wanglab/gogpt-training-data huggingface dataset:
Protein: Protein SSUH2 homolog (Protein ssu-2 homolog) (Q8C3L1)
Organism: Mus musculus (Mouse)
Function: Plays a role in odontogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2M2}. Nucleus {ECO:0000250|UniProtKB:Q9Y2M2}.
Interaction partners:
Sequence:
MDRDPSEEDSMADLSFEAESPVLPPDELLEGLPSYDWLLQGRERQVFFPPLEALGRSQEPACWSSVLEHSRVPVVTEEVAREALLSFVNSHCCYSSAAAGNLIIQELRQQTLCRYRLETFSESRVSEWTFQPVTNHSVDGPQRGTSPRLWDMKVQVPPMFQEDTRKLQVPHSSLVKECHKCHGRGRYKCSGCHGAGMVRCSSCSGTKRKAKQPRRCHLCSGSGRRRCSTCSGRGNKTCATCKGERKLEHFVQLVIMWKNSLFEFMSPHHLHCPKELLAKARGENLFRDENATVYPIVDFPLQDISLASQRGIEEHSTMLASRARILQQMFFYSGGPFHHS
Protein: Uracil permease (Uracil transporter) (Uracil/H(+) symporter UraA) (P0AGM7)
Organism: Escherichia coli (strain K12)
Function: Transport of uracil in the cell.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:21423164}; Multi-pass membrane protein {ECO:0000269|PubMed:21423164}.
Interaction partners:
- Cytosine permease
- Uracil phosphoribosyltransferase
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase large chain
- Dihydroorotate dehydrogenase
- Aspartate carbamoyltransferase regulatory chain
- Adenine permease AdeP
- Putative purine permease YbbY
- Guanine/hypoxanthine permease GhxQ
- Carbamoyl phosphate synthase small chain
Sequence:
MTRRAIGVSERPPLLQTIPLSLQHLFAMFGATVLVPVLFHINPATVLLFNGIGTLLYLFICKGKIPAYLGSSFAFISPVLLLLPLGYEVALGGFIMCGVLFCLVSFIVKKAGTGWLDVLFPPAAMGAIVAVIGLELAGVAAGMAGLLPAEGQTPDSKTIIISITTLAVTVLGSVLFRGFLAIIPILIGVLVGYALSFAMGIVDTTPIINAHWFALPTLYTPRFEWFAILTILPAALVVIAEHVGHLVVTANIVKKDLLRDPGLHRSMFANGLSTVISGFFGSTPNTTYGENIGVMAITRVYSTWVIGGAAIFAILLSCVGKLAAAIQMIPLPVMGGVSLLLYGVIGASGIRVLIESKVDYNKAQNLILTSVILIIGVSGAKVNIGAAELKGMALATIVGIGLSLIFKLISVLRPEEVVLDAEDADITDK
Protein: Tnfrsf21 protein (A5D8S6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPGKMSLIWSLTLLLTVVGDVLTHTLTPIPTTEKPLSPRHYHHIDPATGNKLVCDKCPAGTYVSFHCTEASVRECSPCPDGTFTRGENGVQQCHRCQRRCQAPFIEKTPCTSTTDRLCVCPPGSFSQDGKCQRHSSCLPGWGVRKRGSETEDVRCQPCQRGTFSAITSDSLRCQTHTDCPALGLTLLIKGTKKTDNVCGPNPASSVPVLLGEASVSTVSSTESAYRASTAVLPAADIQDEAEPVFSSTDMALGAQNFPTTTAYPEAIDKDGGLLIAATQDLPKSKLKLTLSRDPQLSNHQGVESISESKAQGLGYRPIRRGAPRPSSHKHFDINEHLPWMIVLLLLLVLVVIVVCSVKRSSRVLKKGPRQDPSSIMEKAIHKKPSSPAQTKERWIYYSNGQGVDILKLVAAQIGSQWIDLYKSLASATEREVAAFSNGYTADHERAYAALQHWTIRDSDANLAKLINALHRQRRIDVVDKIRSVMEDNPQVDLNKLMTAVNVSHCLSPSHKPLESPGVAVEQSPMERSRGFFPDESEPLLRCDSTSSKDSALSRTGSFITKEKKDTVLRQVRLDPCDLQPIFDDMLHILNPDELHVIEEIPMAEDKLDRLFEIAGVKSQEASQTLLDSVYSHLPDLL
Protein: Putative aquaporin-10 (Q09369)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Aquaporin-9
- Aquaporin
- Aquaporin-9
- Aquaporin
Sequence:
MEAVSSEYYFPLYSALGYFALVFGIGEIARIITAKYVSPRGNSQLFLYELIGTIQMCTCVYENGIIFKNYGFPAIFICVALLLTAGNIFNRGAMTNCAPIFEQFVFGNLGSSKFLTILSAQLIGATFASKFAYLIWNITAPYSTAHLENASNLECILHYKQTAGIVIGFEIVGAFVVRIVVAQLLARPALIKLIPFAISAYLSLALYVVGVPGLNPIVATARLYGCRGIDNSSFFILYWFCPVLGWLTGAYVVGQKSPSKKSAKDVKAEKKAKAAAKKSD
Protein: Protein spalten [Includes: Probable guanine nucleotide-binding protein spalten; Protein serine/threonine phosphatase spalten (EC 3.1.3.16)] (O15743)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in cell-type differentiation and morphogenesis. Dephosphorylates casein; in vitro. May also be involved as modulators or transducers in various transmembrane signaling systems.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:9585512}. Cell membrane {ECO:0000269|PubMed:9585512}.
Interaction partners:
- Frizzled/smoothened-like sans CRD protein F
- Ras-related protein rapC
- Frizzled/smoothened-like sans CRD protein A
Sequence:
MKKMLFMNKKEKKEEQSPAHSSLAQQHQLAQQQYQLQQQQLQLQYQQHQQQLQLAQQQKQNEQNLAQLSTSTSSNSSVNNTTNTNTNTTNSSSISSNNNNNNNTAVPILKAHDFCGTIMILGHTESGKTTLQRQLEFIYGVTDPTDAKHYQRLIYGNTLATLIRFIENSERLNITLSPDNLARVKRIQSQPVELARNRLPRFPLKLGWDCKCIWEDKVIQSVYNHSKICSEIRTPGRPKYYMDRMFKVFDPSYTPTEMDIISAYDQKDTIQSSAIIHKRFKVDLFGCSGKQSSPKNWVGLHQNYKPNYIFYVVALKDYFSDHLVATQNTDPTIVEMCNNHIHRNLLLESLNSFETLTKSELFDKSLAIYLIFNTSDIFYENIKQYDLKSCFSEYEGGNDPEKAVSFISNKFTKFLQNKDKPYKSHIVNLLDKNNVREEFEGIFDSLKIDAEKRGFTTPYNQSNSSPVSSIGSNSSRNSRLPNTSVSIPGLYSSDNDNTRLKNVNNNNNNNNNTTTYGSSTFPSSVISTTGSISNSIASAMDNDSSYSNESSPTSSMTLLPTTTTTTTTTTTTATTTDSTNNNNNNATVVIGKGKPPKEPKPVKPPKEPKPPKEPKPPKEPKPPKEPKPIKEPKEKPVKESKPPKEPKPIKEPKESKEPKEPKEPKPTKPPKEKKTSKVDGAAESKKNGADSCGNGGVGSKIKLESGFGSLQGRRKNMEDTHVILNNLMGAVTYNGPPKDIPISYYAVYDGHGGTETSTLLEPTVHNCLVNSQSFRDGDYEQAFRDAYAEADDIVIEKCEKSGSTGVSALLVGNKLYTANVGDSEIVLARAQPNANPKGPVTYEPVLLSYKHLASDDQEKKRVTDLGGMIIFNRLFGSLAVSRSFGDKEYKEGEKKFCVSDPYQTTTDLTARDHFFILACDGLWDKVEYDEAVQFVQRNIKLGKSATEISELLAQDSYDRGSGDNITVLVVILNWN
Protein: Uridine kinase (EC 2.7.1.48) (H2L2A8)
Organism: Caenorhabditis elegans
Interaction partners:
- Uracil phosphoribosyltransferase homolog
- Cytidine deaminase
- Cytidine deaminase
- Probable uridine-cytidine kinase
- Uridine and thymidine phosphorylase
- UMP-CMP kinase 2
- Uridine 5'-monophosphate synthase
- UMP-CMP kinase 1
- Nucleoside-diphosphatase mig-23
- Nucleoside-diphosphatase uda-1
Sequence:
MSKRRSRVLQRTTRMVAEKRDANVAASKGDANRKSVKIEDCPTYSHSSGSSVNEMVNQSGGDSEDSTSPRAAGCRTRRRTMSGGRAEHHLLTTKTGKKIYTKGRPPWYDKKGKSLKHPFVIGVCGGSASGKTTVAEKIVERLGIPWVTILSMDSFYKVLTPEEIKAAHESRYNFDGPNAFDFDLLYEVLKRLREGKSVDVPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDGIMEQYFTFVKPAFDKYIAPCMDSADLIVPRGGENDVAIDMIVQNVMAQLVERGYDRNQNNRDRHDLVRDDLPDCLPENLFILKETPQVKGLVTFVRDRETSRDNHIFYSDRLMRILIEECMNHMPYKDVEIEMAGGRKTIGKRKDAQICGLPIMRAGECMETALRSIVKDCVIGKILIQTNETTFDPELHYIRLPPHITRYKVIIMDATVTTGSAAMMAIRVLLDHDVKEEDIFVASLLMGQQGAHALAYAFPKVKLITTAMDHQMTENCYLIPGMGNFGDRYYGTGLEQDMDEPFDM
Protein: Olfactory receptor (Q7TQU8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MERENQTGERNFLLLGFTEDSDLQSFFFGLLLSMYLVTITGNLLIIVAIISDPHLHMPMYLFLSNLSIADIGFTSTTIPKVLQNIRTQSKFISFSGCITQIFFFIVFGCLDNLLLSVMAYDRFVAICHPLHYVVIMNSCFCAMLALGSWIVSVMSSLPETLTVLRLSFCTNMEIPHFFCDLPEVLKLACSDTLVNNIVTYSITIVIAGFPFSGILLSYSKIFSSILRIPSAGGKYKAFSTCGSHLLVVFLFYSNGLGVYLSSAATSSSRMSLVASLMYSIVTPMLNPFIYSLRNKDMQKALGKLLRKIMLLGEGTMVGLP
Protein: Bradykinin-potentiating and C-type natriuretic peptides (BPP-CNP) [Cleaved into: Bradykinin-potentiating peptide 6a (BPP-6a); Bradykinin-potentiating peptide 10a (BPP-10a) (Bradykinin-potentiating peptide IV-1-A) (BPPIV-1-A) (Bradykinin-potentiating peptide V-8); Bradykinin-potentiating peptide 13a+QQWA (BPP-13a+QQWA); Bradykinin-potentiating peptide 13a+QWA (BPP-13a+QWA); Bradykinin-potentiating peptide 13a (BPP-13a) (Bradykinin-potentiating peptide III-1-A) (III-1-A) (Bradykinin-potentiating peptide V-9); Bradykinin-potentiating peptide 10c+QQWA (BPP-10c+QQWA); Bradykinin-potentiating peptide 10c (BPP-10c) (BPP-2) (Bradykinin-potentiating peptide IV-1-Bbeta) (BPP IV-1-Bbeta) (Bradykinin-potentiating peptide V-7); Bradykinin-potentiating peptide 10c-F (BPP-10c-F); Bradykinin-potentiating peptide 11b (BPP-11b) (Bradykinin-potentiating peptide IIa) (BPP-IIa); Bradykinin-potentiating peptide IIb (BPP-IIb); Bradykinin-potentiating peptide 5a (BPP-5a) (Bradykinin-potentiating peptide Va) (BPPVa) (Proline-rich peptide 5a) (Bj-PRO-5a) (PRO-5a); Poly-His-poly-Gly peptide 1 (pHpG-1); C-type natriuretic peptide (Bj-CNP)] (Q6LEM5)
Organism: Bothrops jararaca (Jararaca) (Bothrops jajaraca)
Function: Modestly inhibits ACE (with highest affinity for the N-site) and reveals strong bradykinin-potentiating activity. Induces nitric oxide (NO) production depended on muscarinic acetylcholine receptor M1 subtype (CHRM1) and bradykinin B2 receptor (BDKRB2) activation. Both these receptors contribute to the vasodilation induced by this peptide that may have an indirect action on BDKRB2 and a direct agonistic action on CHRM1.
Subcellular location: Secreted {ECO:0000269|PubMed:18200607}. Cytoplasm, cytosol. Note=BPP-10c is internalized in the cytosol of prey cells.
Interaction partners:
Sequence:
MVLSRLAASGLLLLALLALSVDGKPVQQWAQSWPGPNIPPLKVQQWAQGGWPRPGPEIPPLTVQQWAQNWPHPQIPPLTVQQWAQGRAPGPPIPPLTVQQWAQGRAPHPPIPPAPLQKWAPLQKWAPLLQPHESPASGTTALREELSLGPEAASGVPSAGAEVGRSGSKAPAAPHRLSKSKGAAATRPMRDLRPDGKQARQNWGRMAHHDHHAAAGGGGGGGGGARRLKGLAKKGAAKGCFGLKLDRIGTMSGLGC
Protein: Growth hormone (A4LAP1)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
FPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDGTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
Protein: ArfGAP with dual PH domains 1 (A0A0G2K7U5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Kinesin family member 13B
Sequence:
MAGERRRALLELLTRPGNSRCADCGAPDPDWASYTLGVFICLSCSGIHRNIPQVSKVKSVRLDAWDETQVEFMTSHGNEAARATFESKVPPFYYRPTFSDCQLLREQWIRAKYERQEFLHVEKQEPYSTGYREGLLWKRGRDNGQFLSRKFVLTEREGALKYFNKNDAKEPKAVMKIEHLNATFQPAKIGHPHGLQVTYLKDNSTRNIFIYHEDGKEIVDWFNALRAARFHYLQVAFPGASDADLVPKLSRNYLKEGYMEKTGPKQTEGFRKRWFTMDDRRLMYFKDPLDAFARGEVFIGSKESGYTVLEGLPPSTQSHHWPHGITIVTPDRKFLFTCETESDQREWIAAFQKVVDRPMLPQEYAEKPAHENIQ
Protein: Type I interferon 1 (A8KCK1)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MYTMQSWSCIFLIICSMQSVCHCCDWIRHHYGHLSAEYLPLLDQMGGDITKQNAPVLFPTSLYRHIDDAEFEDKVIFLKETIYQITKLFDGNMKSATWDKKNLDDFLNILERQLENLNSCVSPAMKPERRLKRYFKKLNSKVLRKMNYSAQAWELIGKETKRNLQRLDILAAQMY
Protein: Lipid A 1-phosphatase (EC 3.1.-.-) (B2RLI7)
Organism: Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Function: Removes the 1-phosphate group from lipid A species. Absence of phosphate groups in lipid A renders the bacteria resistant to host-derived cationic antimicrobial peptides (CAMP) and allowing it to camouflage itself from the host innate immune response.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
Sequence:
MNRESFLLLLVLLFALPLHLQASSPCNNMADTTCISDSAKMFPPAIGVYHVKPMKNTLRHSLPLVAASLLTFNVDDNIRELRFTGAGSFHTKIDNVSQLVPLMAQLSMRGFGYKGRSKSWGKMLVSDALGMALMGGMVNAGKYSFGRLRPDGTAANSYPSGHTATAFACATLFHLEYGSRSPWYSVAGYTVASFTGISRIVNNRHWASDVLCGAAVGILVGELGYWISDLIFRDPTGYNYKLTKKQEGTLESMVISLSTGNRYINRQMDFEGKTVERTDAFGMNLKTTFNPSFARWVRIGLQFSVSTEKQKGLTRERPAKVFVAPAISLGLSAGVEWHPWQRASVWAEILPSILFRTDFTNAQDKPDEMSSKLHRRSSFQPAFQVGVAYRVSDHMGIEAHAGYQLGEAVYHLMEETSTWSIIKKRATVPYRGFEFAVGLQFYPFR
Protein: Aspartate carbamoyltransferase, chloroplastic (EC 2.1.3.2) (Aspartate transcarbamylase) (ATCase) (P49077)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Carbamoyl phosphate synthase small chain, chloroplastic
- Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic
- Argininosuccinate synthase, chloroplastic
- Uridine 5'-monophosphate synthase
- Dihydroorotase, mitochondrial
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase
- Ornithine transcarbamylase, chloroplastic
- Dihydropyrimidinase
- Adenylosuccinate synthetase, chloroplastic
Sequence:
MSIASSLTSATLCGASVFPKALACSSEFPINLPSPFESSKICLTSFPASRDLKKNATLNLTRNVGPVRCHAMQAGTRELKKFELSDVIEGKQFDREMLSAIFDVAREMEKIEKSSSQSEILKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENAREFSSAAKGETLEDTIRTVEGYSDIIVMRHFESGAARKAAATANIPVINAGDGPGEHPTQALLDVYTIQSEIGKLDGISVALVGDLANGRTVRSLAYLLAKFKDVKIYFVSPEIVKMKDDIKDYLTSSGVEWEESSDLMEVASKCDVVYQTRIQRERFGERLDLYEAARGKYIVDKDLLGVMQKKAIIMHPLPRLDEITADVDADPRAAYFRQAKNGLFIRMALLKLLLVGW
Protein: Butyrophilin subfamily 3 member A1 (CD antigen CD277) (O00481)
Organism: Homo sapiens (Human)
Function: Plays a role in T-cell activation and in the adaptive immune response. Regulates the proliferation of activated T-cells. Regulates the release of cytokines and IFNG by activated T-cells. Mediates the response of T-cells toward infected and transformed cells that are characterized by high levels of phosphorylated metabolites, such as isopentenyl pyrophosphate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21113407, ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}; Single-pass type I membrane protein {ECO:0000269|PubMed:21113407, ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}.
Interaction partners:
- Butyrophilin subfamily 3 member A2
- Xanthine dehydrogenase/oxidase
- Butyrophilin subfamily 3 member A3
- Periplakin
- Perilipin-2
- Importin subunit alpha-8
- Lactadherin
- Interleukin-1 family member 10
Sequence:
MKMASFLAFLLLNFRVCLLLLQLLMPHSAQFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELKWVSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSDLHVDVKGYKDGGIHLECRSTGWYPQPQIQWSNNKGENIPTVEAPVVADGVGLYAVAASVIMRGSSGEGVSCTIRSSLLGLEKTASISIADPFFRSAQRWIAALAGTLPVLLLLLGGAGYFLWQQQEEKKTQFRKKKREQELREMAWSTMKQEQSTRVKLLEELRWRSIQYASRGERHSAYNEWKKALFKPADVILDPKTANPILLVSEDQRSVQRAKEPQDLPDNPERFNWHYCVLGCESFISGRHYWEVEVGDRKEWHIGVCSKNVQRKGWVKMTPENGFWTMGLTDGNKYRTLTEPRTNLKLPKPPKKVGVFLDYETGDISFYNAVDGSHIHTFLDVSFSEALYPVFRILTLEPTALTICPA
Protein: Eukaryotic translation initiation factor 2D (eIF2d) (Hepatocellular carcinoma-associated antigen 56) (Ligatin) (P41214)
Organism: Homo sapiens (Human)
Function: Translation initiation factor that is able to deliver tRNA to the P-site of the eukaryotic ribosome in a GTP-independent manner. The binding of Met-tRNA(I) occurs after the AUG codon finds its position in the P-site of 40S ribosomes, the situation that takes place during initiation complex formation on some specific RNAs. Its activity in tRNA binding with 40S subunits does not require the presence of the aminoacyl moiety. Possesses the unique ability to deliver non-Met (elongator) tRNAs into the P-site of the 40S subunit. In addition to its role in initiation, can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20566627}.
Interaction partners:
- Eukaryotic translation initiation factor 1
- Density-regulated protein
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS4, X isoform
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein eS7
Sequence:
MFAKAFRVKSNTAIKGSDRRKLRADVTTAFPTLGTDQVSELVPGKEELNIVKLYAHKGDAVTVYVSGGNPILFELEKNLYPTVYTLWSYPDLLPTFTTWPLVLEKLVGGADLMLPGLVMPPAGLPQVQKGDLCAISLVGNRAPVAIGVAAMSTAEMLTSGLKGRGFSVLHTYQDHLWRSGNKSSPPSIAPLALDSADLSEEKGSVQMDSTLQGDMRHMTLEGEEENGEVHQAREDKSLSEAPEDTSTRGLNQDSTDSKTLQEQMDELLQQCFLHALKCRVKKADLPLLTSTFLGSHMFSCCPEGRQLDIKKSSYKKLSKFLQQMQQEQIIQVKELSKGVESIVAVDWKHPRITSFVIPEPSPTSQTIQEGSREQPYHPPDIKPLYCVPASMTLLFQESGHKKGSFLEGSEVRTIVINYAKKNDLVDADNKNLVRLDPILCDCILEKNEQHTVMKLPWDSLLTRCLEKLQPAYQVTLPGQEPIVKKGRICPIDITLAQRASNKKVTVVRNLEAYGLDPYSVAAILQQRCQASTTVNPAPGAKDSLQVQIQGNQVHHLGWLLLEEYQLPRKHIQGLEKALKPGKKK
Protein: Homeobox protein 4 (DdHbx-4) (Q86IH1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Putative transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein 3
Sequence:
MNTVEENNTKITDNNNNNNNNNNNNNNNNNNNKNNDGENLSQQLIDSNNKKLRSPIQVYFDSDVSSCSLQSQSSPQQLPTQQPIQQQINNIFNHFLPQNQAPLLQAQNQQPINNINQVSNFQIQPIPLTFQLPNNINTNTNNTNMINNVQQFQNNFLNNNDFSLTDPVPSPFVLFNNNNNNNNNNNNNNNNNINNFHHNNINNNFDNNNSNYNTINTHPNNTNNNSSNINQIQSNIYPQQNLHNPFLPIHNNNNINNNNINKNNNNYNNNNNNKNNNNNNNNNNNNNNPQLFSMEPPNGFNHSTTDNTSSVSSVPSNKKKSSKTKQKSKPLTIQQQQQHKSNYHQQPNQNSQHLQSKPNSPILISSPLNSQQNSSPPQPSPTQSFLSPPQYSQSPQNNNFNNNNNNISNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINNSTNNNNNNSNTNNNTNTNTNNNNNKNNNNNNNNEIENNNNEELILLWYNSIIKNIIVDENHFKIENQFNKENGYLVFKQLFKNHFGSIGTIGKEMAEYIQLHCEVMNEITELSKFHFQSIDNFYNNYIRIINGYSLIPAKDSGATIKARPKKGAKLSKESKDILENWIKNHIAHPYPTNDEKEQLQRQTGLTPNQISNWFINTRRRKVPTLCDEAGIITNSNVMPQMTINNNNNNGGNSNFKNNNNNTITTTSTSNNNNNNNNNNHNEMECDDGENEESSEYDD
Protein: Protein Spindly (hSpindly) (Arsenite-related gene 1 protein) (Coiled-coil domain-containing protein 99) (Rhabdomyosarcoma antigen MU-RMS-40.4A) (Spindle apparatus coiled-coil domain-containing protein 1) (Q96EA4)
Organism: Homo sapiens (Human)
Function: Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Plays a role in cell migration.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Nucleus. Cytoplasm, cytoskeleton, spindle pole. Note=Localizes to the nucleus in interphase and to the kinetochore in early prometaphase. Relocalizes to the mitotic spindle pole before metaphase and is subsequently lost from the spindle poles after chromosome congression is completed. Removal of this protein from the kinetochore requires the dynein/dynactin complex.
Interaction partners:
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Centromere protein F
- Spindle and kinetochore-associated protein 3
- SKA complex subunit 1
- Spindle and kinetochore-associated protein 2
- Biorientation of chromosomes in cell division protein 1
- Serine/threonine-protein kinase PLK1
- Cell division cycle protein 20 homolog
- Kinetochore protein NDC80 homolog
- Homeobox protein Hox-D13
Sequence:
MEADIITNLRCRLKEAEEERLKAAQYGLQLVESQNELQNQLDKCRNEMMTMTESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTEFEQQERLLAMLEQKNGEIKHLLGEIRNLEKFKNLYDSMESKPSVDSGTLEDNTYYTDLLQMKLDNLNKEIESTKGELSIQRMKALFESQRALDIERKLFANERCLQLSESENMKLRAKLDELKLKYEPEETVEVPVLKKRREVLPVDITTAKDACVNNSALGGEVYRLPPQKEETQSCPNSLEDNNLQLEKSVSIYTPVVSLSPHKNLPVDMQLKKEKKCVKLIGVPADAEALSERSGNTPNSPRLAAESKLQTEVKEGKETSSKLEKETCKKLHPILYVSSKSTPETQCPQQ
Protein: Reversed polarity (Q24477)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MEHDSFDDPIFGEFGGGPLNPLGAKPLMPTTTAMHPVMLGSVHELCSQQQQQQQQQRLPDCNTILPNAVGGGAGSGGAGGSPNYVTKLDFVNKMGCYSPSQKYEYISAPQKLVEQQQQQQHHHQHHQHYTATPPPSHNGILLHKQSSQQQQQQQQQLVGILDYHPLNGKLDYSSSPKDQYEPQQLQHLYGGSPHHLDHLDHGSDGLLQDSSPVMINGGSAGGKLKKPDEMCSQLEAGGAGVTPPSSSSTVVNGTTNGTGNANSSSSAGVGIQGAAGTAGGVAAPAAKKDGSSSKKKGDPNGIKKKKTRTTFTAYQLEELERAFERAPYPDVFAREELAIKLNLSESRVQVWFQNRRAKWRKHEPPRKTGYIKTSTPPTATLNPGTLAPPFTSYPQTTTVTPPGSMDSWTSYQTPYELTPQFSLLSPAASPYGTYSGQYGAYVHESQLFPMRHYEYGSPTRMEMGATTGSVAGNGDESVANGGSYQTAELQTAQQQQLADGTLVTVHAHQQQQQQQQQLNGKYLSAEEAKYVHLQCHQSGGGLELSPGASCHLVEAQGQHYVTTATGGAASAGGTSSDDNDSGGMQTVIKSEEVSQQQQQQQGQSYVLPPFLH
Protein: RNA editing complex protein MP63 (Q38AE3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-editing ligase 2, mitochondrial
- RNA editing associated helicase 2
- MP18 RNA editing complex protein
- RNA-editing ligase 1, mitochondrial
- REH2-associated factor 1
- RNA editing complex protein MP46
- RNA-editing-associated protein 1
- RNA editing 3' exouridylylase MP99
- RNA editing complex protein MP61
- REH2-associated factor 2
Sequence:
MYRRFFRSAAVKHLGTTSAQCLMRATKYPCGAMCRNASSCHPQTLGYQQRFQSTTDKKFHCSVCKKPFRLEMAAKLHLQQAHGGDGSVEAGPGPGVEASSVNVVSTPVPSPISPVERTFVDEEERRPRRMRPTPKPLHQPDRDIPAAAMEEMLGVWDKIGLNRLEGNFVHSTMVMKVFAAPPDVSEIPLYEHVAPEGENPFDSLDHMTTGTVDATYVGHDAFAEVDLVDPFVAAPDQTLNPFRAGKVRNPFTRISPTQREVVKPLQPPQPKEEPLKAPVTPFGQLPMFGQTREPSASFAAAAVSVQAAANPNEVSSPFAAAVSSSPFVGQVASPFAPAQDVAGSPFEASPCAASSPFVTAGGQETSPFAAPSTPASFGQGSLFPPMGTGAPGFTAITETEQRQQELEHGCPTCGKKFSTFEGAAMHSKSKHGIVLESKKVKDRLNRKGVPDLPAYVPSPVDLSSTSPFGTRSAIGASWAETELIPHAQCVSNITIVGRVLDVSQASENVSHVTVFVEGERSGEEETLTLCCFGEVSQKIRGTLKRNATIFASGTLRLHPVYEASNNKYYVSPVVHVSMPTGTLAVIT
Protein: LD46360p (Q8MRH4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRRRSERKKSSSPAPVPVAVARRSRRSRKVSENEKTEVETPVVAQNNEAECPKVPPASQEINEARASSEERAGSGASPVRRSRGSRTTPRKRTESKGGDKKVDTIPEEEPENGKDVEKDAVEEEKTVAPPAANESESEDRAKTEDQQAQDDESCAEPAVVKDDDVEKEDLKPQQEVPTSTDDDTKQSEPEQEVKVPSPSSKDEEHLKTTSDVLDIQTEEVDERDEEASAPAERRETKKRHKEQIKEQQPAEEEEHKENHKQIDENPEQIHDEPADLSNDKHDPCLNSSATNTTGAPVLQQQRSVRKRKWLTNKKSSDRTPPVLAISTDSLKNIIADVVQPVPLSDVQLESSSEEEGLVTSDRDSERSASPAPPSEASKDRDNKGNTANTCDTTAEASADNEGAGAAPPAAADTVSAQVSLSKATVSTAAPHIVRDPSPARNRASHVLYITNLVRPFTVLQLKGLLARTGKIVEEDGFWIDRIKSKCYVAYSTEDEAIETRHALHGVRWPVSNPKCLNVDFGSRTDMDRAILSTKDEAPRYGQENTRDNQQSGNAWSRLEPSDKKTCATCTRMGCWQKGTKRPRQTQQRQASGQQGSTGLEV
Protein: D-3-phosphoglycerate dehydrogenase (3-PGDH) (EC 1.1.1.95) (2-oxoglutarate reductase) (EC 1.1.1.399) (Malate dehydrogenase) (EC 1.1.1.37) (O43175)
Organism: Homo sapiens (Human)
Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate.
Interaction partners:
- Phosphoserine aminotransferase
- Phosphoglycerate mutase 1
- Phosphoserine phosphatase
- Serine hydroxymethyltransferase, mitochondrial
- Probable phosphoglycerate mutase 4
- Bisphosphoglycerate mutase
- Phosphoglycerate mutase 2
- Transportin-1
- Glyceraldehyde-3-phosphate dehydrogenase
- Serine hydroxymethyltransferase, cytosolic
Sequence:
MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMRAWAGSPKGTIQVITQGTSLKNAGNCLSPAVIVGLLKEASKQADVNLVNAKLLVKEAGLNVTTSHSPAAPGEQGFGECLLAVALAGAPYQAVGLVQGTTPVLQGLNGAVFRPEVPLRRDLPLLLFRTQTSDPAMLPTMIGLLAEAGVRLLSYQTSLVSDGETWHVMGISSLLPSLEAWKQHVTEAFQFHF
Protein: SIX homeobox 3 (A0A8I6G4X0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MNIYPPLLHAPGFSYLSAGQSMVFRSPLDLYSSHFLLPNFADSHHCSLLLASSGGGSGAGGGGGAGGGGGGGGGNRAGGGGAGGAGGGGGGGGGGSRAPPEELSMFQLPTLNFSPEQVASVCETLEETGDIERLGRFLWSLPVAPGACEAINKHESILRARAVVAFHTGNFRDLYHILENHKFTKESHGKLQAMWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRSLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHQAIGPSGMRSLAEPGCPTHGSAESPSTAASPTTSVSSLTERADTGTSILSVTSSDSECDV