wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 5A (eIF-5A) (Q6FLR2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL23
- Deoxyhypusine synthase
- L33
- Deoxyhypusine hydroxylase
- Small ribosomal subunit protein eS6
- Candida glabrata strain CBS138 chromosome M complete sequence
Sequence:
MAEEEHTFETADAGSSTTYPMQCSALRKNGFVVIKGRPCKIVDMSTSKTGKHGHAKVHLVAIDIFTGKKLEDLSPSTHNMEVPVVKRTEFQLLDIDDGFLSLMNMDGDTKDDVRHPEGELGDQMQAAFDEGKDLMVTIIAAMGEEAAISFKEAPRSD
Protein: C2H2 finger domain transcription factor crzA (Q4WJ81)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Transcription factor involved in the regulation of calcium ion homeostasis. Regulates genes encoding calcium transporters, transcription factors and genes that could be directly or indirectly involved in calcium metabolism. Supports especially pmcA, pmcB and pmcC expression encoding for calcium-translocating P-type ATPases. Binds target promoters at motif A[GT][CG]CA[AC][AG]. Plays an essential role germination, radial growth, and asexual development. Also plays a major role in proper chitin and glucan incorporation into the cell wall. Involved in the high-osmolarity glycerol response (HOG) signaling pathway. Required for pathogenicity in an experimental murine model of invasive pulmonary aspergillosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:18298443}. Cytoplasm {ECO:0000269|PubMed:18298443}. Note=Localizes predominantly to the cytosol of the cell in the absence of added calcium and translocates to the nucleus following exposure to CaCl(2). {ECO:0000269|PubMed:18298443}.
Interaction partners:
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Calmodulin
- Calmodulin, putative
- pH-response transcription factor pacC/RIM101
Sequence:
MASQEMFPELGQSPAPGVKSRGVSRSPHPHQQQQQQQHQQHQGQFTGTVTGLDLDSSIATASSFANSSFDPNSNNVSPSAESYGYTAAGYLSGTPASQTDQNYANSLQIPQSYGTGLVPQFNESRGLPIQQQSQQQHHQQPSLDDNFSDLLNSNATEYDFNTVYQTHSPSSNTAPEYDSSLLLDPQVHQQSHPTQIPSSHSSTSPQISPLEQQQHSSPGPMSTQGSTTVAYYTPQHSRHASLDPATAAFLTSNTHPDWQAVMGNSAAFQGHRRAPSEVSEISSAAPSPYLSQHESFDGVDNNPSPLLAPQNDPSLYDSALGIENFTLSEQHQQHQGFSPAHSPYISPRLMPQQGQEMMPNVPYLSGPAPNTQYPTPPNDMYGNGAEGMMNMSQGTHPSVDIGQASQMAPPSINVEFAPPSRIPSFGPSKPASNLDSLSPPPSSTRSRGRSKSDPYAHPSTSRLRSSSTSSSLDPLAPTTPRSLSPFDSFGRQQQSNPSSRDPSPSRSNRRLSTSSIDSRNYILGLADPQRPGASPNDSKRVQKHPATFQCNLCPKRFTRAYNLRSHLRTHTDERPFVCTVCGKAFARQHDRKRHEGLHSGEKKFVCQGELSRGGQWGCGRRFARADALGRHFRSEAGRICIKPLLDEESQERERSLMDQQQHHLQPLPQQVMVPVDNPHAGNFVLPAALLAQYPALQTLQWDQIAASADDPSDIGGRSSFDASSGNEFGFEDDDSGLSSVSGINAGYSAAGNFY
Protein: Protein TusC (tRNA 2-thiouridine synthesizing protein C) (P45531)
Organism: Escherichia coli (strain K12)
Function: Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Protein TusB
- Sulfurtransferase TusD
- Sulfurtransferase TusE
- Sulfur carrier protein TusA
- tRNA-specific 2-thiouridylase MnmA
- Uncharacterized protein YheO
- tRNA sulfurtransferase
- Cysteine desulfurase IscS
- Iron-sulfur cluster assembly scaffold protein IscU
Sequence:
MKRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCAASLRERGLDPQTPFVVEATPLEADALRRELANYDVILRF
Protein: S-adenosyl-L-methionine-dependent methyl transferase PigF (EC 2.1.1.-) (Q5W266)
Organism: Serratia sp. (strain ATCC 39006) (Prodigiosinella confusarubida)
Function: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to the hydroxyl group of 4-hydroxy-2,2'-bipyrrole-5-carbaldehyde (HBC) to yield 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC).
Interaction partners:
- Probable NAD
- dTTP/UTP pyrophosphatase
- L-proline--[L-prolyl-carrier protein] ligase
- Beta-ketoacyl synthase PigJ
- Aminotransferase PigE
- Probable acyl carrier protein PigG
- 4-hydroxy-2,2'-bipyrrole-5-methanol synthase PigH
- Thiamine diphosphate dependent-3-acetyloctanal synthase PigD
- RedY
- 4'-phosphopantetheinyl transferase
Sequence:
MTLTKQDAVNQMMGFFQSKTLITALSLKLFDHLRDQDRNAKQMAALLNCPLRSSEQLLIALQAMGYLEKQDGLYHLPQEHRAFLVSDEPQWLGWLGRHIDTFLYPLWGELKAAVENDTHQRQTVFGDDRSWFDILYQNPDDVTDFQEFLGKFAAPFIDGFIQDYDFSQHQAFLDIGSGIGSLPIAVANAYSGVNLAICELPQTSTFLRDKLVQQGYGQRIQVLEGDVISGDLPIGDYDLIHLGWMLHDYAPETQLIILKNIYDAMPVGGRFIASETPLNADKSGPEFTALLSLNMLVSTDGGIESSPQEYLSRFHQAGFSNARIMDISGPRTLIVGEKTTHNNGSSQC
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q4AB31)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLRKYLYIQKTNIKEENGGGPQTTTAGPSAGNVANATTALAGGKSSSNNMYSTRQSVSTTTGVLMVGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKMEPMKSKAPQLHLEYRFYKLLGSHADNAPDGIPRIYHLGTCGGRYNAMVLELLGLSLEDLFNICARKFSLKTVLMIAKQLLHRIEYVHSRHLIYRDVKPENFLIGRTSTKREKIIHIIDFGLAKEYIDLDTNRHIPYREHKSLTGTARYMSINTHMGREQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCDGHPEEFATYLRYVRRLDFFETPDYDFLRRLFQDLFDRKGYTDEGEFDWTGKTMSTPVGSLQTGHEVIISPNKDRHNVTAKTNAKGGVAAWPDVPKPGATLGNLTPADRHGSVQVVSSTNGELNPDDPTAGHSNTPITQQPEVEVVDETKCCCFFKRKKKKSTRQK
Protein: Clathrin coat assembly protein AP180 (At-AP180) (Clathrin coat-associated protein AP180) (Q9ZVN6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia promotes their assembly into 70-90 nm coats cages.
Subcellular location: Membrane, clathrin-coated pit {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Colocalized with clathrin in the Golgi area. {ECO:0000250}.
Interaction partners:
- Clathrin interactor EPSIN 1
- Clathrin interactor EPSIN 3
- ENTH/VHS family protein
- Clathrin interactor EPSIN 2
- Clathrin heavy chain 1
- AP-2 complex subunit alpha-1
- Clathrin heavy chain 2
- AP-2 complex subunit alpha-2
- DDE family endonuclease
- Dynamin
Sequence:
MPSKLKKAIGAVKDQTSISLAKVANGATGGGDLTTLEVAILKATSHDEEVPIDDRLVTEILGIISSKKSHAASCAAAIGRRIGRTRNWIVALKSLVLVLRIFQDGDPYFPREVLHAMKRGAKILNLSSFRDDSNSCPWDFTAFVRTFALYLDERLDCFLTGKLQRRYTNREQTGRISTNSTTRSRFNPKAGIKSHEPAVRDMKPVMLLDKITYWQKLLDRAIATRPTGDAKANRLVKMSLYAVMQESFDLYRDISDGLALLLDSFFHLQYQSCINAFQACVRASKQFEELNAFYDLSKSIGIGRTSEYPSIQKISLELLETLQEFLKDQSSFPASSGLYPSPNSFLPPPPSSKDSAVSSSLDFGDSTIDTSERYSDYGSFRSTSLEDLMSRTEAGTSSPPMSCHSEPYGGGRDDPNGNNFDTVSTKSLPNNPSVSASNLILDLLSLDDVSNTAEAEDVEDKKKQDDSKAETFDPWEALMLRDDPKKKIETIEEEPSTAEDHQRDSGNWLLALEETATQVQGNNSMAIVPFGLDDPMPAFQAATDQYNPFLEEPVAQLATAGEPMITFGGLALTGFQPEPTFQVNVPDDFEPSSTPTFKATETLPMKCDPFTTFESFGFGETFSENGGVNQQSVLQEQQIWLQNQKKIIAKHLS
Protein: Pebble, isoform C (Q8IQ96)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MESGEKTAKGRWKLILGPPALKYAAEMKQTLGQNSRPIYNYAMRGVVTCFTGIRKKDELTKLVNLIHSMGGCIKKDLNTKTTHLICNHSGGEKYQYAKTFRLTVVRPAWVFAAWADRNSLEFDATQENFTKTHRLKAFEGQKICFFGFPVEEHQHMVDVLLENGGVCAELDDPECSHVVVDEHTTLTKPEPKNNHTHILKSDWFWYTIQNGYANEMDYLFGDYLDSITNTPNTDRRDSLPISFNKRKRKRFSQRIQLEGTPLGSGKRRSSVSDAGLLSVSNSLFDCTTSPDKLESDKLLHAEPEASDATPAKKSMRFNHFMDFYTTESNYVGILDTILNLFKNKLEELAETNDPLLNKSEIKTIFGNFLPIHEVHQSMLEHLRKLHANWREDCLIGDIIIQHRDELIKAYPPYVNFFEQMKEQLQYCDREYPRFHAFLKINQTKPECGRQGLQDLMIRPVQRLPSISLLLNDILKHTTSGNADHGRLEEALKAIKQVTLHINEDKRRTESRMAIFDIFNDIEGCPAHLVSSNRSFILKCEVNELSDSLSGRGDSLVLYLFSDSIELCKRRSKGFNTAKSPSTAKTHKHLKLISLNTIRLVIDISDSPRAFGLLLRGDKEKLYTFTISDEETDKSVYVKKLCNQIAAHTCRTDADKLLICRTSQELEVDISDVNVSTLSKAFKLAAKTRLKVGRAFSFNKTPNKLKRAVSTMMTSPFGSTNSLTPASQLAQMRLASCTNINEVDDEDCASMRSSSPSTQSEMLVVPPLSVQPTRKNKAVVGRI
Protein: Crossover junction endonuclease EME1B (EC 3.1.22.-) (Essential meiotic endonuclease 1B) (AtEME1B) (C5H8J1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks, nicked Holliday junctions and also intact Holliday junctions with a reduced efficiency. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. Plays a role in DNA repair and in genotoxic stress-induced homologous recombination (HR) in somatic cells. Mediates a subset of meiotic recombination events that are insensitive to crossover interference.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Crossover junction endonuclease EME1A
- Crossover junction endonuclease MUS81
- Crossover junction endonuclease MUS81
- DNA repair protein REV1
- DNA repair protein XRCC4
- DEAD-box ATP-dependent RNA helicase FANCM
- Tyrosyl-DNA phosphodiesterase 1
- Replication protein A 70 kDa DNA-binding subunit E
Sequence:
MNDHILISDGEDQTTPLPSLSKRARKYPISAILISDSDPTPQKQPPESSFTPIFVPETPLSDDFSVVKCSFGSRALASNREDKFSGKRIISLDSEFEDSPRPETSKKNESVLAGLREPRFGLEAETSEAYYKNTRIPETNLDDDTSWMHEVSFRSSPTNDTIEVVSDQEKEDISVEKIGRKKKIRTTTLPVPGEALPKKRQSKEDKTSAMEEKKLRKEQERLEKAASKAEEAERKRLEKEKKKWEKGKLALKSIVAEIDTKVLEGSIGGLLLSRFSEKGITIHVGPNPIERSIVWTMTIPEDIAPLFPQGPKIPYLLLVYDAEEFCNLVANGKFLEIISRVQDRYPSYTVCCLTNKLMSYVKKREKEEYKNPGNWRRPPIDEVLAKLTTHYVKVHSRHCVDEAEVAEHIVGLTSSLASCQFRKKLTMLSVSANGALVSKDSVDKHLIKKSPWLKALVAIPKVQPRYALAVWKKYPSMKSLLKVYMDRNKSVHEKEFLLKDLKVEGLVGGDIRLGEICSKRIYRVLMSHDGAIKTDDVENGAAFFTDSPGVN
Protein: Tryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (TrpRS) (Q12109)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, mitochondrial
- Serine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Cysteine--tRNA ligase
- Leucine--tRNA ligase, mitochondrial
Sequence:
MSNDETVEKVTQQVSELKSTDVKEQVVTPWDVEGGVDEQGRAQNIDYDKLIKQFGTKPVNEETLKRFKQVTGREPHHFLRKGLFFSERDFTKILDLYEQGKPFFLYTGRGPSSDSMHLGHMIPFVFTKWLQEVFDVPLVIELTDDEKFLFKHKLTINDVKNFARENAKDIIAVGFDPKNTFIFSDLQYMGGAFYETVVRVSRQITGSTAKAVFGFNDSDCIGKFHFASIQIATAFPSSFPNVLGLPDKTPCLIPCAIDQDPYFRVCRDVADKLKYSKPALLHSRFFPALQGSTTKMSASDDTTAIFMTDTPKQIQKKINKYAFSGGQVSADLHRELGGNPDVDVAYQYLSFFKDDDVFLKECYDKYKSGELLSGEMKKLCIETLQEFVKAFQERRAQVDEETLDKFMVPHKLVWGEKERLVAPKPKTKQEKK
Protein: MHC class I alpha chain 2 (MHC class I antigen) (MHC class I glycoprotein) (MHC class I molecule) (O46789)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGPCGALGLGLLLAAVCGAAAELHTLRYIRTAMTDPGPGLPWYVDVGYVDGELFVHYNSTARRYVPRTEWIAAKADQQYWDGQTQIGQGNEQIDRENLGILQRRYNQTGGSHTVQWMYGCDILEGGPIRGYYQMAYDGRDFTAFDKGTMTFTAAVPEAVPTKRKWEEGDYAEGLKQYLEETCVEWLRRYVEYGKAELGRRERPEVRVWGKEADGILTLSCRAHGFYPRPIVVSWLKDGAVRGQDAHSGGIVPNGDGTYHTWVTIDAQPGDGDKYQCRVEHASLPQPGLYSWEPPQPNLVPIVAGVAVAIVAIAIMVGVGFIIYRRHAGKKGKGYNIAPDREGGSSSSSTGSNPAI
Protein: Small ribosomal subunit protein uS10m (40S ribosomal protein S10, mitochondrial) (P42797)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000303|PubMed:36423343}.
Interaction partners:
- Small ribosomal subunit protein uS13m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS19m
- Uncharacterized protein
- AT3g18240
- Small ribosomal subunit protein uS9m
- At1g64880
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein bS18c
- Small ribosomal subunit protein mS29
Sequence:
MIAGVLRRSSLPSRQTLSAALASFNSCISHNLTPATTGASVSSRFTLASSPNSFGIRARNIHIRSEPSMIVPAGIASQGYATVTKDRKNEIKKAKIKISPDNVRPLSRKEIALQKEAAEESTSKIKGTKICIAIRSFVNPEKQAWCLPPHTRKVAMPDTRTLYTVLRSPHVDKKSREQFEMRFKKRFLVIKAQSHELSKKLFWLKRYRILGAQYELQFHCKTRLDMTQVLGNINGSTTNAY
Protein: Probable protein phosphatase 2C 22 (AtPP2C22) (EC 3.1.3.16) (Q9SLA1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Mitogen-activated protein kinase 11
- RNA-binding
- Arabidopsis thaliana genomic DNA, chromosome 5, P1 clone:MOK16
- V-type proton ATPase subunit c''2
- PRA1 family protein F4
- 14-3-3 family protein
- 14-3-3 family protein
- Eukaryotic translation initiation factor isoform 4E
- GDSL esterase/lipase At4g10955
Sequence:
MEETRGISDPENGSSSYGGKPPNPLSFSSSSAAAAVYRQTFDGERSLAPCNKRSLVRHSSLVKTMVSDISVENEFTIEKNKSEFVPATRSGAWSDIGSRSSMEDAYLCVDNFMDSFGLLNSEAGPSAFYGVFDGHGGKHAAEFACHHIPRYIVEDQEFPSEINKVLSSAFLQTDTAFLEACSLDGSLASGTTALAAILFGRSLVVANAGDCRAVLSRQGKAIEMSRDHKPMSSKERRRIEASGGHVFDGYLNGQLNVARALGDFHMEGMKKKKDGSDCGPLIAEPELMTTKLTEEDEFLIIGCDGVWDVFMSQNAVDFARRRLQEHNDPVMCSKELVEEALKRKSADNVTAVVVCLQPQPPPNLVAPRLRVHRSFSAEGLKDLQSYLDGLGN
Protein: Endoribonuclease YbeY (EC 3.1.-.-) (P0A898)
Organism: Escherichia coli (strain K12)
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. Acts together with the RNase R to eliminate defective 70S ribosomes, but not properly matured 70S ribosomes or individual subunits, by a process mediated specifically by the 30S ribosomal subunit. Involved in the processing of 16S, 23S and 5S rRNAs, with a particularly strong effect on maturation at both the 5'- and 3'-ends of 16S rRNA as well as maturation of the 5'-end of 23S and 5S rRNAs.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00009, ECO:0000269|PubMed:20639334}.
Interaction partners:
- PhoH-like protein
- GTPase Era
- Ribonuclease R
- Magnesium and cobalt efflux protein CorC
- Protein PhoH
- Ribonuclease 3
- tRNA-2-methylthio-N
- Polyribonucleotide nucleotidyltransferase
- Glycine dehydrogenase
- Ribonuclease G
Sequence:
MSQVILDLQLACEDNSGLPEESQFQTWLNAVIPQFQEESEVTIRVVDTAESHSLNLTYRGKDKPTNVLSFPFEVPPGMEMSLLGDLVICRQVVEKEAQEQGKPLEAHWAHMVVHGSLHLLGYDHIEDDEAEEMEALETEIMLALGYEDPYIAEKE
Protein: D-arabinose 1-dehydrogenase (NAD(P)(+)) (A0A1D8PI24)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Asr2p
Sequence:
MKLATEIDFKLNNGKTIPALGLGTVASKDPKDVKDQVITAVKAGYRHIDTAWFYGTEKYIGEALQELFAEGIIKREDLFITTKFWPSYWANPEKSLDESLKDLQLDYVDLFLQHWPICLHGDENGLPKIPKDENGELIYDDDPTPNGTKYIDVYHKLEDILETTTKVRSIGVSNYSIPKLRQLLPKVKKHIPVCNQIEYHPQLPQQDLVDYCTKNNILISCYSPVGSYGAPVLKIPLVKQLAEKYQVTENEIADAYNILNGRVTLPRSSNLERIKTIIRLPDLTKEELDELYQVGVKDPQRYICDPWGYGIGFRWWKGDTLSKEFD
Protein: Stromelysin-1 (SL-1) (EC 3.4.24.17) (Matrix metalloproteinase-3) (MMP-3) (Transin-1) (P08254)
Organism: Homo sapiens (Human)
Function: Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9. Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway. Acts also intracellularly. For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage. In addition, plays a role in immune response and possesses antiviral activity against various viruses such as vesicular stomatitis virus, influenza A virus (H1N1) and human herpes virus 1. Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities.
Subcellular location: Secreted, extracellular space, extracellular matrix. Nucleus {ECO:0000269|PubMed:35940311}. Cytoplasm {ECO:0000269|PubMed:35940311}.
Interaction partners:
- Metalloproteinase inhibitor 1
- Osteopontin
- Interstitial collagenase
- Stromelysin-2
- Metalloproteinase inhibitor 2
- Matrix metalloproteinase-9
- Fibronectin
- Integrin-binding sialoprotein
- Metalloproteinase inhibitor 3
- Aggrecan core protein
Sequence:
MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC
Protein: ALG-1 (H2KY58)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein argonaute-1
- Protein argonaute-1
- ALG-1 INteracting protein
- RING-type E3 ubiquitin transferase
- ATP-dependent RNA helicase cgh-1
- Female germline-specific tumor suppressor gld-1
Sequence:
MHGYQGNDPNYRRQPPYRQLHVDTRSPSSYSQQYVPYEADPGMNGDGWQGPGRGGPHHMNGGGGGRRGGGGGMHNQRIQQNPHHGGMNRMMPHGFRPQQGQFMPQYPPPPPMGGMPDVMDINMRMDGMSLGSTPSGIPGQYGDMGPPPVQQWNQPAPFVPPPQQDDLYDPSGYGGGAGGGGGHHPSHMPPYGQRGNNQNQYGNRMQGGQGGYRGNQQRQQQQQPQQGFNMPPMMVPPGQPPFYGGNQPNHHHQQPSFAPSPFSMGGGGGGSQGGPHEQHGPGGNQNGGFGVSSSSMDDYSMWTDENDEDAKKKKSLRDKGLSGWGDADVSNSKPIRRWIVPEGQEEDFETAMERCPSHLKKKALNEEALRRRLTSENPQIVAQAQQQAEEEANAMMRIGRRPIVPSGWGDIPSEISTDKSDSEFDQSSSRGWDEGSISGGGSGRHPSHHQSNDNSMWNSPSVGGGQSNSETRNPFFAQHMQQQQHQQQHQPHYGGYGDNGVLDGGSLWSAAVMDGSSMVPPHPTMGVGSSASSSSIPIGMLMMSGSGNVGGGPPSSSSLLDEDGSQKKLAENLKLAVQKGHLDISLLSLPHIPPNVLDLLTEILAVIPRLDDYEDELKKLGENRPSNYDEGASKEEKESWMSKDQKNDHDKAVIGVVTAKIEVTQLSKKITEALIEAGLLPPQPQTSTSANTSTNHLNHRGGPPPGSDGGAGPSTSRSGGGGAAGGDSFNSSGGGGPPDHYYDYSFLG
Protein: Cytochrome c oxidase copper chaperone 2 (Q94FT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Copper chaperone for cytochrome c oxidase (COX). Binds 2 copper ions and delivers them to the Cu(A) site of COX (By similarity).
Subcellular location: Mitochondrion intermembrane space.
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40 homolog
- Cytochrome c oxidase copper chaperone 1
- Cytochrome c oxidase 19-1
- Copper transporter 3
- Copper transporter 5
- Copper transporter 4
- Cytochrome c biogenesis protein CCS1, chloroplastic
- Cytochrome c oxidase assembly protein COX11
- Cytochrome c oxidase subunit 6b-2
- Cytochrome c oxidase subunit 6b-3
Sequence:
MSGLQAQDSACSLDKPSKDVVATETKPKKRICCACPDTKKLRDECIVEHGESACTKWIEAHILCLRSEGFKV
Protein: Protocadherin related 15 (A0A8I6AT55)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MSPQFALWKCMPHGILLASLLIVSWGQYDDDWQYEDCKLARGGPPATIVAIDEESRNGTILVDNMLIKGTAGGPDPTIELSLKDNVDYWVLLDPVKQMLFLNSTGRVLDRDPPMNIHSIVVQVQCVNKKVGTVIYHEVRIVVRDRNDNSPTFKHESYYATVNELTPVGTTIFTGFAGDNGATDIDDGPNGQIEYVIQYNPEDPTSNDTFEIPLMLTGNVVLRKRLNYEDKTRYYVIIQANDRAQNLNERRTTTTTLTVDVLDGDDLGPMFLPCVLVPNTRDCRPLTYQAAIPELRTPEELNPILVTPPIQAIDQDRNIQPPSDRPGILYSILVGTPEDYPRFLHMHPRTAELTLLEPVNRDFHQKFDLVIKAEQDNGHPLPAFASLHIEILDENNQSPYFTMPSYQGYILESAPVGATISESLNLTTPLRIVALDKDIEDTKDPELHLFLNDYTSVFTVTPTGITRYLTLLQPVDREEQQTYTFLITAFDGVQESEPVVVNIRVMDANDNTPTFPEISYNVYVYTDMSPGDSVIQLTAVDADEGSNGEISYEILVGSKGDFVINRTTGLVSIAPGVELVVGQTYALTVQASDNAPPAERRHSICTVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAVLLNLQATDREGDPITYAIENGDPQRVFNLSETTGILSLGKALDRESTDRYILIVTASDGRPDGTSTATVNIVVTDVNDNAPVFDPYLPRNLSVVEEEANAFVGQVRATDPDAGINGQVHYSLGNFNNLFRITSNGSIYTAVKLNREARDHYELVVVATDGAVHPRHSTLTLYIKVLDIDDNSPVFTNSTYTVVVEENLPAGTAFLQIEAKDVDLGANVSYRIRSPEVKHLFALHPFTGELSLLRSLDYEAFPDQEASITFLVEAFDIYGTMPPGIATVTVIVKDMNDYPPVFSKRIYKGMVAPDAVKGTPITTVYAEDADPPGLPASRVRYRVDDVQFPYPASIFDVEEDSGRVITRVNLNEEPTTIFKLVVVAFDDGEPVMSSSATVRILVLHPGEIPRFTQEEYRPPPVSELAARGTVVGVISAAAINQSIVYSIVAGNEDDKFGINNVTGVIYVNSPLDYETRTSYVLRVQADSLEVVLANLRVPSKSNTAKVYIEIQDENDHPPVFQKKFYIGGVSEDARMFTSVLRVKATDRDTGNYSAMAYRLIIPPIKEGKEGFVVETYTGLIKTAMLFHNMRRSYFKFQVIATDDYGKGLSGKADVLVSVVNQLDMQVIVSNVPPTLVEKKIEDLTEILDRYVQEQIPGAKVVVESIGARRHGDAFSLEDYSKCDLTVYAIDPQTNRAIDRNELFKFLDGKLLDINKDFQPYYGEGGRILEIRTPEAVTSIKKRGESLGYTEGALLALAFIIILCCIPAILVVLVSYRQFKVRQAECTKTARIQSAMPAAKPAAPVPAAPPPPPPPPPPGAHLYEELGESAMHNLFLLYHFEQSRGNNPVPEDRSSHRDGMAFSSSTTESHEPAHVEGPLDNQANPARTFSFLPDEDDLSTHNPLYMESIGQRSTNSDLQPGTEFGELFVPRTQVKSQSLRGPREKIQRVWNQSVRFPRRLMWKTPNRPETIDLVEWQITRQRAECEKTRCHPSQQGSSNLMVTTEDARGSEKEGGHRDTLIVQQTEQLKSLSSGSSFSSSWSHFSFSTLPTISRAVELGSEPDVVTSPADCTLELSPPRRPRVLNSLGSKRETPTCASDTETKRNSFEMVPHPPSISAPLPQLPLPQPPIAFTTFPLPLSSPNPPRPQLLTFSLPISTTPASSLPPPPPPSLPPPPRPPAPRLFPLPPSTSVPSTDSISTPAAKCTASVTHARETMSTTQPPASNPPCGAEPHRHPKGILRHVKNLAELEKSVSNMYSHIEKNCPPTELSKLHPFCPAEKTNMKITCDQSQETLVRVVEGIDVQTHSQSTSL
Protein: Nickel import ATP-binding protein NikO (EC 3.6.3.-) (Energy-coupling factor transporter ATP-binding protein NikO) (ECF transporter A component NikO) (D5AQY6)
Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Function: Part of the energy-coupling factor (ECF) transporter complex NikMNQO involved in nickel import. The complex confers nickel uptake upon expression in E.coli; can also transport cobalt with a very low affinity. Presumably responsible for energy coupling to the transport system.
Subcellular location: Cell inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Nickel transport protein NikQ
- Fused nickel transport protein NikMN
- Cobalt transport protein CbiQ
- Cobalt transport protein CbiM
- Cobalt import ATP-binding protein CbiO
- Cobalt transport protein CbiN
- DUF4198 domain-containing protein
- ABC transporter, ATP-binding/permease protein
- Energy-coupling factor transporter transmembrane protein BioN
- ABC transporter, ATP-binding/permease protein
Sequence:
MTPAFELQGVQFAYKGVPALNGLDLTLPLGRRTALLGANGSGKSTLLRLLDGLQFPAAGRISAFGTPLTEAMFTDEAAAIAFRRRVGFVFQNPEVQLFCPSVFDELAFGPLQLHWPKERIRARVARAIAQFGLGPLAGRPPHRLSGGEKKRVALASVLILDPEVLLLDEPTAALDPQATDDIAALLETEFGARNPGRTLIFSSHDLDLVARIADHVVVLEAGKVAAAGPAAEVLARTALLRRARLLPGFDGTAP
Protein: LD04103p (Stathmin, isoform A) (Q9VMH3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLIGLVRDSVMQCFCHTCRAPGILPAVSRRSAPIKKNNKIRSKQPRLSKKVKFITTEIRCQEKSRGGLSYEVILAEPAPNVAVPKRPVTPGKNVSVEEIEQKLKAAEERRISLEAKKMADISTKLAKVEEATRKKDEITNEFITQTKEQLESKMELHVEKREAIISDMKEKLKIHAQDIEKTRETLEQQKANEQKAIEEKLKIAQSLRDENIKKMLDRLKEHERRAELVRQNKAQAQDLDGQQSAIASSG