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P07751

- SPTN1_CHICK

UniProt

P07751 - SPTN1_CHICK

Protein

Spectrin alpha chain, non-erythrocytic 1

Gene

SPTAN1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1176 – 11772Cleavage; by mu-calpainBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi2341 – 2352121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi2384 – 2395122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. actin filament capping Source: UniProtKB-KW

    Keywords - Molecular functioni

    Actin capping

    Keywords - Ligandi

    Actin-binding, Calcium, Calmodulin-binding, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Spectrin alpha chain, non-erythrocytic 1
    Alternative name(s):
    Alpha-II spectrin
    Fodrin alpha chain
    Gene namesi
    Name:SPTAN1
    Synonyms:SPTA2
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cytoskeleton Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24772477Spectrin alpha chain, non-erythrocytic 1PRO_0000073454Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1176 – 11761PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by calpain in vitro.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP07751.
    PRIDEiP07751.

    Interactioni

    Subunit structurei

    Like erythrocyte spectrin, the spectrin-like proteins are capable of forming dimers which can further associate to tetramers. Interacts with ACP1 By similarity.By similarity

    Protein-protein interaction databases

    MINTiMINT-139133.
    STRINGi9031.ENSGALP00000007504.

    Structurei

    Secondary structure

    1
    2477
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi967 – 9693
    Beta strandi971 – 9744
    Beta strandi981 – 9844
    Beta strandi993 – 9986
    Beta strandi1001 – 10099
    Beta strandi1012 – 10176
    Helixi1018 – 10203
    Beta strandi1021 – 10233
    Beta strandi1040 – 10434
    Helixi1664 – 168623
    Helixi1695 – 173036
    Beta strandi1733 – 17353
    Helixi1771 – 179121
    Helixi1801 – 183737
    Helixi1843 – 189856
    Helixi1907 – 194438
    Helixi1949 – 198133

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AEYNMR-A965-1025[»]
    1AJ3NMR-A1763-1872[»]
    1BK2X-ray2.01A969-1025[»]
    1CUNX-ray2.00A/B/C1770-1982[»]
    1E6GX-ray2.30A965-1025[»]
    1E6HX-ray2.01A965-1025[»]
    1E7OX-ray3.20A965-1025[»]
    1G2BX-ray1.12A967-1025[»]
    1H8KX-ray2.70A965-1025[»]
    1HD3X-ray1.98A965-1025[»]
    1M8MNMR-A965-1025[»]
    1NEGX-ray2.30A965-1024[»]
    1PWTX-ray1.77A967-1025[»]
    1QKWX-ray2.00A964-1025[»]
    1QKXX-ray1.80A964-1025[»]
    1SHGX-ray1.80A965-1025[»]
    1TUCX-ray2.02A967-1025[»]
    1TUDX-ray1.77A964-1010[»]
    1U06X-ray1.49A965-1025[»]
    1U4QX-ray2.50A/B1662-1982[»]
    1U5PX-ray2.00A1662-1876[»]
    1UUEX-ray2.60A965-1025[»]
    2CDTX-ray2.54A965-1025[»]
    2F2VX-ray1.85A965-1025[»]
    2F2WX-ray1.70A965-1025[»]
    2F2XX-ray1.60A965-1025[»]
    2JM8NMR-A965-1025[»]
    2JM9NMR-A965-1025[»]
    2JMANMR-A965-1025[»]
    2JMCNMR-A983-1025[»]
    2KR3NMR-A965-1025[»]
    2KXDNMR-A967-1025[»]
    2LJ3NMR-A965-1025[»]
    2NUZX-ray1.85A965-1025[»]
    2OAWX-ray1.90A/B/C/D969-1025[»]
    2RMONMR-A965-1025[»]
    2ROTNMR-A965-1025[»]
    3I9QX-ray1.45A969-1025[»]
    3M0PX-ray2.60A965-1025[»]
    3M0QX-ray1.75A965-1025[»]
    3M0RX-ray1.10A965-1025[»]
    3M0SX-ray1.60A969-1025[»]
    3M0TX-ray1.70A965-1025[»]
    3M0UX-ray1.10A965-1025[»]
    3NGPX-ray1.08A965-1025[»]
    4F16X-ray1.93A965-1025[»]
    4F17X-ray1.55A965-1025[»]
    ProteinModelPortaliP07751.
    SMRiP07751. Positions 1-147, 967-1025, 1443-1549, 1662-1979.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07751.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati15 – 119105Spectrin 1Add
    BLAST
    Repeati120 – 225106Spectrin 2Add
    BLAST
    Repeati226 – 331106Spectrin 3Add
    BLAST
    Repeati332 – 437106Spectrin 4Add
    BLAST
    Repeati438 – 543106Spectrin 5Add
    BLAST
    Repeati544 – 648105Spectrin 6Add
    BLAST
    Repeati649 – 754106Spectrin 7Add
    BLAST
    Repeati755 – 860106Spectrin 8Add
    BLAST
    Repeati861 – 966106Spectrin 9Add
    BLAST
    Domaini967 – 102660SH3PROSITE-ProRule annotationAdd
    BLAST
    Repeati1062 – 1167106Spectrin 10Add
    BLAST
    Repeati1204 – 1309106Spectrin 11Add
    BLAST
    Repeati1310 – 1415106Spectrin 12Add
    BLAST
    Repeati1416 – 1521106Spectrin 13Add
    BLAST
    Repeati1522 – 1633112Spectrin 14Add
    BLAST
    Repeati1634 – 1739106Spectrin 15Add
    BLAST
    Repeati1740 – 1845106Spectrin 16Add
    BLAST
    Repeati1846 – 1951106Spectrin 17Add
    BLAST
    Repeati1952 – 2058107Spectrin 18Add
    BLAST
    Repeati2059 – 2171113Spectrin 19Add
    BLAST
    Repeati2172 – 225685Spectrin 20Add
    BLAST
    Domaini2328 – 236336EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2371 – 240636EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2409 – 244436EF-hand 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 1414N-terminal domainAdd
    BLAST
    Regioni2257 – 2477221C-terminal domainAdd
    BLAST

    Domaini

    Spectrin-like proteins have five domains: (1) N-terminal domain (N), (2) domain between the N-terminal and middle domain (NM), (3) middle domain (M), (4) domain between the middle and C-terminal domain (MC), (5) C-terminal domain (C). NM and MC domains are composed of typical spectrin 106 residues repeats (1-8 for NM and 12-19 for MC) and are homologous to each other. N, M, and C domains are composed of sequences that do not form typical spectrin repeats.

    Sequence similaritiesi

    Belongs to the spectrin family.Curated
    Contains 3 EF-hand domains.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation
    Contains 20 spectrin repeats.Curated

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiCOG5126.
    HOGENOMiHOG000246965.
    HOVERGENiHBG059266.
    KOiK06114.
    PhylomeDBiP07751.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR014837. EF-hand_Ca_insen.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR001452. SH3_domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR013315. Spectrin_alpha_SH3.
    IPR002017. Spectrin_repeat.
    [Graphical view]
    PfamiPF13499. EF-hand_7. 1 hit.
    PF08726. EFhand_Ca_insen. 1 hit.
    PF00018. SH3_1. 1 hit.
    PF00435. Spectrin. 20 hits.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    PR01887. SPECTRNALPHA.
    SMARTiSM00054. EFh. 2 hits.
    SM00326. SH3. 1 hit.
    SM00150. SPEC. 20 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P07751-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSSLRRQKL EDSYRFQFFQ     50
    RDADELGKWI QEKLQIASDE NYKDPSNLQG KLQKHQAFEA EVQANSGAIV 100
    KLDETGNQMI NEGHFASETI RTRLQELHRL WELLLEKMRE KGVKLLQAQK 150
    LVQFLRECED VMDWINDKEA IVTSEELGQD LEHVEVLQKK FEEFQTDLAA 200
    HEERVNEVNQ FAGKLIQEQH PEEELIKSKQ DEVNASWQRL KGLAQQRQGK 250
    LFGAAEVQRF NRDVDETISW IKEKGQLMAS DDFGRDLASV QALLRKHEGL 300
    ERDLAAFHHK VKALCAEADR LQQSHPINAS QIQVKREELI ANWEQIRTLA 350
    AERHARLNDS YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL 400
    DRHQEHKGEI DAHEDSFRSA DESGQALLAA GHYASDEVKE KLTILSDERS 450
    ALLELWELRR QQYEQCMDLQ LFYRDTEQVD NWMSKQEAFL LNEDLGDSLD 500
    SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA MDDVATRRDA 550
    LLSRRNALHE RAMKRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 600
    YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYASDEVA 650
    ARMNEVISLW KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH 700
    LASDDYGKDL TSVQNLQKKH ALLEADVAAH QDPIDGITIQ ARQFQDAGHF 750
    DADNIKKKQE ALVARYEALK DPMVARKQKL ADSLRLQQLF RDIEDEETWI 800
    REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI KAVTQKGNAM 850
    VEEGHFAAED VKIKLNELNQ KWDSLKAKAS QRRQDLEDSL QAQQYFADAN 900
    EAQSWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR 950
    EQAQSCRQQV APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST 1000
    NKDWWKVEVN DRQGFVPAAY VKKLDPAQSA SRENLLEEQG SIALRQEQID 1050
    NQTLITKEVG SVSLRMKQVE ELYHSLLELG EKRKGMLEKS CKKFMLFREA 1100
    NELQQWINEK EAALTNEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI 1150
    NKVANDLESE GLMAEEVQAV EHQEVYGMMP RDETDSKTVS PWKSARMMVH 1200
    TVATFNSIKE LNERWRSLQQ LAEERSQLLG SADEVQRFHR DADETKEWIE 1250
    EKNQALNTDN YGHDLASVQA LQRNDEGFER DLAALGDKVN SLGETAQRLI 1300
    QSHPELAEDL QEKCTELNQA WSSLGKRADQ RKEKLGDSHD LQRFLSDFRD 1350
    LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ 1400
    FGQQLLARGH YASPEIKEKL DILDQERTDL EKAWVQRRMM LDQCLELQLF 1450
    HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 1500
    IAVLQSFADQ LIAADHYAKG VIANRRNEVL DRWRRLKAQM IEKRSKLGES 1550
    QTLQQFSRDV DEIEAWISEK LQTASDESYK DPTNIQLSKL LSKHQKHQAF 1600
    EAELHANADR IRGVIEMGNP LIERGACAGS EDAVKARLAA LADQWEFLVQ 1650
    KSSEKSQKLK EANKQQNFNT GIKDFDFWLS EVEALLASED YGKDLASVNN 1700
    LLKKHQLLEA DISAHEDRLK DLNSQADSLM TSSAFDTSQV KDKRETINGR 1750
    FQRIKSMAAA RRAKLNESHR LHQFFRDMDD EESWIKEKKL LVSSEDYGRD 1800
    LTGVQNLRKK HKRLEAELAA HEPAIQGVLD TGKKLSDDNT IGKEEIQQRL 1850
    AQFVDHWKEL KQLAAARGQR LEESLEYQQF VANVEEEEAW INEKMTLVAS 1900
    EDYGDTLAAI QGLLKKHEAF ETDFTVHKDR VNDVCANGED LIKKNNHHVE 1950
    NITAKMKGLK GKVSDLEKAA AQRKAKLDEN SAFLQFNWKA DVVESWIGEK 2000
    ENSLKTDDYG RDLSSVQTLL TKQETFDAGL QAFQQEGIAN ITALKDQLLA 2050
    AKHIQSKAIE VRHASLMKRW NQLLANSAAR KKKLLEAQEH FRKVEDLFLT 2100
    FAKKASAFNS WFENAEEDLT DPVRCNSLEE IKALREAHDA FRSSLSSAQA 2150
    DFNQLAELDR QIKSFRVASN PYTWFTMEAL EETWRNLQKI IKERELELQK 2200
    EQRRQEENDK LRQEFAQHAN AFHQWIQETR TYLLDGSCMV EESGTLESQL 2250
    EATKRKHQEI RAMRSQLKKI EDLGAAMEEA LILDNKYTEH STVGLAQQWD 2300
    QLDQLGMRMQ HNLEQQIQAR NTTGVTEEAL KEFSMMFKHF DKDKSGRLNH 2350
    QEFKSCLRSL GYDLPMVEEG EPDPEFESIL DTVDPNRDGH VSLQEYMAFM 2400
    ISRETENVKS SEEIESAFRA LSSERKPYVT KEELYQNLTR EQADYCISHM 2450
    KPYMDGKGRE LPSAYDYIEF TRSLFVN 2477
    Length:2,477
    Mass (Da):285,363
    Last modified:August 1, 1991 - v3
    Checksum:iAD4C876994E6AB39
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14518 Genomic DNA. Translation: CAA32662.1.
    X14519 mRNA. Translation: CAA32663.1. Sequence problems.
    X02593 mRNA. Translation: CAB51571.1. Sequence problems.
    PIRiA30122. SJCHA.
    RefSeqiNP_001036003.1. NM_001042538.1.
    UniGeneiGga.11413.

    Genome annotation databases

    GeneIDi374234.
    KEGGigga:374234.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14518 Genomic DNA. Translation: CAA32662.1 .
    X14519 mRNA. Translation: CAA32663.1 . Sequence problems.
    X02593 mRNA. Translation: CAB51571.1 . Sequence problems.
    PIRi A30122. SJCHA.
    RefSeqi NP_001036003.1. NM_001042538.1.
    UniGenei Gga.11413.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AEY NMR - A 965-1025 [» ]
    1AJ3 NMR - A 1763-1872 [» ]
    1BK2 X-ray 2.01 A 969-1025 [» ]
    1CUN X-ray 2.00 A/B/C 1770-1982 [» ]
    1E6G X-ray 2.30 A 965-1025 [» ]
    1E6H X-ray 2.01 A 965-1025 [» ]
    1E7O X-ray 3.20 A 965-1025 [» ]
    1G2B X-ray 1.12 A 967-1025 [» ]
    1H8K X-ray 2.70 A 965-1025 [» ]
    1HD3 X-ray 1.98 A 965-1025 [» ]
    1M8M NMR - A 965-1025 [» ]
    1NEG X-ray 2.30 A 965-1024 [» ]
    1PWT X-ray 1.77 A 967-1025 [» ]
    1QKW X-ray 2.00 A 964-1025 [» ]
    1QKX X-ray 1.80 A 964-1025 [» ]
    1SHG X-ray 1.80 A 965-1025 [» ]
    1TUC X-ray 2.02 A 967-1025 [» ]
    1TUD X-ray 1.77 A 964-1010 [» ]
    1U06 X-ray 1.49 A 965-1025 [» ]
    1U4Q X-ray 2.50 A/B 1662-1982 [» ]
    1U5P X-ray 2.00 A 1662-1876 [» ]
    1UUE X-ray 2.60 A 965-1025 [» ]
    2CDT X-ray 2.54 A 965-1025 [» ]
    2F2V X-ray 1.85 A 965-1025 [» ]
    2F2W X-ray 1.70 A 965-1025 [» ]
    2F2X X-ray 1.60 A 965-1025 [» ]
    2JM8 NMR - A 965-1025 [» ]
    2JM9 NMR - A 965-1025 [» ]
    2JMA NMR - A 965-1025 [» ]
    2JMC NMR - A 983-1025 [» ]
    2KR3 NMR - A 965-1025 [» ]
    2KXD NMR - A 967-1025 [» ]
    2LJ3 NMR - A 965-1025 [» ]
    2NUZ X-ray 1.85 A 965-1025 [» ]
    2OAW X-ray 1.90 A/B/C/D 969-1025 [» ]
    2RMO NMR - A 965-1025 [» ]
    2ROT NMR - A 965-1025 [» ]
    3I9Q X-ray 1.45 A 969-1025 [» ]
    3M0P X-ray 2.60 A 965-1025 [» ]
    3M0Q X-ray 1.75 A 965-1025 [» ]
    3M0R X-ray 1.10 A 965-1025 [» ]
    3M0S X-ray 1.60 A 969-1025 [» ]
    3M0T X-ray 1.70 A 965-1025 [» ]
    3M0U X-ray 1.10 A 965-1025 [» ]
    3NGP X-ray 1.08 A 965-1025 [» ]
    4F16 X-ray 1.93 A 965-1025 [» ]
    4F17 X-ray 1.55 A 965-1025 [» ]
    ProteinModelPortali P07751.
    SMRi P07751. Positions 1-147, 967-1025, 1443-1549, 1662-1979.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-139133.
    STRINGi 9031.ENSGALP00000007504.

    Proteomic databases

    PaxDbi P07751.
    PRIDEi P07751.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 374234.
    KEGGi gga:374234.

    Organism-specific databases

    CTDi 6709.

    Phylogenomic databases

    eggNOGi COG5126.
    HOGENOMi HOG000246965.
    HOVERGENi HBG059266.
    KOi K06114.
    PhylomeDBi P07751.

    Miscellaneous databases

    EvolutionaryTracei P07751.
    NextBioi 20813733.
    PROi P07751.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR014837. EF-hand_Ca_insen.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR001452. SH3_domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR013315. Spectrin_alpha_SH3.
    IPR002017. Spectrin_repeat.
    [Graphical view ]
    Pfami PF13499. EF-hand_7. 1 hit.
    PF08726. EFhand_Ca_insen. 1 hit.
    PF00018. SH3_1. 1 hit.
    PF00435. Spectrin. 20 hits.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    PR01887. SPECTRNALPHA.
    SMARTi SM00054. EFh. 2 hits.
    SM00326. SH3. 1 hit.
    SM00150. SPEC. 20 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. Erratum
      Wasenius V.-M., Saraste M., Salven P., Eraemaa M., Holm L., Lehto V.-P.
      J. Cell Biol. 108:1177-1178(1989)
      Cited for: SEQUENCE REVISION.
    3. "Sequencing of the chicken non-erythroid spectrin cDNA reveals an internal repetitive structure homologous to the human erythrocyte spectrin."
      Wasenius V.-M., Saraste M., Knowles J., Virtanen I., Lehto V.-P.
      EMBO J. 4:1425-1430(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1695-2153.
    4. "Crystal structure of a Src-homology 3 (SH3) domain."
      Musacchio A., Noble M., Pauptit R., Wierenga R.K., Saraste M.
      Nature 359:851-855(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 965-1025.
    5. "Obligatory steps in protein folding and the conformational diversity of the transition state."
      Martinez J.C., Pisabarro M.T., Serrano L.
      Nat. Struct. Biol. 5:721-729(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 969-1025.
    6. "Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil."
      Pascual J., Pfuhl M., Walther D., Saraste M., Nilges M.
      J. Mol. Biol. 273:740-751(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1763-1872.
    7. "Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands."
      Trave G., Lacombe J.-P., Pfuhl M., Saraste M., Pastore A.
      EMBO J. 14:4922-4931(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2320-2403.

    Entry informationi

    Entry nameiSPTN1_CHICK
    AccessioniPrimary (citable) accession number: P07751
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3