wanglab/gogpt-training-data huggingface dataset:
Protein: Polarized growth protein rax2 (Revert to axial protein 2) (O14239)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Controls cell polarity, through the G1 phase of mitosis, via regulation of for3 localization. Required for actin cable formation where it directs the spatial distribution of the actin cables.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17085965}; Single-pass type I membrane protein {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17085965}. Note=Localizes at the cell cortex of the 'old' growing cell tips.
Interaction partners:
- Protein rax1
- Putative zinc protease mug138
Sequence:
MAIYSSFWIRLYFTFRFFCYFLTSVVASDVSFLGDFSGFNVLSNSSANTDLSSQFFEQTNNGSLSSLIDTSYSNSQICYSSWQGDLYVIVLDSEQQTVLLQSNFTSNPTSLEIFSSQNTSFFGNISAIFCDDKFPYAYATFTFSDKPSFTSIYRWNVTNSNVTIEHFYNVKGNVDSLFFLNNDSVAISGNFTEISPFSSSNGPQIAKLAFRSNNSFSQNSLNRNLSSVSCDLTDSYSLWDPSSSGLVSIYAWAPYLIDFNRIRFYNYESSENSVAFFSAINPADGTVLPLTHYDLETGLSSTCDVNCSLQNFANYQDFYFSKGYNSYQIEIQMFGNGEATENSAFGLSSLQFFETNQNSYFDDSYNQESCGFPGLNSLSSYEGNFEASFSNASMPYWIQTIAGEQASVSFFPNITVPTNGTVQLLIPGCTYDNTCSQRGSVIANVYFAKNKQPATKLVQQASDFDQYVSLYSGYLQGFSDNFRPYVELLPYKNSRMVTHSIRFLEQSYTNVSNGLVFVNTTTDVNKLPSIIEFPAASKLRGTAISQIKSLSNGNFSLYMTGNFSDNYGNNVVYMDSLNHLHSFPNNGLNGWVSYIYVSGDSSYFGGNFTHTGDGSIKLNYIAMYSETSRNWSSLGLGTNGPVTHIGSTSLFIDGKIESFISFQGDFNEVYTSEGYAISTSGFSLWNPSSKSWVSMEKLGFYMSGYLFDIPGFNSTQRIYSGNLSAIASYSTRNIAHFSSDSLNDTFIPCYVNAFPSYIRLEDIAYPFANNSMIAILGSEEMEDKCTAAVYFANSTEPIYPKRILSANCSSKFIVLEDCLIIYSNDTDESDIVKNTFVSFNTTSNSLGNTTALSQLKGHINSVIVDDSYNNIFFGGNLSEQSSGCVGFCIFEYNSSSWRNISHNLISAEVQSILWVNETYSSMYLAGKFVWDTSDVDYLLMYNFDNNTIMSCKGSSSIPGPVLLASLKSQSKDEYSVLLYGTEVSSSDTYLNVLNSEGAINSYSLDIHLNQSTINSIDFFESNQISQIPINDSIIVLSGLIVLDDSSKASAVYCVNKSCLPLLTAFKDNGEAGIVRKVVQQKSFSSSASKMIPVTTKYDHIGQPRYVVIISLGISIGVMFLIMSGSIVVEIIHWFFSEHVETLHDYSNFLKELKTQ
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (F7FHM1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSRGPRLLLPAVLFLGLGGLVSSSGSSGVRKRGPLVFFDVRIGDKDVGRIVIGLFGKVVPRTVENFVTLATGEKGYGYKGSIFHRVIKDFMIQGGDFTARDGTGGMSIYGETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPAWLDGKHVVFGKVLDGMTVVHSIELQATDDHDRPLTDCTIVNSGKIDVKTPFVVEVPDW
Protein: Protein Wnt (A1BPR0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
Interaction partners:
Sequence:
MMLLKLKWTSSGVKDTPHTLLSIIITFCVFFMLEIVDANSWWSLAMNPLLIPEVYVIGGQPLCSQLSGLSKGQKKLCQLYQDHMQYIGEGAKTGIRECQHQFRHRRWNCSTVDNSTVLGRVMHIGSRESAFAFAISAAGVLHAVSRACREGALSSCGCSRASRPKDLPRDWLWGGCGDNLNYGYRFSREFVDAREREKTFSKGSAESARQMMNLHNNEAGRRIVSDLADVSCKCHGVSGSCSLKTCWLQLADFRKVGDVLKEKYDSAAAMRMNGRGKLVQMHSKFSPPSGQDLLYLQPSPDYCIRNSSSGSLGTQGRLCNKTSEGMDGCALMCCGRGYDQYKAELVERCHCKFHWCCYVRCKRCSSIVDQYVCK
Protein: NOP2 nucleolar protein (F5GYR3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVNHGDLWGSEDDADTVDDYGADSNSEDEEEGEALLPIERAARKQKAREAAAGIQWSEEETEDEEEEKEVTPESGPPKVEEADGGLQINVDEEPFVLPPAGEMEQDAQAPDLQRVHKRIQDIVGILRDFGAQREEGRSRSEYLNRLKKDLAIYYSYGDFLLGKLMDLFPLSELVEFLEANEVPRPVTLRTNTLKTRRRDLAQALINRGVNLDPLGKWSKTGLVVYDSSVPIGATPEYLAGHYMLQGASSMLPVMALAPQEHERILDMCCAPGGKT
Protein: Carboxylic acid reductase (CAR) (EC 1.2.1.-) (ATP/NADPH-dependent carboxylic acid reductase) (FAAL9) (Medium/long-chain-fatty-acid--AMP ligase FadD9) (EC 6.2.1.-) (Q50631)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes (By similarity). In vitro, also catalyzes the activation of medium/long-chain fatty acids as acyl-adenylates (acyl-AMP).
Interaction partners:
- Phenyloxazoline synthase MbtB
- Polyketide synthase Pks13
- Phthioceranic/hydroxyphthioceranic acid synthase
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks1
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Mycoketide-CoA synthase
- Mycocerosic acid synthase-like polyketide synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Mycolipanoate synthase
- Probable polyketide synthase Pks7
Sequence:
MSINDQRLTRRVEDLYASDAQFAAASPNEAITQAIDQPGVALPQLIRMVMEGYADRPALGQRALRFVTDPDSGRTMVELLPRFETITYRELWARAGTLATALSAEPAIRPGDRVCVLGFNSVDYTTIDIALIRLGAVSVPLQTSAPVTGLRPIVTETEPTMIATSIDNLGDAVEVLAGHAPARLVVFDYHGKVDTHREAVEAARARLAGSVTIDTLAELIERGRALPATPIADSADDALALLIYTSGSTGAPKGAMYRESQVMSFWRKSSGWFEPSGYPSITLNFMPMSHVGGRQVLYGTLSNGGTAYFVAKSDLSTLFEDLALVRPTELCFVPRIWDMVFAEFHSEVDRRLVDGADRAALEAQVKAELRENVLGGRFVMALTGSAPISAEMTAWVESLLADVHLVEGYGSTEAGMVLNDGMVRRPAVIDYKLVDVPELGYFGTDQPYPRGELLVKTQTMFPGYYQRPDVTAEVFDPDGFYRTGDIMAKVGPDQFVYLDRRNNVLKLSQGEFIAVSKLEAVFGDSPLVRQIFIYGNSARAYPLAVVVPSGDALSRHGIENLKPVISESLQEVARAAGLQSYEIPRDFIIETTPFTLENGLLTGIRKLARPQLKKFYGERLERLYTELADSQSNELRELRQSGPDAPVLPTLCRAAAALLGSTAADVRPDAHFADLGGDSLSALSLANLLHEIFGVDVPVGVIVSPASDLRALADHIEAARTGVRRPSFASIHGRSATEVHASDLTLDKFIDAATLAAAPNLPAPSAQVRTVLLTGATGFLGRYLALEWLDRMDLVNGKLICLVRARSDEEAQARLDATFDSGDPYLVRHYRELGAGRLEVLAGDKGEADLGLDRVTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNAAGTAELLRLALTGKRKPYIYTSTIAVGEQIPPEAFTEDADIRAISPTRRIDDSYANGYANSKWAGEVLLREAHEQCGLPVTVFRCDMILADTSYTGQLNLPDMFTRLMLSLAATGIAPGSFYELDAHGNRQRAHYDGLPVEFVAEAICTLGTHSPDRFVTYHVMNPYDDGIGLDEFVDWLNSPTSGSGCTIQRIADYGEWLQRFETSLRALPDRQRHASLLPLLHNYREPAKPICGSIAPTDQFRAAVQEAKIGPDKDIPHLTAAIIAKYISNLRLLGLL
Protein: ATP synthase subunit 9, mitochondrial (Lipid-binding protein) (Oligomycin resistance protein 1) (P61829)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Subcellular location: Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit 4
- ATP synthase subunit J, mitochondrial
- ATP synthase subunit d
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit H
- ATP synthase subunit delta, mitochondrial
- ATP synthase protein 8
Sequence:
MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRNPSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV
Protein: Annexin (Q804H2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004187}. Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein S100
- Protein S100
- Dysferlin
- Actin alpha 1, skeletal muscle b.
- Formyl peptide receptor 1
- Cellular tumor antigen p53
Sequence:
MSFVSSFLEQLAYQGMQETTVQDITEVQGTVKPYAQFNAAADAAVLDKAIKAKGVDEPTIIDTLVHRSNAQRQQIKAAYQQATSKPLDVALKNALKGELEDVVLGLLMTPAQYDAFQLKYAMKGAGTTEDTLIEILASRTNKEIGDIKQVYKQEYKKDLEADIKSDTSGDFRNALLSLCKATRSEDNIVKDDLADKDARALYEAGEKRKGTDCSVFIDILTSRNGPHLRKVFQQYNKYSKVDVAKAIDLELKGDIESCLIAVVKCVSNKPAFFAEKLNLAMKGSGYRGKILTRILVSRSEIDLANIKQEYQKKYGKSLYQDIQDDTKGDYETILLALCGN
Protein: SEC23-interacting protein (p125) (Q9Y6Y8)
Organism: Homo sapiens (Human)
Function: Plays a role in the organization of endoplasmic reticulum exit sites. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P) and phosphatidylinositol 5-phosphate (PI(5)P).
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum {ECO:0000305}.
Interaction partners:
- Protein transport protein Sec31A
- Protein SEC13 homolog
- Protein transport protein Sec23A
- Protein transport protein Sec24B
- Protein transport protein Sec24A
- Sec1 family domain-containing protein 1
- Programmed cell death protein 6
- Protein transport protein Sec16A
- Protein transport protein Sec24C
- WW domain-containing oxidoreductase
Sequence:
MAERKPNGGSGGASTSSSGTNLLFSSSATEFSFNVPFIPVTQASASPASLLLPGEDSTDVGEEDSFLGQTSIHTSAPQTFSYFSQVSSSSDPFGNIGQSPLTTAATSVGQSGFPKPLTALPFTTGSQDVSNAFSPSISKAQPGAPPSSLMGINSYLPSQPSSLPPSYFGNQPQGIPQPGYNPYRHTPGSSRANPYIAPPQLQQCQTPGPPAHPPPSGPPVQMYQMPPGSLPPVPSSVQSPAQQQVPARPGAPSVQVPSPFLLQNQYEPVQPHWFYCKEVEYKQLWMPFSVFDSLNLEEIYNSVQPDPESVVLGTDGGRYDVYLYDRIRKAAYWEEEPAEVRRCTWFYKGDTDSRFIPYTEEFSEKLEAEYKKAVTTNQWHRRLEFPSGETIVMHNPKVIVQFQPSSVPDEWGTTQDGQTRPRVVKRGIDDNLDEIPDGEMPQVDHLVFVVHGIGPVCDLRFRSIIECVDDFRVVSLKLLRTHFKKSLDDGKVSRVEFLPVHWHSSLGGDATGVDRNIKKITLPSIGRFRHFTNETLLDILFYNSPTYCQTIVEKVGMEINHLHALFMSRNPDFKGGVSVAGHSLGSLILFDILSNQKDLNLSKCPGPLAVANGVVKQLHFQEKQMPEEPKLTLDESYDLVVENKEVLTLQETLEALSLSEYFSTFEKEKIDMESLLMCTVDDLKEMGIPLGPRKKIANFVEHKAAKLKKAASEKKAVAATSTKGQEQSAQKTKDMASLPSESNEPKRKLPVGACVSSVCVNYESFEVGAGQVSVAYNSLDFEPEIFFALGSPIAMFLTIRGVDRIDENYSLPTCKGFFNIYHPLDPVAYRLEPMIVPDLDLKAVLIPHHKGRKRLHLELKESLSRMGSDLKQGFISSLKSAWQTLNEFARAHTSSTQLQEELEKVANQIKEEEEKQVVEAEKVVESPDFSKDEDYLGKVGMLNGGRRIDYVLQEKPIESFNEYLFALQSHLCYWESEDTALLLLKEIYRTMNISPEQPQH
Protein: Exo-poly-alpha-D-galacturonosidase (EC 3.2.1.82) (E0SKR4)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- Pectinesterase A
- Pectin acetylesterase
- Xylosidase/arabinosidase
- Pectinesterase B
- 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
- Pectate lyase
Sequence:
METITFSRRPALASIVAACLISTPALAATAQAPQKLQIPTLSYDDHSVALVWDAPEDTSNITDYQIYQNGQLIGLASQNNDKNSPAKPYISAFYKNDTGNFHRRVVIQNAKIDGLKANTDYQFTVRTVYADGSTSADSNAVTATTAATPQVINITQYGAKGDGTTLNTTAIQKAIDACQTGCRVDIPAGVFKTGALWLKSDMTLNLLQGATLLGSDNAADYPDAYKIYSYSSQVRPASLINAIDKTSSAVGTFKNIRIIGKGVIDGNGWKRSADAKDELGNSLPQYVKSDSSKVSKDGILAKNQVAAAVAKGMDTKTAYSQRRSSLVTLRGVKNVYIADVTIRNPANHGVMFLESQNVVENGVIHQTFDANNGDGVEFGNSQNIMVFNSVFDTGDDSINFAAGMGQDAQSQEPSQNAWLFNNYFRRGHGAVVMGSHTGAGIIDVLAENNVISQNDVGLRAKSAPAIGGGAHGIVFRNSAMKNLAKQAVIVTLSYSDSNGTIDYTPAKVPARFYDFTVKNVTVQDSTGSSPVIEITGDSGKGIWHSQFTFSNMKLSGVTPASISDLSDSQFNNLTFSKLRSGSSPWKFGTVKNVSVDGKIVTP
Protein: Inactive serine/threonine-protein kinase ZRK12 (O64798)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with RPP13L4/ZAR1, involved in the regulation of the ambient temperature-sensitive intersection of growth and immune response in the absence of pathogens.
Interaction partners:
Sequence:
MGWWRKKKKPKSEIASERGAKLLKDLIECCDGKSNPIKFFSADEIRKATNNFGVSNLVSELSHDFDYKWYSGKNENHDMILVRKAFSQSVYYKDTFFRDIAVSSMVSGHKNFLKLIGYCLEFEEPVMVYHGVKKHYHLESSEQPWKRRMKIAEDIATALAYLHTAFPRPFVYRCLSLTNILLDEDGVAKLMDFSFCVSIPEGETFVQVDYIAGTVDYLKPNYLKHGVVSEETDVFAVGHSMQMLLMGEKIFDRIMRRPFPTSKFMEEPKMDEIADPEMGEISEEELCQMKAFLLLSLRCTGHVGEVPTMVEVAKELKSIQRCLHNDTFSPSVETQFDSHQDISSSVILSNQTKDTRALLRCIACHVFDEMFQWVMMNWFRFFRRNRRIC
Protein: Metal transporter (F1QIW8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU369091}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369091}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Transient receptor potential cation channel, subfamily M, member 6.
- Cystathionine beta-synthase
- Cystathionine beta-synthase
- Solute carrier family 41 member 1
- FXYD domain-containing ion transport regulator
- Cytosolic purine 5'-nucleotidase
- Arsenite methyltransferase.
Sequence:
MAEPSVPVPPRKMASLSRVRAFTLIFLTASSCLITPTSGKEGGGEETVIIGLRLEDTDDISFMDRGFLRVSERSRVRLRVYGQNINNETWSKIAFTEHERSRVIGNIDSSSGDNQSQEDTSGLHPCGIRTSDILILPNIVLNRKTSGTVEIEVKPLRKTERSKAYYLCIATSTPAVAGAHDPWTENTWIYHDGEDTKVIVVEEKKFLLPFWLQVIFISMLLCLSGMFSGLNLGLMALDPMELQIVQNCGTEKEKNYARKIEPVRSQGNYLLCSLLLGNVLVNTTLTILLDDIAGSGLIAVVMSTIGIVIFGEIVPQAICSRHGLAVGANTIFLTKFFMLLTFPASYPVSKLLDYLLGQEIGTVYNREKLLEMLRVTDPYNDLVKEELNIIQGALELRTKTVEDVMTPLRDCFMITGDATLDFNSMSEIMESGYTRIPVFEGDRSNIVDLLFVKDLAFVDPDDCTPLKTITKFYSHPLHFVFNDTKLDAMLEEFKKGKSHLAIVQRVNNEGEGDPFYEVLGIVTLEDVIEEIIKSEILDETDLYTDNKTKKKITHRERKQDFSAFKHMDNEMKVKISPQLLLATLRFLATEVEPFSPSQMSEKILLRLLKHPNVIQEVKYNDKNKKAIEHYLFHRNKPVDYFILVLQGKVEVEAGKEGLRFEAGAFSSYGMMALTASPENKSPPRSFGLNHSDSLNRSERIEVITPSLGSSNNQLNAFLQIYVPDYSVRAVSDVQYIKVTRQQYQNAVMASRIDKTPQSSESEYTKIEMALTELHDGLTDETTTLFNQTQNCVVHNKSNHTGHSEGPI
Protein: Tubulin-specific chaperone E (Tubulin-folding cofactor E) (Q15813)
Organism: Homo sapiens (Human)
Function: Tubulin-folding protein; involved in the second step of the tubulin folding pathway and in the regulation of tubulin heterodimer dissociation. Required for correct organization of microtubule cytoskeleton and mitotic splindle, and maintenance of the neuronal microtubule network.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Tubulin-specific chaperone D
- Serine protease FAM111A
- Tubulin-folding cofactor B
- Tubulin-specific chaperone A
- Tubulin-specific chaperone E
- Tubulin-specific chaperone C
- Carboxypeptidase N catalytic chain
- E3 ubiquitin-protein ligase synoviolin
- Tubulin alpha-1A chain
- Tubulin alpha-8 chain
Sequence:
MSDTLTADVIGRRVEVNGEHATVRFAGVVPPVAGPWLGVEWDNPERGKHDGSHEGTVYFKCRHPTGGSFIRPNKVNFGTDFLTAIKNRYVLEDGPEEDRKEQIVTIGNKPVETIGFDSIMKQQSQLSKLQEVSLRNCAVSCAGEKGGVAEACPNIRKVDLSKNLLSSWDEVIHIADQLRHLEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITWAEVLRCVAGCPGLEELYLESNNIFISERPTDVLQTVKLLDLSSNQLIDENQLYLIAHLPRLEQLILSDTGISSLHFPDAGIGCKTSMFPSLKYLVVNDNQISQWSFFNELEKLPSLRALSCLRNPLTKEDKEAETARLLIIASIGQLKTLNKCEILPEERRRAELDYRKAFGNEWKQAGGHKDPEKNRLSEEFLTAHPRYQFLCLKYGAPEDWELKTQQPLMLKNQLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCLLVRW
Protein: Tight junction protein ZO-1 (Q56VX4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSEDPSWYKTSMSSTSSCIEEEHEPVDQDEEEMYNPSGCTWQLLSVSLHRAANLGFGIAISGGRDNPHFTSGDPVVVISDVVPNGPAWGLLQVNDRILSANQVSFENIEYSSAVDIIKNKDHIDMIVKRRVAVPMLEYEQRTLKFTLSKSRKKDDFGIVVGCKFYIKEIRNPKLAEKDPGLKEGDSVLRINGQSLEGASLEEVNKWLERSRDKLCLVIQRDVRRGTSRWPSQNTVYERVGSVAATPRHSPSPMLPHMPITQRNSHEYVNSPRHRSDGSVERRVSSPANSQLSNFNGMASSQITTQDYDCYTRQPSRSIDANGVANIMFRKVGGSVGVRVIGGNEVGIFVSAVAADSPASLHGVSCGDRILEVNGRNMRGVTRESAVQLLLGLDDRVSLRLEHARQDFEHVRANQLGDNFYIRSHFSREKRDKASPLELSINEGDIFHVTDTLFGGTVGLWQAARVYSSSENKGEPVKGVIPNQATAEQIAKEWRVYVEAKQAKSGGSGTLLRRKFESRRTKSLPKNMICDPTELNLPLPAYERVALNTPSFHRPVVLFGPLADIARHQLLTQFSARFGSPESDGGVIRLSSVDHVIASMKHCVLDISIESVERLQLAQYAPIVVFLDVDGRSKIREIRKKCNAPHLSSRKLAENGNQIKKHHSHLLSATIDATHETGWFDALRELIGHLQQRRLWMPEFPPNLPLEDVLLFPLPKWDGDVDSLKSEYVDYQDSLPRKGGEKKWDSSPLQTPGDLPSEMREYSTMPRPQHHQLGQDFGGNRNRQSSNSQSTLSTFVTTASSSNPPRPLLTPTRDESASRTTTPHGYYHVKQLSPSNMQHRLDNTTPSNFDFSNVQPSNSNPVPNGRYHPLTPSSMTSSSSGASRTAGQGQQQTAPPPRPPPVNSGNSSPYTQSYIRNKWNNDGAMDARGAENQTPPVVPARTNGSASPANASISLTVSNVPTGSSIASKSPTPRLDENENGQKSEEEEPTVVEESTALIGSLGGVIRCEKSNVELRIPAGAITEGQEHEIYVKVCREGDSSPIDRSKGETLLSPLVMCGPQGLKFEKQCELRMPHTGPVTADSDGQWSFSLKTGEGGEWKHMEIEQQQATNANLDQFLTVPITHF
Protein: Tachykinin-like peptide-IV (P.nigriventer tachykinin peptides IV) (PnTkP-IV) (U29-ctenitoxin-Pn1d) (U29-CNTX-Pn1d) (P86301)
Organism: Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer)
Subcellular location: Secreted {ECO:0000269|PubMed:15573368}.
Interaction partners:
Sequence:
QKKDKKDKF
Protein: Ephrin type-B receptor 6 (HEP) (Tyrosine-protein kinase-defective receptor EPH-6) (O15197)
Organism: Homo sapiens (Human)
Function: Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2.
Subcellular location: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
Interaction partners:
- Ephrin-B1
- Ephrin-B2
- Ephrin-B3
- Ephrin-A1
- Ephexin-1
- Ephrin-A5
- Ras GTPase-activating protein 1
- Ephrin-A3
- Tyrosine-protein kinase ABL1
- Ephrin-A4
Sequence:
MATEGAAQLGNRVAGMVCSLWVLLLVSSVLALEEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEACHVAGAPPGTGQDNWLQTHFVERRGAQRAHIRLHFSVRACSSLGVSGGTCRETFTLYYRQAEEPDSPDSVSSWHLKRWTKVDTIAADESFPSSSSSSSSSSSAAWAVGPHGAGQRAGLQLNVKERSFGPLTQRGFYVAFQDTGACLALVAVRLFSYTCPAVLRSFASFPETQASGAGGASLVAAVGTCVAHAEPEEDGVGGQAGGSPPRLHCNGEGKWMVAVGGCRCQPGYQPARGDKACQACPRGLYKSSAGNAPCSPCPARSHAPNPAAPVCPCLEGFYRASSDPPEAPCTGPPSAPQELWFEVQGSALMLHWRLPRELGGRGDLLFNVVCKECEGRQEPASGGGGTCHRCRDEVHFDPRQRGLTESRVLVGGLRAHVPYILEVQAVNGVSELSPDPPQAAAINVSTSHEVPSAVPVVHQVSRASNSITVSWPQPDQTNGNILDYQLRYYDQAEDESHSFTLTSETNTATVTQLSPGHIYGFQVRARTAAGHGPYGGKVYFQTLPQGELSSQLPERLSLVIGSILGALAFLLLAAITVLAVVFQRKRRGTGYTEQLQQYSSPGLGVKYYIDPSTYEDPCQAIRELAREVDPAYIKIEEVIGTGSFGEVRQGRLQPRGRREQTVAIQALWAGGAESLQMTFLGRAAVLGQFQHPNILRLEGVVTKSRPLMVLTEFMELGPLDSFLRQREGQFSSLQLVAMQRGVAAAMQYLSSFAFVHRSLSAHSVLVNSHLVCKVARLGHSPQGPSCLLRWAAPEVIAHGKHTTSSDVWSFGILMWEVMSYGERPYWDMSEQEVLNAIEQEFRLPPPPGCPPGLHLLMLDTWQKDRARRPHFDQLVAAFDKMIRKPDTLQAGGDPGERPSQALLTPVALDFPCLDSPQAWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLLQQHLRQQGSVEV
Protein: Stage VI sporulation protein D (P37963)
Organism: Bacillus subtilis (strain 168)
Function: Required for assembly of a normal spore coat. May be a component of the innermost layer of the spore coat that aids in its adherence to the prespore.
Interaction partners:
- Stage IV sporulation protein A
- Spore coat protein E
- SpoIVD-associated factor A
- Uncharacterized protein YsxE
- Stage V sporulation protein M
- Sporulation-specific transcriptional regulator GerR
- Spore coat protein GerQ
- Stage II sporulation protein Q
- Uncharacterized protein YabS
- Stage II sporulation protein P
Sequence:
MPQNHRLQFSVEESICFQKGQEVSELLSISLDPDIRVQEVNDYVSIIGSLELTGEYNIDQNKHTEEIYTDKRFVEQVRKREDGSAELTHCFPVDITIPKNKVSHLQDVFVFIDAFDYQLTDSRILTIQADLAIEGLLDDTQDKEPEIPLYEAPAAFREEELSEPPAHSVVEEPGASSAEEAVLQHEPPAEPPELFISKAGLREELETEKAESEPPESVASEPEAREDVKEEEESEELAVPETEVRAESETEESEPEPDPSEIEIQEIVKAKKETAEPAAAIADVREEADSPAETELREHVGAEESPALEAELHSETVIAKEKEETTVSPNHEYALRQEAQNEEAAQSDQADPALCQEEAEPDEALESVSEAALSIEDSRETASAVYMENDNADLHFHFNQKTSSEEASQEELPEPAYRTFLPEQEEEDSFYSAPKLLEEEEQEEESFEIEVRKTPSAEEPKEETPFQSFQLPESSETERKETDAVPRVAPAAETKEPQTKESDNSLYLTKLFTKEADEFSRMKICIVQQEDTIERLCERYEITSQQLIRMNSLALDDELKAGQILYIPQYKNSHA
Protein: Bifunctional peptidoglycan hydrolase (A0A0F6T2T1)
Organism: Pediococcus acidilactici
Interaction partners:
Sequence:
MFKSGKKWAFASIATASLGLVALNTNAEKAHADSDAQANTNSASQLDQQTKTAPVNEKQVTLAKPATVKASSAAVTAQSAAPASSAAQSVAKVNADSTAKADQHSAAAKVGTKATTSSAVKPAKEAASANAVKAAPASSAAKKASTSVASSAAPSSAASKTVTSAAVKDSAAKEAVSSAANVKSSSAAAKTSVNSSAVSEAAQKDAKVEKTAEKKTDNSSKDYTIDNTYRLADNEGSDQKTNNKIIVAHAVGQYSSARDVAIYEKREWDSSETYVQYIVGDGGRVYAVGEEGYVAWGAGKWANENAPVQVELAQTYSDSQFKKDYQTYVNLLRDSAKKWNIPTTLDSDEYTGIKSHVWVTEHVWGNHVDPYGYLGTHGITKEQFAHDLAYGFDNDAANDNQNNNQNDNHQNDNQNNQNNNHQNDSSNNHGNQNNQSYHVGDKVTIKNSASHWATGQSIYNGVKGHTYKIIQTNGHKLLLDQVISWINDGDVYKAGSNSGSSNNHNNNHTTNNADIKVGTVVTINNNASHWATGQSIYSGVKGKSYKVIQTNGNRLLLDKVISWINKGDVHVPGSNSNNNNSGNQNHNNGNNHNNNGNTESIHVGSKVTINNNAKRWATGQNIYSGVKGKTYTVIQMNGSRLLLDKVISWINKGDVHLPGSNGSQNNNNNNNNHANNNDGTIRVGTNVTIKPSAKRWATGQNIYYGVKGKTYKVIQMNGNRLLLDKVISWINKGDVYVPGSSNNNNSNSNNNHNNNGSNYHFTNQNWTAAQTNFVNSIASDVMNVCQNNHLYASVAMAQAVVESAYGASTLAQEAHNLFGIKADSTWHGATYTKNTQEVINGRVVTISAAFRKYDSFKDSIADYAKKLESRPQYANAFSNHAHNYVESVKAIKAGGYATAPTYVSSIVNCINNYGFYKLDGLNSAISL
Protein: Immunolglobulin kappa light chain variable region L22 (A2NXD2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDMRVPAQLLGLLLLWLPGVRFDIQMIQSPSFLSASVGDRVSIICWASEGISSNLAWYLQKPGKSPKLFLYDAKDLHPGVSSRFSGRGSGTDFTLTIISLKPEDFAAYYCKQDFSYP
Protein: Small ribosomal subunit protein uS8 (40S ribosomal protein S15a) (P62244)
Organism: Homo sapiens (Human)
Function: Structural component of the ribosome. Required for proper erythropoiesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.
Interaction partners:
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein eL39
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein eL32
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL27
- Small ribosomal subunit protein uS3
Sequence:
MVRMNVLADALKSINNAEKRGKRQVLIRPCSKVIVRFLTVMMKHGYIGEFEIIDDHRAGKIVVNLTGRLNKCGVISPRFDVQLKDLEKWQNNLLPSRQFGFIVLTTSAGIMDHEEARRKHTGGKILGFFF
Protein: Geranylgeranyl transferase type-2 subunit beta (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit beta) (GGTase-II-beta) (Type II protein geranyl-geranyltransferase subunit beta) (P46960)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit alpha
- GTP-binding protein ypt1
- Uncharacterized Rab geranylgeranyltransferase C15C4.03
- Synaptobrevin homolog ykt6
- Uncharacterized protein PB24D3.07c
- GTP-binding protein ypt2
- GTP-binding protein ypt3
Sequence:
MAVLLRDKHISYLHDIGNRTDELDFWLKEHLHVSAIYWSCMSFWLLKKKDQIDKERIVSFLLSCLTESGGFACYPGHDDHITNTVYAVQVLAMLDSLHVVDKDKVASYIIGLQNEDGSMKGDRWGEIDARFLYSGINCLAILGKLDYLNKNTAVDWLMKCYNFDGGFGLCPGAESHGAMVFTCVAALKILNKLDLIDEELLGWWISERQVKGGGLNGRPEKLPDSCYGWWDLSPLAIIGKLDWIDRNQLIDFLLGTQDADSGGFADRKEDATDVYHTCFSLAGLSLLQFPNIEPVDPRFCLPLEVTQKMKL
Protein: Small monomeric GTPase (P91857)
Organism: Caenorhabditis elegans
Interaction partners:
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- EEA1
- FYVE-type domain-containing protein
- Vps8 domain-containing protein
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar fusion protein MON1 homolog
- Vacuolar protein sorting-associated protein 39 homolog
- Vacuolar fusion protein CCZ1 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Receptor-mediated endocytosis protein 6
Sequence:
MAARNAGTARPGGPNRTCQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQTVCLDDATIKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNQESFQKAKNWVKELQRQASPNIVMALAGNKADVANKRTVEYEEANAYAEDNALLFMETSAKTSMNVNDIFMAIAKKLPIGPAQGEPTGTVDMNQPQQQQKGSCCK
Protein: ATP-sensitive inward rectifier potassium channel 11 (BIR) (Inward rectifier K(+) channel Kir6.2) (Potassium channel, inwardly rectifying subfamily J member 11) (P70673)
Organism: Rattus norvegicus (Rat)
Function: This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium. Can form cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q14654}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q14654}.
Interaction partners:
- ATP-binding cassette sub-family C member 9
- ATP-binding cassette sub-family C member 8
- ATP-sensitive inward rectifier potassium channel 8
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid type B receptor subunit 1
- Rap guanine nucleotide exchange factor 4
- Hexokinase-4
- Rap guanine nucleotide exchange factor 3
- Insulin-2
- tRNA-t
Sequence:
MLSRKGIIPEEYVLTRLAEDPTEPRYRTRERRARFVSKKGNCNVAHKNIREQGRFLQDVFTTLVDLKWPHTLLIFTMSFLCSWLLFAMVWWLIAFAHGDLAPGEGTNVPCVTSIHSFSSAFLFSIEVQVTIGFGGRMVTEECPLAILILIVQNIVGLMINAIMLGCIFMKTAQAHRRAETLIFSKHAVITLRHGRLCFMLRVGDLRKSMIISATIHMQVVRKTTSPEGEVVPLHQVDIPMENGVGGNSIFLVAPLIIYHVIDSNSPLYDLAPSDLHHHQDLEIIVILEGVVETTGITTQARTSYLADEILWGQRFVPIVAEEDGRYSVDYSKFGNTVKVPTPLCTARQLDEDRSLLDALTLASSRGPLRKRSVAVAKAKPKFSISPDSLS