWMGGVPVGVDGMDGSLQVTSTMLGPWANSTISLTEEPEMGMRLLCEGKNQNGTHALSILLMSRKSSLAAQAFVKGLIQGAIYAGIVIALLFLCLLPLIVKHIRKKQAKKAAAIRAKKSSKVRASQELEMSLKPEEPGKPVVATFSESRILEKQDKRAS
Protein: Aspartyl-tRNA synthetase 2, mitochondrial (A0A3B3ITS3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYFPSWLSQLYRGLSRPIRRTTQPIWGSLYRSLLQSSQRRIPEFSSFVVRTNTCGELRSSHLGQEVTLCGWIQYRRQNTFLVLRDFDGLVQVIIPQDESAASVKKILCEAPVESVVQVSGTVISRPAGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKNFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNLHGFVDIETPTLFKRTPGGAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSWPNDKDPVVVPFPTMTFAEVLATYGTDKPDTRFGMKIIDISDVFRNTEIGFLQDALSKPHGTVKAICIPEGAKYLKRKDIESIRNFAADHFNQEILPVFLNANRNWNSPVANFIMESQRLELIRLMETQEEDVVLLTAGEHNKAKKFQSSASKLNVIPRLPFPYNSKMKKAIYFQILL
Protein: RWD domain-containing protein 3 (RWD domain-containing sumoylation enhancer) (RSUME) (Q9Y3V2)
Organism: Homo sapiens (Human)
Function: Enhancer of SUMO conjugation. Via its interaction with UBE2I/UBC9, increases SUMO conjugation to proteins by promoting the binding of E1 and E2 enzymes, thioester linkage between SUMO and UBE2I/UBC9 and transfer of SUMO to specific target proteins which include HIF1A, PIAS, NFKBIA, NR3C1 and TOP1. Isoform 1 and isoform 2 positively regulate the NF-kappa-B signaling pathway by enhancing the sumoylation of NF-kappa-B inhibitor alpha (NFKBIA), promoting its stabilization which consequently leads to an increased inhibition of NF-kappa-B transcriptional activity. Isoform 1 and isoform 2 negatively regulate the hypoxia-inducible factor-1 alpha (HIF1A) signaling pathway by increasing the sumoylation of HIF1A, promoting its stabilization, transcriptional activity and the expression of its target gene VEGFA during hypoxia. Isoform 2 promotes the sumoylation and transcriptional activity of the glucocorticoid receptor NR3C1 and enhances the interaction of SUMO1 and NR3C1 with UBE2I/UBC9. Has no effect on ubiquitination.
Subcellular location: Nucleus {ECO:0000269|PubMed:17956732}. Cytoplasm {ECO:0000269|PubMed:17956732}. Note=Colocalizes with UBC9/UBE2I in nuclear spots. {ECO:0000269|PubMed:17956732}.
Interaction partners:
- SUMO-conjugating enzyme UBC9
- Small ubiquitin-related modifier 1
Sequence:
MAEPVQEELSVLAAIFCRPHEWEVLSRSETDGTVFRIHTKAEGFMDVDIPLELVFHLPVNYPSCLPGISINSEQLTRAQCVTVKENLLEQAESLLSEPMVHELVLWIQQNLRHILSQPETGSGSEKCTFSTSTTMDDGLWITLLHLDHMRAKTKYVKIVEKWASDLRLTGRLMFMGKIILILLQGDRNNLKEYLILQKTSKVDVDSSGKKCKEKMISVLFETKVQTEHKRFLAFEVKEYSALDELQKEFETAGLKKLFSEFVLALVK
Protein: Extended synaptotagmin-3 (E-Syt3) (Chr3Syt) (A0FGR9)
Organism: Homo sapiens (Human)
Function: Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:29469807}; Peripheral membrane protein {ECO:0000269|PubMed:17360437}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:29469807}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS) (PubMed:29469807, PubMed:30220461). Recruited to the cell membrane via the third C2 domain. {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:29469807, ECO:0000269|PubMed:30220461}.
Interaction partners:
- Extended synaptotagmin-1
- Extended synaptotagmin-2
Sequence:
MRAEEPCAPGAPSALGAQRTPGPELRLSSQLLPELCTFVVRVLFYLGPVYLAGYLGLSITWLLLGALLWMWWRRNRRGKLGRLAAAFEFLDNEREFISRELRGQHLPAWIHFPDVERVEWANKIISQTWPYLSMIMESKFREKLEPKIREKSIHLRTFTFTKLYFGQKCPRVNGVKAHTNTCNRRRVTVDLQICYIGDCEISVELQKIQAGVNGIQLQGTLRVILEPLLVDKPFVGAVTVFFLQKPHLQINWTGLTNLLDAPGINDVSDSLLEDLIATHLVLPNRVTVPVKKGLDLTNLRFPLPCGVIRVHLLEAEQLAQKDNFLGLRGKSDPYAKVSIGLQHFRSRTIYRNLNPTWNEVFEFMVYEVPGQDLEVDLYDEDTDRDDFLGSLQICLGDVMTNRVVDEWFVLNDTTSGRLHLRLEWLSLLTDQEVLTEDHGGLSTAILVVFLESACNLPRNPFDYLNGEYRAKKLSRFARNKVSKDPSSYVKLSVGKKTHTSKTCPHNKDPVWSQVFSFFVHNVATERLHLKVLDDDQECALGMLEVPLCQILPYADLTLEQRFQLDHSGLDSLISMRLVLRFLQVEERELGSPYTGPEALKKGPLLIKKVATNQGPKAQPQEEGPTDLPCPPDPASDTKDVSRSTTTTTSATTVATEPTSQETGPEPKGKDSAKRFCEPIGEKKSPATIFLTVPGPHSPGPIKSPRPMKCPASPFAWPPKRLAPSMSSLNSLASSCFDLADISLNIEGGDLRRRQLGEIQLTVRYVCLRRCLSVLINGCRNLTPCTSSGADPYVRVYLLPERKWACRKKTSVKRKTLEPLFDETFEFFVPMEEVKKRSLDVAVKNSRPLGSHRRKELGKVLIDLSKEDLIKGFSQWYELTPNGQPRS
Protein: Transmembrane channel-like protein (A4FUA6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU310713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU310713}.
Interaction partners:
Sequence:
VEWSGECLRSCRREVQIKVEEKEDETEESSSEEEEEVEDKLPRRESLRPKRKRTRDVINEDDPEPEPEDEETRKAREKERRRRLKRGAEAKKFVSENEGALGKGKGKRWFAFKMMMAKKWAKFLRDFENFKAACVPWENKIKAIESQFGSSVASYFLFLRWMYGVNMVLFILTFSLIMLPEYLWGLPYGSLPRKTVPRAEEASAANFGVLYDFNGLAQYSVLFYGYYDNKRTIGWMNFRLPLSYFLVGIMCIGYSFLVVLKAMTKNIGDDGGGDDNTFNFSWKVFTSWDYLIGNPETADNKFNSITMNFKEAITEEKAAQVEENVHLIRFLRFLANFFVFLTLGGSGYLIFWAVKRSQEFAQQDPDTLGWWEKNEMNMVMSLLGMFCPTLFDLFAELEDYHPLIALKWLLGRIFALLLGNLYVFILALMDEINNKIEEEKLVKANITLWEANMIKAYNASFSENSTGPPFFVHPADVPRGPCWETMVGQEFVRLTVSDVLTTYVTILIGDFLRACFVRFCNYCWCWDLEYGYPSYTEFDISGNVLALIFNQGMIWMGSFFAPSLPGINILRLHTSMYFQCWAVMCCNVPEARVFKASRSNNFYLGMLLLILFLSTMPVLYMIVSLPPSFDCGPFSGKNRMFEVIGETLEHDFPSWMAKILRQLSNPGLVIAVILVMVLAIYYLNATAKGQKAANLDLKKKMKMLQLLVASNKYPESPEKVHFALLFKSNAICERPENKHC
Protein: Chitin synthase 4 (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase 4) (Class-V chitin synthase 4) (J9VF17)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer. Produces a large proportion of the chitin that is not deacetylated to chitosan.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPPTSSQAPFHRYSHLDQRSAPDTQESSPADGNHDPRRQSTSFDHPNLYAQRDVFAVPNHPQSTNLNHQPYLHQGRSGSFEEPIYETPQPGHNVGYEDAEPYGHEQHDGTMWSERPSYSAPYDSDIKAPLDPTPYTPDLEADGMVVKEKKVHATEVMATTNARRWWIRITWMMTWWIPSFLLVHLGRMKRADVRMAWREKLAIFMMICLACAVVLFYIIFFGKLLCPDSDKAWNEKELATHQGDDDYYAAIAGKVYDFTNFYKAQHSDLSSYTTSSALMLEFAGQDLTNYFPMPMTVACPNLVTSTDLTLMYSNFTPIVQYAVHTSGPLQTGTDTKLNDINWYTDTLNPALEDYYKGYYVYDKSSIASGADSDSKYWAIYNNKVYDLSNYIYTISYYSSSSGTDLPNYSFLNSDITDLFQTSAGQDITKDMDEKLSALTAEDAANQMTCLNNAFYLGELDFRKTPRCTVQNYLLLAFSIILIATIASKFLAALQLGSKRQPELLDKFVICQVPCYTEGEESLKRTIDSLAALNYDDKRKLIFIICDGNIVGSGNNRPTPRIVLDLLGVDDKLEAEPLLFKSIGEGSKQLNYGKVYSGLYEFEGHVVPYIVVVKVGKPSEISKPGNRGKRDSQVLLMQYLNRVHFDAPMTPLELEIYHQMRNVIGIDPAFYEYIFQVDADTSVTPDSLNRLIACTADDQQIIGICGETKLANENESLTTMIQVYEYYISHHLTKAFESLFGSVTCLPGCFSVYRIRTAEGGRPVIISSVVIDEYAEPNVDTLHKKNLFSLGEDRYLTTLMMKNFPTFKMKFTPDAIAHTVAPSKWSVLLSQRRRWINSTIHNLVELLFLPEMCGFCFFSMRWVVFLDLLGTIILPATCGYLIYLVIVVSTGKAAIPVISLAMIGATYGLQALIFILKREFMLIGWMLVYILAFPVWSVFLPIYSFWSMDDFSWGNTRKVIGEGNQKTVVIDDDEPFNEGMIPYRTFKEYEWNAWEAASLHSESPAPSEKSQRTTRTGQSYRPHPHSIRSPSFHSSASELPSKADYWRDSSPLGMGNESKRLHQVSSDPSMRGDKSFIRGSKPQVERVQSMAGMSMWGSGSVYDPYKQAMGGPGFLHPMMTGNSLASQATFYPPQTQYPMSMYGSPMMMPMGMPMMGLQYAGNASMAGGAAGPRGTMMTMGMGDQSRISSFSMGGPVAESGAGRLVGLSINEEKEVQDEEVLDKLKTWLSKQDLMSVTKRQTREAIYTLFPNAGLQNRAGWLNEQIDKILSES
Protein: BCL6 corepressor (H7C2V9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLSATPLYGNVHSWMNSERVRMCGASEDRKILVNDGDASKARLELREENPLNHNVVDASTAHRIDGLAALSMDRTGLIREGLRVPGNIVYSSLCGLGSEKGREAATSTLGGLGFSSERNPEMQFKPNTPETVEASAVSGKPPNGFSAIYKTPPGIQKSAVATAEALGLDRPASDKQSPLNINGASYLRLPWVNPYMEGATPAIYPFLDSPNKYSLNMYKALLPQQSYSLAQPLYSPVCTNGERFLYLPPPHYVGPHIPSSLASPMRLSTPSASPAIPPLVHCADKSLPWKMGVSPGNPVDSHAYPHIQNSKQPRVPSAKAVTSGLPGDTALLLPPSPRPSPRVHLPTQPAADTYSEFHKHYARISTSPSVALSKPYMTVSSEFPAARLSNGKYPKAPEGGEGAQPVPGHARKTAVQDRKDGSSPPLLEKQTVTKDVTDKPLDLSSKVVDVDASKADHMKKMAPTVLVHSRAGSGLVLSGSEIPKETLSPPGNGCAIYRSEIISTAPSSWVVPGPSPNEENNGKSMSLKNKALDWAIPQQRSSSCPRMGGTDAVITNVSGSVSSAGRPASASPAPNANADGTKTSRSSVETTPSVIQHVGQPPATPAKHSSSTSSKGAKASNPEPSFKANENGLPPSSIFLSPNEAFRSPPIPYPRSYLPYPAPEGIAVSPLSLHGKGPVYPHPVLLPNGSLFPGHLAPKPGLPYGLPTGRPEFVTYQDALGLGMVHPMLIPHTPIEITKEEKPERRSRSHERARYEDPTLRNRFSEILETSSTKLHPDVPTDKNLKPNPNWNQGKTVVKSDKLVYVDLLREEPDAKTDTNVSKPSFAAESVGQSAEPPKPSVEPALQQHRDFIALREELGRISDFHETYTFKQPVFTVSKDSVLAGTNKENLGLPVSTPFLEPPLGSDGPAVTFGKTQEDPKPFCVGSAPPSVDVTPTYTKDGADEAESNDGKVLKPKPSKLAKRIANSAGYVGDRFKCVTTELYADSSQLSREQRALQMEGLQEDSILCLPAAYCERAMMRFSELEMKEREGGHPATKDSEMCKFSPADWERLKGNQDKKPKSVTLEEAIAEQNESERCEYSVGNKHRDPFEAPEDKDLPVEKYFVERQPVSEPPADQVASDMPHSPTLRVDRKRKVSGDSSHTETTAEEVPEDPLLKAKRRRVSKGLHPKKQRHLLHLRERWEQQVSAADGKPGRQSRKEVTQATQPEAIPQGTNITEEKPGRKRAEAKGNRSWSEESLKPSDNEQGLPVFSGSPPMKSLSSTSAGGKKQAQPSCAPASRPPAKQQKIKENQKTDVLCADEEEDCQAASLLQKYTDNSEKPSGKRLCKTKHLIPQESRRGLPLTGEYYVENADGKVTVRRFRKRPEPSSDYDLSPAKQEPKPFDRLQQLLPASQSTQLPCSSSPQETTQSRPMPPEARRLIVNKNAGETLLQRAARLGYEEVVLYCLENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKMTHSELMEKFLTDYLNDLQGRNDDDASGTWDFYGSSVCEPDDESGYDVLANPPGPEDQDDDDDAYSDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDLEAFNPERSPLK
Protein: PPIase cyclophilin-type domain-containing protein (Q4GZ47)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCDLFSSSSVFSFCSSAFERFSMQATLGFAFPHPQRKQQVYEISITVFVPAPETRPRTVANFYYMCTGELPPTYPTYGAVVGNNNTVCGALPSLEAIKSNASLKPFEGSAVVRIEKGVVLEIGSSTTKTIFGGFTEDESSPLAKESASVGASKAAAGRQSVSASMQELRAGTLLIGNMGIPNSNGSRYYILLQDASVNERKAEFSPYKPLGFVISGMEALQAACASVAVHPRTLVPTQKVKMLVSEVHFRRSVMQPAEAMAKQRLANIAPTAGRTRCRDEFEGSEIAKEGLDSNTSVFFDHTRKFPLWGNESHGGANGESGGNLPQAKRPRTERVVSNDDGSVSLRKTAVEGPAGEPFDYMAAQEAVFLNDIDLIAETQAVRHRRRAKRQQKKRKHAGSGQSKSAGADNSKKGKHAVPPSGGGKVLRRRY
Protein: Myosin regulatory light chain 1 (Q9UUG5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm.
Interaction partners:
- Myosin type-2 heavy chain 1
- Myosin type-2 heavy chain 2
- Ras GTPase-activating-like protein rng2
- Cell division control protein 15
- Actin
- Cell division control protein 12
- Myosin regulatory light chain cdc4
- Anillin-related medial ring protein mid1
- Tropomyosin
- LIM domain-containing protein C4F6.12
Sequence:
MFSSKENSLGAKRAPFSSNTTSSQRVAAQAAKRASSGAFAQLTSSQIQELKEAFALLDKDGDGNIGREDVKTMLTSLNQDASEDSINHMFESINPPINLAAFLTAMGSMLCRISPRNDLLEAFSTFDDTQSGKIPISTMRDALSSMGDRMDPQEVESILRSYTSHGVFYYEKFVDAIAGSKDSN
Protein: GH05923p (Regulator of eph expression, isoform B) (Q8MRQ2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- MIP26555p1
- Serine/threonine-protein kinase minibrain
- DDB1- and CUL4-associated factor 7
Sequence:
MIKFVRQKNRENTLRESKNFMRKKRESNDSGTESDGELLDVENQRHLDVDMETSVAGQKPIASAMMCHQQTSSSCAHLMYDQHSSEEELEVINGPSSQAGQHPGTAATGSSCASRISNRGCTSSLDTEAPYEERATTSNSKRSSSTLMVENRKRSLAHSSDDELRNSLEPILTPVNFRTSPPLEAFKPNRSHMMFRSTTPLILSEARCGIENIKLCDNSVNEENGDNGGGGGAANSSKCAKIGALAGNASGTVAATGNGNGGNENEPSVIKACSSSLKMSNSSHHIYQPQPKYSFHYNSSRSSPASTTGLDMEVRSVSPPAKLFHCAISPRRRPSNNASGAAGGATTISPSSASSSSGTTTTHNAANSAGNAANVTAVATQRLQRPHRPCLDFDKMQQVSL
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (E9PKY5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNESELFGRTIRVNLAKPMRIKEGSSRPVWSDDDWLKKFSGKTLEENKEEEGSEPPKAETQEGEPIAKKARSNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEVTEGLDVLRQIE
Protein: Beta-carbonic anhydrase 1 (Beta-CA 1) (EC 4.2.1.1) (Carbonate dehydratase 1) (mtCA 1) (P9WPJ7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reversible hydration of carbon dioxide to form bicarbonate.
Interaction partners:
- Carbonic anhydrase 2
- carbonic anhydrase
- Oligopeptide transport system permease protein OppC
- Oligopeptide-binding protein OppA
- Oligopeptide transport system permease protein OppB
Sequence:
MTVTDDYLANNVDYASGFKGPLPMPPSKHIAIVACMDARLDVYRMLGIKEGEAHVIRNAGCVVTDDVIRSLAISQRLLGTREIILLHHTDCGMLTFTDDDFKRAIQDETGIRPTWSPESYPDAVEDVRQSLRRIEVNPFVTKHTSLRGFVFDVATGKLNEVTP
Protein: SD01504p (Q86P77)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYANLTTGECVWDPPEDVPIKRTDSSQWWELFDTNTQRFYYYNAATQKTVWHRPSKCDIIPLAKLQTLKQNTDPSERREQTTPQKQQQQQVQHASQQQQHPSPMSGPNKKGRGQQRISGGNGTVASSEEKLTSSEVISSPRGRQSFRVGTGDSSRSMDMQQQHPQGYASRRSQDSCNQYKESGKSSDSSLSSAHGYRRFNDSGVPVSGHPDNLRLGSLQKQQRGGGKDNGAFEMLQESTSSHNLPHGSTSTSSSYAGGSGYGDKYFDHQLLPNHLQGYSSKSSDIASPTHSIHTPQSQKKKMSPDAAPAAQYNYAQQQHQQRSAQRSGGGAAGTGAPAGKSYGGDREYKVSLARSGSFMSSSINPAAAGHHSKSYRKSSAEAANGGAASDDSMHEKYFKSVENTPLSRRRHTTNATKSGGGASGSNTATSTAGSGSSSHKKHSSDSSPQSPISPQTKSSRQAKTSATSTVPQLQHSPRLQEPSHSLDLLSLERISLGKSGPISPGGGTENLGLLTHSSRGSNDSARQRQKSNNSSANRSQSHHYPGQSSLRHSASSSLDKRGYHVGGGSGDGRGVTGGEKRRSKQHHYQQQADNSDVEYDNGNTSPLYTNWDQEMPHLLPLKHYIIEQAKLSGRYEYRGGDGGDSDSYHSDSQSEHSLSGHEPDNEDSDGGSDTHGGYLEHNYGMIDDYANMGDSVSYYAYMYPPHDPAGREDISENVEAVLEGIGGNATEPSAPTATAPKPKPRYQISYYDTVSHSPSAGSGYHGQQLYSNTPPYSGHGHGHHVPPPSLPHQQQLHLEPSDTKQKQSQTLPSPNRQISRLAGAGHQGSGPTASSKEETGHSTVAGQQQATVGTVTPASLSRPGHKMAPPSLKPTIQQIFPPSERAPGMGNLGLGGPTLACMKECDIEKFAADNLNLHSKGIFRKKASVRDMLSWTAEAISRPMLALSRDKADKKTAIELFKLVQIYMADRKARIGMTLNSVAIEIISASLPQQQLRDELYVQLCRQTTENPKRDSLIRGWELMAICLSYVPPSPTFQPTLLNYVNRHRDPSFATCFMEVSKWPIHVQISHYATVCCRRLDRIGSSGRRMAKKPTVDEVEQARQQILRNSMFGNTLSEVMDLQKEKFPFRKLPWIQTTLSEHVLLLNGKQTEGIFRVSADVDEVGCMKNRLDRWDVPDYKNTLVDAHTPASLLKLWYRELYDPLIPDAYYEDCVNTEDPDKAKEIVNKLPEINQLVLTYLIHFLQQFAIPEVVSCTKMDSSNLAMVFAPNCLRCTSEDPKVILENARKEMSFMRTLIQHMDTTHVANLV
Protein: N-terminal EF-hand calcium binding protein 3 (U3KQF5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQWRLQVNRLQELIDQLECKAPRLEPLREEDLAKGPDLHILMAQRQVQVAEEGLQDFHRALRCYVDFTGAQSHCLHVSAQKMLDGASFTLYEFWQDEASWRRHQQSPGSKAFQRILIDHLRAPDT