wanglab/gogpt-training-data huggingface dataset:
Protein: Iron-sulfur cluster co-chaperone protein HscB (DnaJ homolog subfamily C member 20) [Cleaved into: Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic (C-HSC20); Iron-sulfur cluster co-chaperone protein HscB, mitochondrial] (Q8IWL3)
Organism: Homo sapiens (Human)
Function: Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria. Required for incorporation of iron-sulfur clusters into SDHB, the iron-sulfur protein subunit of succinate dehydrogenase that is involved in complex II of the mitochondrial electron transport chain. Recruited to SDHB by interaction with SDHAF1 which first binds SDHB and then recruits the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20. Plays an essential role in hematopoiesis (By similarity).
Subcellular location: [Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:20668094, ECO:0000269|PubMed:29309586}.; SUBCELLULAR LOCATION: [Iron-sulfur cluster co-chaperone protein HscB, mitochondrial]: Mitochondrion {ECO:0000269|PubMed:20668094}.
Interaction partners:
- Stress-70 protein, mitochondrial
- Iron-sulfur cluster assembly enzyme ISCU
- Cytochrome b-c1 complex subunit 9
- Glutaredoxin-related protein 5, mitochondrial
- Cysteine desulfurase
- Succinate dehydrogenase assembly factor 1, mitochondrial
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Complex III assembly factor LYRM7
- LYR motif-containing protein 4
- GrpE protein homolog 1, mitochondrial
Sequence:
MWRGRAGALLRVWGFWPTGVPRRRPLSCDAASQAGSNYPRCWNCGGPWGPGREDRFFCPQCRALQAPDPTRDYFSLMDCNRSFRVDTAKLQHRYQQLQRLVHPDFFSQRSQTEKDFSEKHSTLVNDAYKTLLAPLSRGLYLLKLHGIEIPERTDYEMDRQFLIEIMEINEKLAEAESEAAMKEIESIVKAKQKEFTDNVSSAFEQDDFEEAKEILTKMRYFSNIEEKIKLKKIPL
Protein: Cytochrome b559 subunit alpha (PSII reaction center subunit V) (P0C369)
Organism: Oryza sativa subsp. indica (Rice)
Function: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00642}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00642}.
Interaction partners:
- Cytochrome b559 subunit beta
- Photosystem II D2 protein
- Photosystem II CP43 reaction center protein
- Photosystem II CP47 reaction center protein
- Photosystem II protein D1
- Cytochrome b6-f complex subunit 4
- Cytochrome b6
- Photosystem II reaction center protein H
- Photosystem II reaction center protein K
- Photosystem II reaction center protein L
Sequence:
MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESRQGIPLITDRFDSLEQLDEFSRSF
Protein: Without children, isoform B (A8JRE3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Heterochromatin protein 1c
- Telomere-binding protein cav
- Relative of woc, isoform C
- Ubiquilin-like protein
Sequence:
MEEISSLDSFGADSNARPESATPRSEEQQDQDRQQTAPAASETLDTPASPPAEDAAAQESKPPPSKEADDDFEQISEGSLDADDNQSRDKAASTPADPVDAEEPAEEPTPNEEPQGGEDEQPQTEAVRVDPQEEPEEAEEETDALQATAEEVEAAAAEADAVDGGPASPEAMDVDEGEVDAEGEAEQEAEDDAALDREATDDVDMQSVGADSHQAEDAEPPEGRDEVDTSLEEQENGQDPDEREKDAAADEDDPDAEGDAESEQVDENAEETGEAEHGDDTVENVLEPEESDVCLIPDDQETEVTEAEKELARENAEKAAEEEEAEERQAKTPDNDRKSPADAAADPEDDSAAAVDATDVSPTTPTDAQAGAKSAATGIAEADGVAAAANEEEAGGDVPDPDEPTAEESSSAGAGEPGSTPKIIISWIVGSVQKCKQCGDEKNCGFRYRSPEESEEMDKEKENDKAEENAEEGEEEEARQKPAAPSGFEYICDTACVDALLEDQPGKYFVRRKKFLVEEVVREEGAAEAEASADGEGGDAEEEATPANTQDCLQCKDKTRCKYFIKQDQDCFYICNDDCFNLLNAEEPDKFKLKRHSIRVRNIGATTLQPPQNSPTKRTDGSVVARTVEEAETARLDRIESFRRRCADCEADINTDEKQLMWETMDFCNEVCLGSYQRTIGSTCETCKQEVSSIALGKYCVRFGFDVRQFCCAGCLNTFKKGLKTCSCCQKDISGGQEGFLAPVGDKDQFKDFCSQSCLRRYESMCNPRRKLRTDVCGVCNNQKPVRVEMLLEDREHYFCSNPCFSAFKFVSNVNADPCAMCSKYFERRSAESYTIYNEQQSPKVFCSRVCINVYIIVNRHIVSCQWCKVKKYNFDMIYQIGGPHDQETLTCSINCLTMHGVSCNISARAVTKCDNCSNFNTPQYHLTMSDASMRNFCTYQCVMQFQNQFARAPLTLDSDLPPSSAGSSKSQQQSNRGNKNAAPFPTGLPKRVKLKLSHTGKGGVGGKKSGSGTMLPVISTVQSLASGETEARIGNLTVRRKRGRPRESGTSSPPLSMPGVHPPAQRGRPRKHAVDYSARSPSPTMSGGSSHMGIPVRRNTTTTMDFGPATVTETKIITVPPYPKAVRNVNISCKPLTVTQGEQCSPDVRDCATQTEKDYSNKVLIPVPVPIFVPQPMYMYSAPFPVPVPIPLPIPVPIFIPTTRNTAQGILKEIKKIQDKMPEDPLEAELLMMAEMVAEEKHESDSDSDNEIKPDPGLVALQYQNSLESVAQQQQQQQVVDVSGAGHNPYGDDMLQIALKMATGDYDNHHQTSTVDLETSMTANTISSQSPMGHDGMGQMGVHHLDQQHHMLDATQRTARGRKRGVGVVMDPPNRNSRSPVKRQRGGEMDHSALQQQSQQAQQPQEKPDAQMFLKYTFGVNAWKQWVMTKNADIEKSSMRRRPFKTELLQMTADELNYSLCLFVKEVRKPNGTEYAPDTIYYLVLGIQQYLYVNGRIDNIFYDPYYERFTECLDEVARKFSVLYNDSQYIVTRVEEEHLWECKQLGAHSPHVLLSTLMFFNTKHFNLTTVEEHMQLSFSHIMKHWKRSSQNSKVPGSRNVLLRFYPPQAGLDANPRKKKVYEQQENEENPLRCPVRLYEFYLSKCPESVKTRNDVFYLQPERSCVPDSPVWYSTQALGQDALQRMLHRVKMVKEINIALLTT
Protein: Cell division cycle-associated protein 4 (Hematopoietic progenitor protein) (Q9CWM2)
Organism: Mus musculus (Mouse)
Function: May participate in the regulation of cell proliferation through the E2F/RB pathway (By similarity). May be involved in molecular regulation of hematopoietic stem cells and progenitor cell lineage commitment and differentiation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Sororin
Sequence:
MFARGLKRKYGDQEEGVEGFGTVPSYSLQRQSLLDMSLVKLQLCHMLVEPNLCRSVLIANTVRQIQEEMSQDGVWHGMAPQNVDRAPVERLVSTEILCRTVRGAEEEHPAPELEDAPLQNSVSELPIVGSAPGQRNPQSSLWEMDSPQENRGSFQKSLDQIFETLENKNSSSVEELFSDVDSSYYDLDTVLTGMMSGTKSSLCNGLEGFAAATPPPSSTCKSDLAELDHVVEILVET
Protein: Fibril biogenesis regulator DifD (Q1CXR3)
Organism: Myxococcus xanthus (strain DK1622)
Interaction partners:
- Fibril biogenesis regulator DifG
- Chemotaxis protein CheA
- Methyl-accepting chemotaxis protein DifA
- Fibril biogenesis regulator DifC
- Chemotaxis protein CheY
- Response regulator
- histidine kinase
- Chemotaxis protein CheY
- Response regulator
- Chemotaxis protein CheY
Sequence:
MAKRVLVVDDAIFMRNMIKDIFASGGFEVVGEAANGLEAVEKYKELKPDLTTMDIVMPFKSGIEATREIIKADSSAVVIMCSALGQESLVMEAIEAGASDFIVKPFRAEDVLAVVKKVLGET
Protein: Serpentine receptor class gamma (G3MU03)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- SRBC-64)
- Serpentine Receptor, class BC
- G-protein coupled receptor daf-37
- G-protein coupled receptor daf-38
- Serpentine receptor class X-43
- 7TM GPCR serpentine receptor class x
- Guanine nucleotide-binding protein alpha-3 subunit
- Guanine nucleotide-binding protein alpha-2 subunit
Sequence:
MNRNVLESKKIKCIIGFLSFNLSSNLTNLAQNKQVNFQNILTYLNSFISIRLPQNTGINGNLSNFFLTHNEFNMNMGCPINLFHALHYYFAYTQYIYNFLISYNRFCAITSLLDIEKRWKRSLWIFVTIMFVYPMIPAGLIFFNRSYYTYVSSKDNFYISSTLGHKAIYGFLAPNLFIITIFNTVLNIKAYKKLLVLKKTLRSVPDTNLFYMSLAMFGIDSFLAVLSTFKAIIFLLELKNSSEFFERLVDWIDLLVPFASDALTLTQPLLLLYFSSTLRQKCIERLPFLKVFLNNRFFVRSRNMHQELTKY
Protein: S-adenosylmethionine synthase 2 (AdoMet synthase 2) (EC 2.5.1.6) (Methionine adenosyltransferase 2) (MAT 2) (P17562)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9LUT2}.
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic
- Homocysteine S-methyltransferase 3
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 1
- S-adenosylmethionine decarboxylase proenzyme 1
- S-adenosylmethionine decarboxylase proenzyme 2
- S-adenosylmethionine decarboxylase proenzyme 3
- S-adenosylmethionine decarboxylase proenzyme 4
Sequence:
METFLFTSESVNEGHPDKLCDQISDAVLDACLEQDPDSKVACETCTKTNMVMVFGEITTKATIDYEKIVRDTCRSIGFISDDVGLDADKCKVLVNIEQQSPDIAQGVHGHFTKRPEDIGAGDQGHMFGYATDETPELMPLSHVLATKIGARLTEVRKNGTCRWLRPDGKTQVTVEYYNDNGAMVPVRVHTVLISTQHDETVTNDEIARDLKEHVIKPIIPEKYLDDKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVANGMARRALVQVSYAIGVPEPLSVFVDTYGTGLIPDKEILKIVKETFDFRPGMMTINLDLKRGGNGRFQKTAAYGHFGRDDPDFTWEVVKPLKWDKPQA
Protein: Toxin Tf2 (C0HJM9)
Organism: Tityus fasciolatus (Central Brazilian scorpion)
Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active against hNav1.3/SCN3A.
Subcellular location: Secreted {ECO:0000269|PubMed:26083731}.
Interaction partners:
Sequence:
MKRFLLFISILMMIGTIVVGKEGYAMDHEGCKFSCFIRPSGFCDGYCKTHLKASSGYCAWPACYCYGVPSNIKVWDYATNKCGK
Protein: T. brucei spp.-specific protein (Q38AW4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGCAPLVSGLRASVQKISEPGARGCSKGSCRTRLRSTGPCCVESFFFWTVWGVGGSCCDSRLAAIVSLLPLQWQVCGLTCFLSGVIICRRGGTGYITTRGLIVCWRHTRVYQHVVGWCGSNLTQPLKVLSHHARQRVLNRSRCIPAHMGGDVVFVLLLREATCSCIKKRKKTYKGRFQ
Protein: GSQUA2 protein (D2T2G0)
Organism: Gerbera hybrida (Daisy)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRGRVQLKRIENKISRQVTFSKRRTGLLKKAHEISVLCDADVALIVFSTKGKLFEYSTHSSMDAILERYERYSYAEKLLTAPETETQGSWTLESSKLRAKIEVLEKNIKHYVGEDLEPLNLRELQSVEQQIETALKRVRTRKNQVMHESISELHKKERSLQEQNNTLSKKLKGNQKNTEQQNVGFMFPPQPHHLAHPAIGSGSFEGGGAVREEEYSTQAHPISGTMMPPWLFHHIYQ
Protein: Acryloyl-CoA reductase (NADH) (EC 1.3.1.95) (Propionyl-CoA dehydrogenase) (G3KIM8)
Organism: Anaerotignum propionicum (Clostridium propionicum)
Function: Probable catalytic subunit of the acryloyl-CoA reductase complex involved in the pathway of L-alanine fermentation. Catalyzes the irreversible NADH-dependent formation of propionyl-CoA from acryloyl-CoA. It can also use 3-buten-2-one as substrate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12603323}.
Interaction partners:
Sequence:
MFLLKIKKERMKRMDFSLTREQEMLKKLARQFAEIELEPVAEEIDREHVFPAENFKKMAEIGLTGIGIPKEFGGSGGGTLEKVIAVSEFGKKCMASASILSIHLIAPQAIYKYGTKEQKETYLPRLTKGGELGAFALTEPNAGSDAGAVKTTAILDSQTNEYVLNGTKCFISGGGRAGVLVIFALTEPKKGLKGMSAIIVEKGTPGFSIGKVESKMGIAGSETAELIFEDCRVPAANLLGKEGKGFKIAMEALDGARIGVGAQAIGIAEGAIDLSVKYVHERIQFGKPIANLQGIQWYIADMATKTAAARALVEFAAYLEDAGKPFTKESAMCKLNASENARFVTNLALQIHGGYGYMKDYPLERMYRDAKITEIYEGTSEIHKVVIAREVMKR
Protein: 3-alpha-hydroxysteroid dehydrogenase (3-alpha-HSD) (EC 1.1.1.50) (Hydroxyprostaglandin dehydrogenase) (P23457)
Organism: Rattus norvegicus (Rat)
Function: Besides being a 3-alpha-hydroxysteroid dehydrogenase, the enzyme can accomplish diverse functions: as quinone reductase, as an aromatic alcohol dehydrogenase, as dihydrodiol dehydrogenase, and as 9-, 11-, and 15-hydroxyprostaglandin dehydrogenase.
Subcellular location: Cytoplasm.
Interaction partners:
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- 15-hydroxyprostaglandin dehydrogenase [NAD
- 17-beta-hydroxysteroid dehydrogenase type 3
Sequence:
MDSISLRVALNDGNFIPVLGFGTTVPEKVAKDEVIKATKIAIDNGFRHFDSAYLYEVEEEVGQAIRSKIEDGTVKREDIFYTSKLWSTFHRPELVRTCLEKTLKSTQLDYVDLYIIHFPMALQPGDIFFPRDEHGKLLFETVDICDTWEAMEKCKDAGLAKSIGVSNFNCRQLERILNKPGLKYKPVCNQVECHLYLNQSKMLDYCKSKDIILVSYCTLGSSRDKTWVDQKSPVLLDDPVLCAIAKKYKQTPALVALRYQLQRGVVPLIRSFNAKRIKELTQVFEFQLASEDMKALDGLNRNFRYNNAKYFDDHPNHPFTDE
Protein: Thioredoxin peroxidase 2 (EC 1.11.1.15) (Q8I5Q6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Thioredoxin-like protein
- Peroxiredoxin
- Thioredoxin 3
- NADH-cytochrome b5 reductase, putative
- Glutathione peroxidase
Sequence:
MFLKKLCRSNFFGNSRRSFSLVTKKAYNFTAQGLNKNNEIINVDLSSFIGQKYCCLLFYPLNYTFVCPTEIIEFNKHIKDFENKNVELLGISVDSVYSHLAWKNMPIEKGGIGNVEFTLVSDINKDISKNYNVLYDNSFALRGLFIIDKNGCVRHQTVNDLPIGRNVQEVLRTIDSIIHVDTSGEVCPINWKKGQKAFKPTTESLIDYMNNANKNV
Protein: Chaperonin CPN60-like 2, mitochondrial (HSP60-like 2) (Q93ZM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Heat shock 70 kDa protein 10, mitochondrial
- Heat shock 70 kDa protein 9, mitochondrial
- 20 kDa chaperonin, chloroplastic
- Heat shock 70 kDa protein 4
- GrpE protein homolog 2
- Protein groES
- Heat shock protein 90-6, mitochondrial
- T-complex protein 1 subunit alpha
- Heat shock protein 70
- 10 kDa chaperonin, mitochondrial
Sequence:
MYRVLSKLSSSIGSSTSRKLVSGRIISSRNYAAKDISFGIGARAAMLQGVSEVAEAVKVTMGPKGRNVIIESSYGGPKITKDGVTVAKSISFQAKAKNIGAELVKQVASATNKVAGDGTTCATVLTQAILIEGCKSVAAGVNVMDLRVGINMAIAAVVSDLKSRAVMISTPEEITQVATISANGEREIGELIARAMEKVGKEGVITVADGNTLDNELEVVEGMKLARGYISPYFITDEKTQKCELENPIILIHEKKISDINSLLKVLEAAVKSSRPLLIVAEDVESDALAMLILNKHHGGLKVCAIKAPGFGDNRKASLDDLAVLTGAEVISEERGLSLEKIRPELLGTAKKVTVTRDDTIILHGGGDKKLIEERCEELRSANEKSTSTFDQEKTQERLSKLSGGVAVFKVGGASESEVGERKDRVTDALNATRAAVEEGIIPGGGVALLYATKALDNLQTENEDQRRGVQIVQNALKAPAFTIAANAGYDGSLVVGKLLEQDDCNFGFDAAKGKYVDMVKAGIIDPVKVIRTALTDAASVSLLLTTTEASVLVKADENTPNHVPDMASMGM
Protein: Protein MADS AFFECTING FLOWERING 5 (MADS box protein FCL1) (MADS-box protein AGAMOUS-LIKE 68) (Q683D7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in the negative regulation of flowering time in short days, probably through the photoperiodic and vernalization pathways. Prevents premature flowering, particularly in the cv. Landsberg erecta background. In non-inductive photoperiods (e.g. short days), required for flowering through VIL2-mediated maintenance of the epigenetically repressed state of MAF5 via H3K9me2 and plant homeodomain / polycomb repressive complex 2 (PHD-PRC2)-dependent H3K27me3.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Inactive protein FRIGIDA
- VIN3-like protein 2
- Protein FLOWERING LOCUS D
- Histone deacetylase 6
- WD-40 repeat-containing protein MSI4
- Protein TWIN SISTER of FT
- Polycomb group protein VERNALIZATION 2
- Protein VERNALIZATION INSENSITIVE 3
- Protein KNATM
- Lysine-specific histone demethylase 1 homolog 1
Sequence:
MGRRRVEIKRIENKSSRQVTFCKRRNGLMEKARQLSILCGSSVALFIVSSTGKLYNSSSGDSMAKIISRFKIQQADDPETLDLEDKTQDYLSHKELLEIVQRKIEEAKGDNVSIESLISMEEQLKSALSVIRARKTELLMELVKNLQDKEKLLKEKNKVLASEVGKLKKILETGDERAVMSPENSSGHSPPETLPLLK
Protein: Nuclear movement protein nudC (Nuclear distribution protein C) (P17624)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Required for nuclear movement. May interact between microtubules and nuclei and/or may be involved in the generation of force used to move nuclei during interphase.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Nuclear distribution protein nudF
- Polo-like kinase
- Dynein light chain, cytoplasmic
- Nuclear distribution protein nudE
- Mitochondrial division protein 1
- Uncharacterized protein
- Kinesin-like protein
- Dynein light intermediate chain
- Clip 170 homolog
- 40S ribosomal protein S27
Sequence:
MSEQEPSSADLAAREAEEKQRKAAEEAEQATLPYKWTQTIRDVDVTIPVSANLKGRDLDVVLKKDSIKVKVKGENGEVFIDGQFPHPIKPSESSWTLETTSKPPGKEVSIHLDKVNQMEWWAHVVTTAPKIDVSKITPENSSLSDLDGETRAMVEKMMYDQRQKEMGAPTSDEQRKMDILKKFQKEHPEMDFSNAKIG
Protein: Monoterpene synthase like 2, chloroplastic (PbTPS-mono2) (EC 4.2.3.-) (R9QMW6)
Organism: Pinus banksiana (Jack pine) (Pinus divaricata)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MALVSAVPLDSRLCLCRTLFGLTHELKAIRRTIPNLGMCRGGKSIAPSMSMSSTTFVSSEDGVPRRIGGHHSNLWDDDSIDSLSTSYEAPSYRERADRLIGEVKDMFHLISVEDGVSTSPLNDLHHRLWMVDSVERLGIDRHFKNETNAGLDHVYSYWTEKGIGRGRESGATDLNSTALGLRTLRLHGYMVSSHVLDHFKNEKGQFTCSAIQTEGEIRDVLNLFRASLIAFPGEKIMDAAEIFSTMYLKDALQKIPPSGLSQEIEYLLEFGWHTNLPRMETRMYIDVFGEDTTFETPYLIRERLLELAKLEFNIFHSLVKRELQSLSRWWKDYGFPEITFSRHRHVEYYTLAACIANDPKHSAFRLGFAKICHMVTILDDIYDTFGTMEELELLTAAFKRWDPSSIECLPDYMKGVYMAVYDNINETAREAQKIQGWDIVSYARKSWEALFDAHMQEAKWISSGYLPTFEEYLENGKVSFGSRLTTLEPMLTLGFPLPPRILQEIDFPSNFNELICAILRLRGDTQCYKADRARGEEASSVSCYMKDHPGITEEDAVNQINALVNNLTKELNSELLRPDSGVPISYKKFYFDIWRVFHYGYKYRDGFSVASIEIKNLVTITVVETVPL
Protein: Wall-associated receptor kinase-like 2 (EC 2.7.11.-) (Q7X8C5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein kinase that may function as a signaling receptor of extracellular matrix component.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- F-box protein PP2-B13
- Transcription factor bHLH61
- Receptor-like protein 2
Sequence:
MKTETHNRQCIPLAISVLSLFINGVSSARQPPDRCNRVCGEISIPFPFGIGGKDCYLNPWYEVVCNSTNSVPFLSRINRELVNISLNGVVHIKAPVTSSGCSTGTSQPLTPPPLNVAGQGSPYFLTDKNLLVAVGCKFKAVMAGITSQITSCESSCNERNSSSQEGRNKICNGYKCCQTRIPEGQPQVISVDIEIPQGNNTTGEGGCRVAFLTSDKYSSLNVTEPEKFHGHGYAAVELGWFFDTSDSRDTQPISCKNASDTTPYTSDTRCSCSYGYFSGFSYRDCYCNSPGYKGNPFLPGGCVDVDECKLDIGRNQCKDQSCVNLPGWFDCQPKKPEQLKRVIQGVLIGSALLLFAFGIFGLYKFVQKRRKLIRMRKFFRRNGGMLLKQQLARKEGNVEMSRIFSSHELEKATDNFNKNRVLGQGGQGTVYKGMLVDGRIVAVKRSKAVDEDRVEEFINEVVVLAQINHRNIVKLLGCCLETEVPVLVYEFVPNGDLCKRLHDESDDYTMTWEVRLHIAIEIAGALSYLHSAASFPIYHRDIKTTNILLDERNRAKVSDFGTSRSVTIDQTHLTTQVAGTFGYVDPEYFQSSKFTEKSDVYSFGVVLVELLTGEKPSSRVRSEENRGLAAHFVEAVKENRVLDIVDDRIKDECNMDQVMSVANLARRCLNRKGKKRPNMREVSIELEMIRSSHYDSGIHIEDDDEEDDQAMELNFNDTWEVGATAPASMFNNASPTSDAEPLVPLRTW
Protein: Late endosome and vacuole interface protein 11 (P53246)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in vacuolar processing and morphology.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein TBF1
- Putative ISWI chromatin-remodeling complex subunit YPL216W
Sequence:
MNTALDDLHGDLVTLEDNEIINNSDHSSSHSTSHEEEDEEEDDTEDIELIEKDGNKILSSRIHPEDEIINDGLNIWIPVQMLKKNIAKFWSHFLAIEKKLTKVKCKHCGEILTRSDASLTKTFRSHLKTKHNISANKNFYSMNFTVGDSNLKNNTSSTEITRRHGYDSLTFNSDQSFKCFDIGKLQSSNYLSISQLVAIVIASENLPLNFFENVSFKSLLSKFHRIPPLTTNIIEESIIGLSKSIDELIRRSISRNDTQLPFTIHLSDSKESNQPLYLKYSREIRAQLSNLDLSHLISVNFTELAGKRSLFSLQLFDNTNKVSKGLPLSIFVRKTTDIDISVWQEQLNNLYSKYPGLQKSVISITLPQSHYTMVLENRNSHNFTFHSGSVREIKYHTCIVSELLHCFLQPLFNVPTESMLSSFSVAKENHSGGSLLDSLIDFSHIDLSSTILGKICCLIEEVNLNDSLKSDFLLYCQNYTQPNCNELTSILSCNCDRFSALKSILEKFANLVPFFKSINSHLENESLSESDFRLINTVEETLRTFEQSIEYFASSAPLKFTHTLVFIIKFELYLTEIIRSFKFTKSKKPFEKILARLLKVKDLYLLDDVNLIGAFLYPSIFQSKSLLNEIFGTTSVNKIVHNMTKIVLRYLKNFINITNFRSSNSGGESGRNSGNNLLSDYEAIFMKESRDVELLCNTKLTAPLTEDSLLVQIIRDDLLRYVNRIAHELPNAYHDYLNDNDISFDGSHFTKHELSEENDSNSGEWCLNPMEETFDIHIPISDSIWNNYISSKNKIEVIDILLQLLSVNSTSSIRSELSSLTANQDFSTKLSEETIKIKLLNSQFNLEKINFHSGSIFDAC
Protein: Liprin-beta-2 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein-binding protein 2) (PTPRF-interacting protein-binding protein 2) (Q8ND30)
Organism: Homo sapiens (Human)
Function: May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A.
Interaction partners:
- Liprin-alpha-1
- Liprin-alpha-2
- Receptor-type tyrosine-protein phosphatase S
- Liprin-alpha-3
- Receptor-type tyrosine-protein phosphatase delta
- Liprin-alpha-4
- Receptor-type tyrosine-protein phosphatase F
Sequence:
MASDASHALEAALEQMDGIIAGTKTGADLSDGTCEPGLASPASYMNPFPVLHLIEDLRLALEMLELPQERAALLSQIPGPTAAYIKEWFEESLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEEEPEGGFSKWNATNKDPEELFKQEMPPRCSSPTVGPPPLPQKSLETRAQKKLSCSLEDLRSESVDKCMDGNQPFPVLEPKDSPFLAEHKYPTLPGKLSGATPNGEAAKSPPTICQPDATGSSLLRLRDTESGWDDTAVVNDLSSTSSGTESGPQSPLTPDGKRNPKGIKKFWGKIRRTQSGNFYTDTLGMAEFRRGGLRATAGPRLSRTRDSKGQKSDANAPFAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAINTKQEEKSALLDHIWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLHVNKFNPHCLHRRPADESNLSPSEVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALIGPEAEQEKREKMASPAYTPLTTTAKVRPRKLGFSHFGNIRKKKFDESTDYICPMEPSDGVSDSHRVYSGYRGLSPLDAPELDGLDQVGQIS
Protein: GH02003p (Starvin, isoform A) (Q9VU81)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKPTVMAANQAQSNPATAAGNNVSPGGPGVNIPVNREYVSGGYGSPQQSAQFHTPQNAYGSPRQQQQHFQQHQQVPPNQQQQHFQPTFGFEPNMDMDNMFPRSHLGRMHDPFAGFGDSHFGFPRFSTMGRRGRMAGGANTHMDHDDDFFNRLPSEFRQYIPDGFGGRRGTGAAPAPGQVPQQQQPQPQPQYTQQQPQTHFQFGVPPQQQPVYAGPTQQQVPQTPSKRLCDAAIQTEDPAGRSEVDCAPPTNLNQHGLRNTVDMGVKSVAEQDQGLRSHSAPPPEQQQQNLQYHQQQQQHQQPGVHSQPFGTQTSPPVQGQQFKTYYAPHQQTHPQQKQQTPPPAPQTPGGTYVRTIPIFVEGRSEPIINAHKEIPNQNAPPSAQAQAQAQAYAQAQPQAHAAPQQHNRPTPLNTQAQPEQQVPVEGAAGLPPQTPHTLNSINKIQDIQRDVLELMGKVEQFKGTREEKEYAYLDEMLTRNLLKLDTIDTNGKDSIRLARKEAIKCIQASINVLEAKAEENARAASGAAPAPSATAPAVDTGAVAASEAAGQNAEPVTPQPQDATKMQEPIPLPAPPNAAAVEGAAASEATAAEATQSAVQSETTTTTSE
Protein: Adhesion G-protein coupled receptor F3 (G-protein coupled receptor 113) (G-protein coupled receptor PGR23) (Q8IZF5)
Organism: Homo sapiens (Human)
Function: Orphan receptor.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MVCSAAPLLLLATTLPLLGSPVAQASQPVSETGVRPREGLQRRQWGPLIGRDKAWNERIDRPFPACPIPLSSSFGRWPKGQTMWAQTSTLTLTEEELGQSQAGGESGSGQLLDQENGAGESALVSVYVHLDFPDKTWPPELSRTLTLPAASASSSPRPLLTGLRLTTECNVNHKGNFYCACLSGYQWNTSICLHYPPCQSLHNHQPCGCLVFSHPEPGYCQLLPPGSPVTCLPAVPGILNLNSQLQMPGDTLSLTLHLSQEATNLSWFLRHPGSPSPILLQPGTQVSVTSSHGQAALSVSNMSHHWAGEYMSCFEAQGFKWNLYEVVRVPLKATDVARLPYQLSISCATSPGFQLSCCIPSTNLAYTAAWSPGEGSKASSFNESGSQCFVLAVQRCPMADTTYACDLQSLGLAPLRVPISITIIQDGDITCPEDASVLTWNVTKAGHVAQAPCPESKRGIVRRLCGADGVWGPVHSSCTDARLLALFTRTKLLQAGQGSPAEEVPQILAQLPGQAAEASSPSDLLTLLSTMKYVAKVVAEARIQLDRRALKNLLIATDKVLDMDTRSLWTLAQARKPWAGSTLLLAVETLACSLCPQDHPFAFSLPNVLLQSQLFGPTFPADYSISFPTRPPLQAQIPRHSLAPLVRNGTEISITSLVLRKLDHLLPSNYGQGLGDSLYATPGLVLVISIMAGDRAFSQGEVIMDFGNTDGSPHCVFWDHSLFQGRGGWSKEGCQAQVASASPTAQCLCQHLTAFSVLMSPHTVPEEPALALLTQVGLGASILALLVCLGVYWLVWRVVVRNKISYFRHAALLNMVFCLLAADTCFLGAPFLSPGPRSPLCLAAAFLCHFLYLATFFWMLAQALVLAHQLLFVFHQLAKHRVLPLMVLLGYLCPLGLAGVTLGLYLPQGQYLREGECWLDGKGGALYTFVGPVLAIIGVNGLVLAMAMLKLLRPSLSEGPPAEKRQALLGVIKALLILTPIFGLTWGLGLATLLEEVSTVPHYIFTILNTLQGVFILLFGCLMDRKIQEALRKRFCRAQAPSSTISLVSCCLQILSCASKSMSEGIPWPSSEDMGTARS