wanglab/gogpt-training-data huggingface dataset:
Protein: Protein lifeguard 2 (Fas apoptotic inhibitory molecule 2) (Neural membrane protein 35) (O88407)
Organism: Rattus norvegicus (Rat)
Function: Antiapoptotic protein which protects cells uniquely from Fas-induced apoptosis. Regulates Fas-mediated apoptosis in neurons by interfering with caspase-8 activation. Plays a role in cerebellar development by affecting cerebellar size, internal granular layer (IGL) thickness, and Purkinje cell (PC) development (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12414123}; Multi-pass membrane protein {ECO:0000269|PubMed:12414123}. Membrane raft {ECO:0000250}. Postsynaptic cell membrane {ECO:0000269|PubMed:12414123}.
Interaction partners:
Sequence:
MTQGKLSVANKAPGTEGQQQANGEKKDAPAVPSAPPSYEEATSGEGLKAGAFPQGPTAVPLHPSWAYVDPSSSSGYEGGFPAGHHELFSTFSWDDQKVRQLFIRKVYTILLVQLLVTLAVVALFTFCDVVKDYVQANPGWYWASYAVFFATYLTLACCSGPRRHFPWNLILLTIFTLSMAYLTGMLSSYYNTTSVLLCLGITALVCLSVTIFSFQTKFDFTSCHGVLFVLLMTLFFSGLLLAILLPFQYVPWLHAVYAVLGAGVFTLFLAFDTQLLMGNRRHSLSPEEYIFGALNIYLDIIYIFTFFLQLFGTNRE
Protein: von Willebrand factor A domain-containing protein DDB_G0292188 (Q54DL7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- DUF7788 domain-containing protein
- Transmembrane protein
- WW domain-containing protein
- von Willebrand factor A domain-containing protein DDB_G0292028
- EGF-like domain-containing protein
- C2 domain-containing protein DDB_G0290753
- EGF-like domain-containing protein
- Vegetative-specific protein H7
- Uncharacterized protein
- GRAM domain-containing protein
Sequence:
MFTENQNNNQRHALKTEIKTVFNSDSGVTYFSILIETSSKMSLYNVIIKTFITQLQKANRECQIQIITYGDSVNTIFEFDSEPNELKDSLKEIKFSKDNEEAKLGEAMRMCFNNIESNWSSDLMSKIIIISSGQSTDDSSDDLVDILSLDNNSIYGLAGCNLANKSSDEAVKDLQSLLPDQKVIPLGKNPSQDIRLLMNGGGGAANGGGAANGASSSDEHSINCPVNIEVYPHTNETKSIKDDLLLDVVIKPDGNTASVPSGTKIKFLSNKYYSGYTIQLKQNLVFGEPYEETIKLEFKKGQMEKTQFENFPSKIIFHIELANDRDNVHEGFVALNISYFLGELKSKYRCCIGVEGEIGNGKSTCLNGFVNLFNPVGELEEYFNANRTSGTHVTTSINNTSLKEILSAKHYIHPVQESFHDIDIAWSDSWGFVDTDVQLRHKAEGRIHHGTKKDECTILQPDDRYRIDCFIFVVSIRNFTNPASMQRIEKKIKEVLQMNITPLLAITFSDTLSKNQLQDVMKNKVAELSVQESNTFIISNYTEKETHKDISKDVQYLRLLTKAVQLCKVKNEKDIMNKVKGISNLSINDNNNSFNQTPIKNQPFFESSSTSSPSPAFFRSPIQQQQQQTSTTSTQSPSPSSSSASTPPPPSQMLNEQPSKTINVTIDVVTDSSGTVLTSFEIESSTNESVSELKCKLINEIDPEMNANDWSITKESGTVLFESARLSSIIKSFDNSDSIKLVLKKKQKLF
Protein: Calcium-activated potassium channel subunit beta-4 (BK channel subunit beta-4) (BKbeta4) (Hbeta4) (Calcium-activated potassium channel, subfamily M subunit beta-4) (Charybdotoxin receptor subunit beta-4) (K(VCA)beta-4) (Maxi K channel subunit beta-4) (Slo-beta-4) (Q86W47)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Decreases the gating kinetics and calcium sensitivity of the KCNMA1 channel, but with fast deactivation kinetics. May decrease KCNMA1 channel openings at low calcium concentrations but increases channel openings at high calcium concentrations. Makes KCNMA1 channel resistant to 100 nM charybdotoxin (CTX) toxin concentrations.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Calcium-activated potassium channel subunit alpha-1
- Potassium channel subfamily U member 1
- Small conductance calcium-activated potassium channel protein 3
- Intermediate conductance calcium-activated potassium channel protein 4
- Small conductance calcium-activated potassium channel protein 2
- Calcium-activated potassium channel subunit beta-1
- Small conductance calcium-activated potassium channel protein 1
- Calcium-activated potassium channel subunit beta-2
- cGMP-dependent protein kinase 1
- Calcium-activated potassium channel subunit beta-3
Sequence:
MAKLRVAYEYTEAEDKSIRLGLFLIISGVVSLFIFGFCWLSPALQDLQATEANCTVLSVQQIGEVFECTFTCGADCRGTSQYPCVQVYVNNSESNSRALLHSDEHQLLTNPKCSYIPPCKRENQKNLESVMNWQQYWKDEIGSQPFTCYFNQHQRPDDVLLHRTHDEIVLLHCFLWPLVTFVVGVLIVVLTICAKSLAVKAEAMKKRKFS
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (H0Y3C5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
LGGRSSCEDPGCPRDEERAPRMGCMKSKFLQVGGNTFSKTETSASPHCPVYVPDPTSTIKPGPNSHNSNTPGIREGSEDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIPSNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSYSLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVPCMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDFYTATESQYQQQP
Protein: Two-component response regulator ORR5 (OsRR5) (OsRRA4) (Q2HWH1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22383541}. Nucleus {ECO:0000269|PubMed:22383541}.
Interaction partners:
Sequence:
MATCRSRGVERGGAPHVLAVDDSSVDRAVISGILRSSQFRVTAVDSGKRALELLGSEPNVSMIITDYWMPEMTGYELLKKVKESSRLKEIPVVIMSSENVSTRINRCLEEGAEDFLLKPVQPSDVSRLCSRVLR
Protein: Uncharacterized protein (Q54GR0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- RRM domain-containing protein
- Methyltransferase type 11 domain-containing protein
- Methyltransferase type 11 domain-containing protein
- Cation-transporting P-type ATPase C-terminal domain-containing protein
- SAP domain-containing protein
- Uncharacterized protein
- J domain-containing protein
- DH domain-containing protein
Sequence:
MINEEEEDDEFLINNTQFKPPDRSTSAPPSLTRLNSNSLFSFRANEFINDIRADEQYYEFYINHVNQDKLPPPLEIQQSFYNAPEPESDFSGTSRNAFFQEYFKQPVLNIPQPQQFYQKPPIPQTQQTQQPQQYYQPIPQQPQIQQPIPHKPPQQQQQQQTPQPPYLQRQPSFGNAPIGYPLPQQQQQAYQQQQQQLLQQQQQLLQQQQQQQQLQQQQLLQQQLQQRQLLQQQQQRQQQQQQQYLQQQQQFNNSNNNNNSSHHHHQQQQQQQQQQQNGNNDLWAVQSELYSLKMNDGKPDDYIVKSSFDVAFSTVNQFFDEPRSNSNSLPRSTSNSSLNQIFEPQLRNSNINSNNNNNNSNNNNNKQPPQPPQSNGVSGNGAIVRPIAKVGNNLLHSPIDLNQFSNFNGNMNGTTSNNNNNNNNNNNNNNNNNNNSNNNSNNNGNGNSNSNSSNNNNTVHPARTPTPPQSSGNSTSPSQHCRYFTQGYCSKGSKCNFVHDSETSSEKVEEKQQNVSPITSTNNNNNNSSSSNNNTNTNNNHNNSNNNNNNSVNNSNSNSNSSNNNNNNNNNNNNNNNNSNNNNSNNSNSNNNNKQNNRNNNNNNNNSNNNNNNSNNNSTNSNNTQNNNNNTQSRKSLPVELQPSNIMQLTKVQPHSKQQQGGRGRNNPMMQNQQQMAQLSITSPPITDPITSDISKKIDLIANKTYTSIDQVMGSIYPLCRDQHGCRFLQKKLEESDLQLTEIIFKEVCDYMLELMTDPFGNYLCQKLLEHCNDRQRLTIIEKVGTDIVRISMNMHGTRAVQKMIEYLTTPEQIQLIKRSLKDSVVPLIQDLNGNHVIQKCLNKLSPQDNQFIYDAVSSDGSCIAVATHRHGCCVLQRCIDHASESQKLQLIQEVIANSLVLVQDPYGNYVVQYVLDLPFQGLATEMAKRFVGHVPILATQKFSSNVVEKCLHVADAITRGYLIQEVIDYDNLLHLLQDPYANYVIQTSLTISEPHQHTKLVEAIRPHLPLLKNTPYGKRIQNKIIKEGRDTYNFN
Protein: Protection of telomeres protein 1 (Q7Z862)
Organism: Emericella nidulans (Aspergillus nidulans)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVSQGPRLPPNYVNVDDAIVRRGVLSVMGVVVDIMGGTAYRTNGTSMCITFTIKDQNLYNGHVWDGLRIKYFKESEPLLPPVQEGDVILLRDLRIKIWNGKVLGVAPQDRIIPWAVFRPDRDPTAHLPALTGPSPFEPTYQEKTYAATLLEASPGAFRSVTVTRPSLAQVSASRPASTAKKFSLLQDIQDGQFVDLIGEIIKIYGNDSEKATLYLTDYTKNENLFLYASDDDDDSGHGREGDPYGYIQRQKKNWNGPVGRMSIQITLWEPHASFVRGNFNIGDIVRLKNVKIKWSRVEQGSLEAVVHGNRANPGETNAFPVDSNNDPRVQQLLARREAYWNARPKKQKRKPNEDNERPSKKPNKKQSKVAPKKESGQTILDIKKRMAVNEHVEPRVPPSGVHAQSLEAILNNPAHDNTSTSGIRYRLPFQNLCYLTTVRVVDFYPPLLEDFAVHKEQVSLAYNRKRDPASRTFRIWEWRFCLLVEGSFPATVGQSNERAKLFVSNYEAEHLLQLNAVDLRRHSEVLGQLREKLFILWGDLEERKRRAIEAGNKSLDIGPVSSKPFNCCIMEYGVKCSHPRDSNKCHNGRSYGCTDRDCFGWERRFGLLKTTIHG
Protein: Uncharacterized protein (Q4GZG0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMQVKLKHFDEGQSWTEKRNSTAAAAAAAAGASAPGGGNSGMPKSFSVCTVDAANASSSAADAEALGRILSGSSPSFVFIHNCNAATRRQLMQLSSVRKFYGITDNIRYEPREPTERGTVTLVRIGMTCESVENVTKELEISNNTNGESEGSTSHSSVASAVKLFMTLQVRSFPGASVTVGMLYMDPGAQPWVRTAALSSIIPLLGSAEVIVICANLLTSTTTLNEEICAACNSYGFADATEDAVEKPVSPGSSASHRDWGLWVKSSKLCVTSCAPSFHEGERCVFTSLMAVVGPRSPAGIAIPQPRSAKSANPRGSPWSPAAPPVITDPAILSAEAGSRTGSVQAIKGGGSAIIERLLQQQQQQQQQFTTRWRASSTCPIKNNDKLTREEQAFDVSSHFTSIQEAVDALNSKTIHWPADFCVVCDTILFSDAVGQGDKRTAFRRYAKEYKNSSTLLAQMIVASGAANNPTTNATAEKSAWLKRALATQNHKSADREEKAGSVSTGPAVKREEEHRVRVWDAAWCTVVYQVTPREMKFNVTHLVGLGKDNLAEAIQFLNARALPKGGKAANGRENPLQNYPYDYALLFSWELQGFWLIAATDVPCDIVACRAAA
Protein: Tyrosine--tRNA ligase (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (Q9VV60)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- leucine--tRNA ligase
- leucine--tRNA ligase
- Glycine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Probable glutamine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, cytoplasmic
Sequence:
MVGITPAEKKALITRNLQETLGDDKLTKILAERDLKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWSLLELRTKYYEQVIKAMLSSIGVPLEKLKFVKGSDYQLSKEYTLDVYKLSSVVTQHDAKKAGAEVVKQVEYPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFSEKYLPQLGYEKRIHFMNPMVPGLAGGKMSSSEEDSKIDLLDSPANVKKKLKKAFCEPGNIADNGLLSFVKHVLFSLFKEGEGFEVNREAEHGGDVTFLKYEDLEKYYAEDKLHPGDLKATVEKYINRLLDPIRKAFENPELQKLSAAAYPPPAKVKAGAAPAAGADEDAPHRLDIRVGKVVEVARHPDADTLYVLKIDLAEAQPRTIISGLVKFVTEEELNQRLVAVLCNLKPSKMRGILSEGMVLCTSNADHTVVEPIVLPATATAGSRLSFEGFSGTPDEQLNPKKKVWEKLSADFKTNSDGLAVWKDNFLLTPEGEKLSSKLANCSIK
Protein: Pectinesterase A (PE A) (EC 3.1.1.11) (Pectin methylesterase A) (PME) (P0C1A9)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Function: Catalyzes the first step in maceration and soft-rotting of plant tissue.
Subcellular location: Secreted {ECO:0000269|PubMed:8370537}. Note=Upon overexpression also accumulates in the periplasm. {ECO:0000269|PubMed:8370537}.
Interaction partners:
- Pectate lyase D
- Pectate lyase C
- Pectate lyase A
- Pectate lyase B
- Pectate lyase E
- Exopolygalacturonate lyase PelX
- Pectate lyase
- Pectinesterase B
- Pectate disaccharide-lyase
- Exo-poly-alpha-D-galacturonosidase
Sequence:
MLKTISGTLALSLIIAASVHQAQAATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIKNGVYNERLTITRNNLHLKGESRNGAVIAAATAAGTLKSDGSKWGTAGSSTITISAKDFSAQSLTIRNDFDFPANQAKSDSDSSKIKDTQAVALYVTKSGDRAYFKDVSLVGYQDTLYVSGGRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKSGNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYGLGRPWHPTTTFSDGRYADPNAIGQTVFLNTSMDNHIYGWDKMSGKDKNGNTIWFNPEDSRFFEYKSYGAGATVSKDRRQLTDAQAAEYTQSKVLGDWTPTLP
Protein: 2'-5'-oligoadenylate synthase 2 ((2-5')oligo(A) synthase 2) (2-5A synthase 2) (EC 2.7.7.84) (2',5'-oligoadenylate synthetase-like 11) (E9Q9A9)
Organism: Mus musculus (Mouse)
Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation. Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates. Non-infected lobules would not be affected, allowing efficient pup feeding during infection.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}.
Interaction partners:
- Interferon-induced, double-stranded RNA-activated protein kinase
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon regulatory factor 7
- Antiviral innate immune response effector IFIT1
- Interferon-induced protein with tetratricopeptide repeats 3
- Interferon-induced protein with tetratricopeptide repeats 2
- Interferon-induced protein 44
- Nucleotide-binding oligomerization domain-containing protein 2
- Interferon regulatory factor 9
- Ubl carboxyl-terminal hydrolase 18
Sequence:
MGNWLTGNWSSDRSSGYSSGWSPGGSSGVPSGPVHKLEKSIQANLTPNENCLKQIAVSSVPSQKLEGYIQENLKPNRESLKQIDQAVDAIWDLLRSQIPVKEVAKGGSYGRETALRGCSDGTLVLFMDCFQQFQDQIKYQDAYLDVIELWLKIHEKKSVKHEHALVVQVSVPGQRILLQLLPVFNPLRSNENPSSCVYVDLKKSMDQVRASPGEFSDCFTTLQQRFFKKYPQRLKDLILLVKHWYEQCQEKWKTPPPQPLLYALELLTVYAWEQGCQAEDFDMAQGVRTVLRLIQRPTELCVYWTVNYNFEDETVRNILLHQLRSQRPVILDPTDPTNNVGKDDGFWELLTEEAMAWLYSPSLNTESPAPYWDVLPMPLFVTPSHLLNKFIKDFLQPNKLFLKQIKEAVDIICSFLKNVCFLNSDTKVLKTVKGGSTAKGTALKRGSDADIVVFLSSLESYDSLKTNRSQFVQEIQKQLEEFVQAQEWEVTFEISKWKAPRVLSFTLKSKTLNESVEFDVLPAYDALGQLRSDFTLRPEAYKDLIELCASQDIKEGEFSICFTELQRNFIQTRPTKLKSLLRLIKHWYKQYERKMKPKASLPPKYALELLTVYAWEQGSGTDDFDIAEGFRTVLDLVIKYRQLCIFWTVNYNFEEEYMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAEEAKEWLSSPCFQVEQKGLVQPWKVPVMQTPGSCGGQIYPTVGGVTK
Protein: Uncharacterized protein (Q38AK3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- NADH dehydrogenase 1 beta subcomplex subunit 8
- Uncharacterized protein
- NADH dehydrogenase 1 beta subcomplex subunit 9
- 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein
- Uncharacterized protein
- NADH-ubiquinone oxidoreductase complex I subunit
- Uncharacterized protein
- Uncharacterized protein
- Complex 1 LYR protein domain-containing protein
Sequence:
MRRLQIRASLPFSSGELLISTTDNSWPSFTIRVQRRDTAGLSREQRRSQPNADPTTGHQISVVEPPDLTHHIQFGLNNLEYVTLPDVSEADRTRTDMEKERDMQKRFGEGGPGERTNKSSQQVRRDMLQGQQDVDGLPWEVRWRKTVIPTPEEMVQDVRDRFDLYIQDPIDREQEWYLHWKDRSFKIQKDRMIWPQGYTDYLDHYDAHGRRRVLPSDQRWSDTSWKHLADTKYKDRMWLIEGEERNAVHQSLKAEHELLGEEEQRQLEMADVYNGIVSGVVDLDPEQTYQALSGTADPLEVARTKMKLQAYGARQALECAKGIDSPRLDPISGLPKADMAPLPTGVTVEQGVAIAAHANIKNEMLEQTADIARQAGQDPVPALMKAHYKASKQYDDRPALRSLVEEKIERTTRTLETTSDSKLGDAGRIVEQIESSAVPVIGCKLNESEKLSEASCTSSETERQASKEGKPHKGTPAGFIEVKKRPQGAEPDIPTELYHVPCGRETEGMPEWYRRTLVETEPMIQSYGLTHDPLERRIVDTHEYYDPPQLTEDTRITNDDAVAGVSSFDELKMRKMKSLPELVEGYKPLPLYREVASGKGDAGPQDNSVSGGSAKRSDLLRKERQDRVRKAKVHYDPDILLPSLPWESDSIADPYRGVAKGDAIDFNKADLEKTWRAYRDTFRQSMTEFGNLTQVTTEDKCERMLMDVMDRFRRGDVGDHPQIPEELEAIFRMIFEAHTKHFLSDFYRFKGNRVTEGKTVKAEADEILRRASAKCKLLGPNFMNFIQEMTSLELDSVRNNPAQRYAIMVRDRAYEPLGKPFINWINSELSEFIVNEFQGIEQLETHMEFLKRHVNDARAKCPMRLEGVRDSARDATVEAFYQWCRGALCFYAGKHLQRLCIDFADTRFRTRAEELFEDSIEWFSNYAKASNGIVQIPIPDSDPPYEYEEKDFLDGENAIYEEISGHLDKAEGLWHSGTSRRWYPVIDETEYIWYNERRGRITLALDISDRCLENVNKKTHPSVHPFPERARLFLEGAPLTQETAEHLWMRHLGDLYYEHSELMFRNGRFQTARIYREKCLNLYHLATRTAAERLPPSWKAPLLTRAKYLMRVYEPGSGVEEHIKDVERVVDRLFAEKEPPHWIEPFSELPYRLAVVHANLPAFGECITARVKSCVKNSPGNELLLKNMEQRSRGGAQLPETEEYFAAVDRVADEVFRKRILRWRSQECEGSDPYLFWTHLYFAFRVHPKSCEEVAKMWDMYEPAYLYIYTQGALASRNRGQKLINDALRRVCQILLPGDEKQKKVLLRELVKVREKLSHLVHRRELDQTIHALESHLADPSRQTFCYGTSLLYREALTHERIANNPSLRADLAARDYAELKQRKASLQTQGSSLNPQQAAKLQEQQGCTMLVDEEAIGLKPDPSTKELFETK
Protein: ATP-dependent 6-phosphofructokinase subunit alpha (EC 2.7.1.11) (ATP-dependent 6-phosphofructokinase) (ATP-PFK) (Phosphofructokinase 1) (Phosphohexokinase) (P16861)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:18313953}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:16962558}.
Interaction partners:
- ATP-dependent 6-phosphofructokinase subunit beta
- Fructose-1,6-bisphosphatase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Pyruvate kinase 1
- 6-phosphofructo-2-kinase 1
- Hexokinase-2
- 6-phosphofructo-2-kinase 2
- Hexokinase-1
- Glucokinase-1
Sequence:
MQSQDSCYGVAFRSIITNDEALFKKTIHFYHTLGFATVKDFNKFKHGENSLLSSGTSQDSLREVWLESFKLSEVDASGFRIPQQEATNKAQSQGALLKIRLVMSAPIDETFDTNETATITYFSTDLNKIVEKFPKQAEKLSDTLVFLKDPMGNNITFSGLANATDSAPTSKDAFLEATSEDEIISRASSDASDLLRQTLGSSQKKKKIAVMTSGGDSPGMNAAVRAVVRTGIHFGCDVFAVYEGYEGLLRGGKYLKKMAWEDVRGWLSEGGTLIGTARSMEFRKREGRRQAAGNLISQGIDALVVCGGDGSLTGADLFRHEWPSLVDELVAEGRFTKEEVAPYKNLSIVGLVGSIDNDMSGTDSTIGAYSALERICEMVDYIDATAKSHSRAFVVEVMGRHCGWLALMAGIATGADYIFIPERAVPHGKWQDELKEVCQRHRSKGRRNNTIIVAEGALDDQLNPVTANDVKDALIELGLDTKVTILGHVQRGGTAVAHDRWLATLQGVDAVKAVLEFTPETPSPLIGILENKIIRMPLVESVKLTKSVATAIENKDFDKAISLRDTEFIELYENFLSTTVKDDGSELLPVSDRLNIGIVHVGAPSAALNAATRAATLYCLSHGHKPYAIMNGFSGLIQTGEVKELSWIDVENWHNLGGSEIGTNRSVASEDLGTIAYYFQKNKLDGLIILGGFEGFRSLKQLRDGRTQHPIFNIPMCLIPATVSNNVPGTEYSLGVDTCLNALVNYTDDIKQSASATRRRVFVCEVQGGHSGYIASFTGLITGAVSVYTPEKKIDLASIREDITLLKENFRHDKGENRNGKLLVRNEQASSVYSTQLLADIISEASKGKFGVRTAIPGHVQQGGVPSSKDRVTASRFAVKCIKFIEQWNKKNEASPNTDAKVLRFKFDTHGEKVPTVEHEDDSAAVICVNGSHVSFKPIANLWENETNVELRKGFEVHWAEYNKIGDILSGRLKLRAEVAALAAENK
Protein: Spindle pole body component alp14 (Altered polarity protein 14) (O94534)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for bipolar spindle formation and proper chromosome segregation. Has a role in connecting the kinetochores and the plus end of pole to chromosome microtubules. Also required for the activation of the spindle checkpoint pathway.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Chromosome, centromere, kinetochore. Note=Kinetochore periphery. Spindle localization is alp7-dependent.
Interaction partners:
- Microtubule protein alp7
- Kinetochore protein ndc80
- Microtubule integrity protein mal3
- Tubulin beta chain
- DASH complex subunit ask1
- Kinesin-like protein 5
- DASH complex subunit dam1
- DASH complex subunit dad2
- Tubulin alpha-2 chain
- DASH complex subunit spc34
Sequence:
MSQDQEEDYSKLPLESRIVHKVWKVRLSAYEECSKSFSLSADGSDNCFELWNNQSELWKSVLTDSNVAAQEAGTAAFVAYCRFSDPSHLLKAREISVLSISEKCLTSPRAGTRENALEALMLLVEADSAAPVIESIIPSLSARSPKVIASNVAAIASLVEQFGAKVIPSKMIIPHISNLFGHADKNVRKEASRLTVNIYRWTGDPLKDLLFKDLRPVQTKELESLFAELPTEPPKQTRFLKSQQPTSEPNVETQVEEQPALENEESEPEPSDDQFDLVEEVDVLPNVDPNLETLMASSKWKDRKEALDKLLPVLSQPKIKDNDFFNLVAILTKSVSKDANIMVVINAAHCIQAMAKGLRSNFSKYASTSINALLERSKEKKANVIESLSSAMDAVLATSSLDDLAELIASFAGNKNPQIKSSCFSLFSRSFSNMTSLPSKFTVDTCAKACVPGVSDTFEPVRSAAAEALGVLMKLVGERAINQYLSPLDDIRKSKIRSFYETATVKAKAPTKKSKVKPSKQEESKVVVPSNAKAVKKSVVPSSPVVPSPRKATNKSLSMDVSKGNAFENGPLLPRPTTRPVSRGLSRGTSSSLQQKVKASTPLNSGALNETVQNLKNMELDDPAPQPAKHSRVDRYEHPKVLEDNDSTISSLESLKRENEELREQLKVEHEENISMQKQLSELKGELNTLRSARKASPIGDRKPAFMRRANTDFLELSTSPSFQRSVREFEPTRPKLYSSIDVNQRSPLASAKTNGNFTFHAELPRSPFSSRANNINPDWTKAIDLAAKLKQKITEMKQTDQRHQGLIH
Protein: Son of sevenless homolog 1 (SOS-1) (Q07889)
Organism: Homo sapiens (Human)
Function: Promotes the exchange of Ras-bound GDP by GTP. Probably by promoting Ras activation, regulates phosphorylation of MAP kinase MAPK3 in response to EGF. Catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity (By similarity).
Interaction partners:
- Focal adhesion kinase 1
- SHC-transforming protein 1
- GTPase HRas
- Epidermal growth factor receptor kinase substrate 8
- Growth factor receptor-bound protein 2
- GTPase KRas
- Tyrosine-protein phosphatase non-receptor type 11
- Epidermal growth factor receptor
- Abl interactor 1
- Fibroblast growth factor receptor substrate 2
Sequence:
MQAQQLPYEFFSEENAPKWRGLLVPALKKVQGQVHPTLESNDDALQYVEELILQLLNMLCQAQPRSASDVEERVQKSFPHPIDKWAIADAQSAIEKRKRRNPLSLPVEKIHPLLKEVLGYKIDHQVSVYIVAVLEYISADILKLVGNYVRNIRHYEITKQDIKVAMCADKVLMDMFHQDVEDINILSLTDEEPSTSGEQTYYDLVKAFMAEIRQYIRELNLIIKVFREPFVSNSKLFSANDVENIFSRIVDIHELSVKLLGHIEDTVEMTDEGSPHPLVGSCFEDLAEELAFDPYESYARDILRPGFHDRFLSQLSKPGAALYLQSIGEGFKEAVQYVLPRLLLAPVYHCLHYFELLKQLEEKSEDQEDKECLKQAITALLNVQSGMEKICSKSLAKRRLSESACRFYSQQMKGKQLAIKKMNEIQKNIDGWEGKDIGQCCNEFIMEGTLTRVGAKHERHIFLFDGLMICCKSNHGQPRLPGASNAEYRLKEKFFMRKVQINDKDDTNEYKHAFEIILKDENSVIFSAKSAEEKNNWMAALISLQYRSTLERMLDVTMLQEEKEEQMRLPSADVYRFAEPDSEENIIFEENMQPKAGIPIIKAGTVIKLIERLTYHMYADPNFVRTFLTTYRSFCKPQELLSLIIERFEIPEPEPTEADRIAIENGDQPLSAELKRFRKEYIQPVQLRVLNVCRHWVEHHFYDFERDAYLLQRMEEFIGTVRGKAMKKWVESITKIIQRKKIARDNGPGHNITFQSSPPTVEWHISRPGHIETFDLLTLHPIEIARQLTLLESDLYRAVQPSELVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVETENLEERVAVVSRIIEILQVFQELNNFNGVLEVVSAMNSSPVYRLDHTFEQIPSRQKKILEEAHELSEDHYKKYLAKLRSINPPCVPFFGIYLTNILKTEEGNPEVLKRHGKELINFSKRRKVAEITGEIQQYQNQPYCLRVESDIKRFFENLNPMGNSMEKEFTDYLFNKSLEIEPRNPKPLPRFPKKYSYPLKSPGVRPSNPRPGTMRHPTPLQQEPRKISYSRIPESETESTASAPNSPRTPLTPPPASGASSTTDVCSVFDSDHSSPFHSSNDTVFIQVTLPHGPRSASVSSISLTKGTDEVPVPPPVPPRRRPESAPAESSPSKIMSKHLDSPPAIPPRQPTSKAYSPRYSISDRTSISDPPESPPLLPPREPVRTPDVFSSSPLHLQPPPLGKKSDHGNAFFPNSPSPFTPPPPQTPSPHGTRRHLPSPPLTQEVDLHSIAGPPVPPRQSTSQHIPKLPPKTYKREHTHPSMHRDGPPLLENAHSS
Protein: Sizzled (Szl protein) (Q7SX78)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Chordin
- Dorsal-ventral patterning tolloid-like protein 1
- Wnt inhibitory factor 1
- BMP-binding endothelial regulator.
- Protein Wnt-5b
- Even-skipped-like1
- Protein Wnt
- Bone morphogenetic protein 2
- Protein Wnt-8a
Sequence:
MSLFSLLLFFSLAAHTGAFDLGQTTRCVPIPPQMSVCQDVPYSEMRLPNLLGHGSLEEAAPRSDDLRTLLHTGCHPQARAFVCSLIAPVCLDRFIQPCRSVCLAVKESCSPVLACHGHSWPESLNCERFPEQDDCLTPLPKHISAFSKEFPQPACQSCPSVQESPSLKTLLDSLCLNDFAVKVKIMRRRVPSSEPEFTVEGAVELIERGPLMPYDTASLLQRWMLINLRCAHALVRPGRAQLYLITGKMRAGGSIEIANLFPWLKKDLHIATATRKWKHYKC
Protein: Gap junction gamma-2 protein (Connexin-46.6) (Cx46.6) (Connexin-47) (Cx47) (Gap junction alpha-12 protein) (Q5T442)
Organism: Homo sapiens (Human)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a role in myelination in central and peripheral nervous systems.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
Interaction partners:
- Hyccin
- Patatin-like phospholipase domain-containing protein 6
- AP-5 complex subunit zeta-1
- Maspardin
- Gap junction beta-2 protein
- Gap junction alpha-1 protein
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Forkhead box protein C2
- Spatacsin
- Gap junction beta-6 protein
Sequence:
MTNMSWSFLTRLLEEIHNHSTFVGKVWLTVLVVFRIVLTAVGGEAIYSDEQAKFTCNTRQPGCDNVCYDAFAPLSHVRFWVFQIVVISTPSVMYLGYAVHRLARASEQERRRALRRRPGPRRAPRAHLPPPHAGWPEPADLGEEEPMLGLGEEEEEEETGAAEGAGEEAEEAGAEEACTKAVGADGKAAGTPGPTGQHDGRRRIQREGLMRVYVAQLVARAAFEVAFLVGQYLLYGFEVRPFFPCSRQPCPHVVDCFVSRPTEKTVFLLVMYVVSCLCLLLNLCEMAHLGLGSAQDAVRGRRGPPASAPAPAPRPPPCAFPAAAAGLACPPDYSLVVRAAERARAHDQNLANLALQALRDGAAAGDRDRDSSPCVGLPAASRGPPRAGAPASRTGSATSAGTVGEQGRPGTHERPGAKPRAGSEKGSASSRDGKTTVWI
Protein: Putative carboxypeptidase suro-1 (EC 3.4.17.-) (Suppressor of roller 1) (Q9XU75)
Organism: Caenorhabditis elegans
Function: May play a role in processing or organization of cuticle collagen proteins, including rol-6 and col-19.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:21094156}. Secreted {ECO:0000305|PubMed:21094156}.
Interaction partners:
Sequence:
MRYLCKSILLAVHTILLVGSVCCSTDVHNTDDKYALIHVSAHDEQSLHLIKQLQLNDFKYDLDFWKSPSSISDKADIMVKRGKSERMLRQILSFANVTVSMSVPDVEKLIMRNEGTTSKSHLGFGSLSKWLHDDPILDSEPDLDLTKVGALKKAKYPFGDYASYADMVKYMRTIEFYYPRIAKIVRIGATHEGKPIEGLKIGARSSHKKRAVWVDGNIHAREWASSHTALYFINQLVSEYGKDAQITNYVDTLDFYIVPCLNPDGYEYTRTSPIPTVRLWRKNRSPELCRPSLWGGEKCCRGVDLNRNFRFHWAERGSSYEPCSNIYHGEEVFSEPETRAVRNFLATPEMKDRVDAFVTLHSYAQLWIYPYSHEEQNYPEDIGELRKTARKAINRLSRVYGTNYRMGTGADTLSPAAGGSDDWAKSALNVKYVYLIELRPQMELSNGFILHKKELIPTAVETFEGFREVVDAVLTLNNSTSSIGLSSGSNTSRKTISDLQMRKQQYRMRLLASQAAGSTTRSTTTLKTSTTSVSTTSEATSPSKTSRHFDRFTADLNSSTRARPTPPMAPPIMSPSTEFSTTTTEEEDVTGVIRSSSIASRATTYGFFTATKPSAFLDPECRDMRYSCGFWLKNNKQVCEEQQSFMRAQCAYTCKFCTSFIKRH