P02549

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession SPTA1_HUMAN; P02549;
Entrez ID 6708
GenBank Protein ID NM_003126.2; XM_011509916.2;
GenBank Nucleotide ID NP_003117.2; XP_011508218.1;
Protein Name Spectrin alpha chain, erythrocytic 1 (Erythroid alpha-spectrin)
Gene Name SPTA1; SPTA
Organism Homo sapiens
NCBI Taxa ID 9606
Functional DescriptionSpectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
Sequence
(Fasta)
MEQFPKETVV ESSGPKVLET AEEIQERRQE VLTRYQSFKE RVAERGQKLE DSYHLQVFKR 60
DADDLGKWIM EKVNILTDKS YEDPTNIQGK YQKHQSLEAE VQTKSRLMSE LEKTREERFT 120
MGHSAHEETK AHIEELRHLW DLLLELTLEK GDQLLRALKF QQYVQECADI LEWIGDKEAI 180
ATSVELGEDW ERTEVLHKKF EDFQVELVAK EGRVVEVNQY ANECAEENHP DLPLIQSKQN 240
EVNAAWERLR GLALQRQKAL SNAANLQRFK RDVTEAIQWI KEKEPVLTSE DYGKDLVASE 300
GLFHSHKGLE RNLAVMSDKV KELCAKAEKL TLSHPSDAPQ IQEMKEDLVS SWEHIRALAT 360
SRYEKLQATY WYHRFSSDFD ELSGWMNEKT AAINADELPT DVAGGEVLLD RHQQHKHEID 420
SYDDRFQSAD ETGQDLVNAN HEASDEVREK MEILDNNWTA LLELWDERHR QYEQCLDFHL 480
FYRDSEQVDS WMSRQEAFLE NEDLGNSLGS AEALLQKHED FEEAFTAQEE KIITVDKTAT 540
KLIGDDHYDS ENIKAIRDGL LARRDALREK AATRRRLLKE SLLLQKLYED SDDLKNWINK 600
KKKLADDEDY KDIQNLKSRV QKQQVFEKEL AVNKTQLENI QKTGQEMIEG GHYASDNVTT 660
RLSEVASLWE ELLEATKQKG TQLHEANQQL QFENNAEDLQ RWLEDVEWQV TSEDYGKGLA 720
EVQNRLRKHG LLESAVAARQ DQVDILTDLA AYFEEIGHPD SKDIRARQES LVCRFEALKE 780
PLATRKKKLL DLLHLQLICR DTEDEEAWIQ ETEPSATSTY LGKDLIASKK LLNRHRVILE 840
NIASHEPRIQ EITERGNKMV EEGHFAAEDV ASRVKSLNQN MESLRARAAR RQNDLEANVQ 900
FQQYLADLHE AETWIREKEP IVDNTNYGAD EEAAGALLKK HEAFLLDLNS FGDSMKALRN 960
QANACQQQQA APVEGVAGEQ RVMALYDFQA RSPREVTMKK GDVLTLLSSI NKDWWKVEAA 1020
DHQGIVPAVY VRRLAHDEFP MLPQRRREEP GNITQRQEQI ENQYRSLLDR AEERRRRLLQ 1080
RYNEFLLAYE AGDMLEWIQE KKAENTGVEL DDVWELQKKF DEFQKDLNTN EPRLRDINKV 1140
ADDLLFEGLL TPEGAQIRQE LNSRWGSLQR LADEQRQLLG SAHAVEVFHR EADDTKEQIE 1200
KKCQALSAAD PGSDLFSVQA LQRRHEGFER DLVPLGDKVT ILGETAERLS ESHPDATEDL 1260
QRQKMELNEA WEDLQGRTKD RKESLNEAQK FYLFLSKARD LQNWISSIGG MVSSQELAED 1320
LTGIEILLER HQEHRADMEA EAPTFQALED FSAELIDSGH HASPEIEKKL QAVKLERDDL 1380
EKAWEKRKKI LDQCLELQMF QGNCDQVESW MVARENSLRS DDKSSLDSLE ALMKKRDDLD 1440
KAITAQEGKI TDLEHFAESL IADEHYAKEE IATRLQRVLD RWKALKAQLI DERTKLGDYA 1500
NLKQFYRDLE ELEEWISEML PTACDESYKD ATNIQRKYLK HQTFAHEVDG RSEQVHGVIN 1560
LGNSLIECSA CDGNEEAMKE QLEQLKEHWD HLLERTNDKG KKLNEASRQQ RFNTSIRDFE 1620
FWLSEAETLL AMKDQARDLA SAGNLLKKHQ LLEREMLARE DALKDLNTLA EDLLSSGTFN 1680
VDQIVKKKDN VNKRFLNVQE LAAAHHEKLK EAYALFQFFQ DLDDEESWIE EKLIRVSSQD 1740
YGRDLQGVQN LLKKHKRLEG ELVAHEPAIQ NVLDMAEKLK DKAAVGQEEI QLRLAQFVEH 1800
WEKLKELAKA RGLKLEESLE YLQFMQNAEE EEAWINEKNA LAVRGDCGDT LAATQSLLMK 1860
HEALENDFAV HETRVQNVCA QGEDILNKVL QEESQNKEIS SKIEALNEKT PSLAKAIAAW 1920
KLQLEDDYAF QEFNWKADVV EAWIADKETS LKTNGNGADL GDFLTLLAKQ DTLDASLQSF 1980
QQERLPEITD LKDKLISAQH NQSKAIEERY AALLKRWEQL LEASAVHRQK LLEKQLPLQK 2040
AEDLFVEFAH KASALNNWCE KMEENLSEPV HCVSLNEIRQ LQKDHEDFLA SLARAQADFK 2100
CLLELDQQIK ALGVPSSPYT WLTVEVLERT WKHLSDIIEE REQELQKEEA RQVKNFEMCQ 2160
EFEQNASTFL QWILETRAYF LDGSLLKETG TLESQLEANK RKQKEIQAMK RQLTKIVDLG 2220
DNLEDALILD IKYSTIGLAQ QWDQLYQLGL RMQHNLEQQI QAKDIKGVSE ETLKEFSTIY 2280
KHFDENLTGR LTHKEFRSCL RGLNYYLPMV EEDEHEPKFE KFLDAVDPGR KGYVSLEDYT 2340
AFLIDKESEN IKSSDEIENA FQALAEGKSY ITKEDMKQAL TPEQVSFCAT HMQQYMDPRG 2400
RSHLSGYDYV GFTNSYFGN

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1Tyrosine PhosphorylationSickle-cell diseaseUY42220206558
[Reference]: In SCD RBCs we identified the phosphopeptides for protein 4.1R located in the protein FERM domain (Tyr-13) and for alpha-spectrin located near or in a linker region (Tyr-422 and Tyr-1498) involving protein areas crucial for their functions in the context of red cell membrane properties, suggesting that Tyr-phosphorylation may be part of the events involved in maintaining membrane mechanical stability in SCD red cells.
2Tyrosine PhosphorylationSickle-cell diseaseUY54820206558
[Reference]: Deoxygenation affects tyrosine phosphoproteome of red cell membrane from patients with sickle cell disease.
3Tyrosine PhosphorylationSickle-cell diseaseUY149920206558
[Reference]: In SCD RBCs we identified the phosphopeptides for protein 4.1R located in the protein FERM domain (Tyr-13) and for alpha-spectrin located near or in a linker region (Tyr-422 and Tyr-1498) involving protein areas crucial for their functions in the context of red cell membrane properties, suggesting that Tyr-phosphorylation may be part of the events involved in maintaining membrane mechanical stability in SCD red cells.

※ Disease Cross-ref Annotation

DatabaseAnnotation
CTD (Curated)
(count: 3)
MESH:C565058 ; Elliptocytosis 2
MESH:C563004 ; Pyropoikilocytosis, Hereditary
MESH:C567489 ; Spherocytosis, Type 3
GWASdb
(count: 54)
(view all)
rs2479868; Other erythrocyte phenotypes; hematopoietic system disease
rs2479868; Red blood cell traits; hematopoietic system disease
rs12128171; Red blood cell traits; hematopoietic system disease
rs12601; Iris characteristics; iris disease
rs2157691; Other erythrocyte phenotypes; hematopoietic system disease
rs2157691; Red blood cell traits; hematopoietic system disease

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 35)
(view all)
1064      QEQIENQYRSLLDRA     dbPAF
1167      ELNSRWGSLQRLADE     dbPAF
1250      GETAERLSESHPDAT     dbPAF
1257      SESHPDATEDLQRQK     dbPAF
1278      WEDLQGRTKDRKESL     dbPAF
1284      RTKDRKESLNEAQKF     dbPAF
Acetylation
(count: 2)
1803      QFVEHWEKLKELAKA     PLMD
283       AIQWIKEKEPVLTSE     PLMD
Ubiquitination
(count: 1)
1803      QFVEHWEKLKELAKA     PLMD
Glycation
(count: 58)
(view all)
104       LEAEVQTKSRLMSEL     PLMD
1102      LEWIQEKKAENTGVE     PLMD
1238      DLVPLGDKVTILGET     PLMD
1290      ESLNEAQKFYLFLSK     PLMD
130       HSAHEETKAHIEELR     PLMD
1374      EKKLQAVKLERDDLE     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource