Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P07751

- SPTN1_CHICK

UniProt

P07751 - SPTN1_CHICK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-KW
Complete GO annotation...

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.
InParanoidiP07751.
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

        10         20         30         40         50
MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSSLRRQKL EDSYRFQFFQ
60 70 80 90 100
RDADELGKWI QEKLQIASDE NYKDPSNLQG KLQKHQAFEA EVQANSGAIV
110 120 130 140 150
KLDETGNQMI NEGHFASETI RTRLQELHRL WELLLEKMRE KGVKLLQAQK
160 170 180 190 200
LVQFLRECED VMDWINDKEA IVTSEELGQD LEHVEVLQKK FEEFQTDLAA
210 220 230 240 250
HEERVNEVNQ FAGKLIQEQH PEEELIKSKQ DEVNASWQRL KGLAQQRQGK
260 270 280 290 300
LFGAAEVQRF NRDVDETISW IKEKGQLMAS DDFGRDLASV QALLRKHEGL
310 320 330 340 350
ERDLAAFHHK VKALCAEADR LQQSHPINAS QIQVKREELI ANWEQIRTLA
360 370 380 390 400
AERHARLNDS YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL
410 420 430 440 450
DRHQEHKGEI DAHEDSFRSA DESGQALLAA GHYASDEVKE KLTILSDERS
460 470 480 490 500
ALLELWELRR QQYEQCMDLQ LFYRDTEQVD NWMSKQEAFL LNEDLGDSLD
510 520 530 540 550
SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA MDDVATRRDA
560 570 580 590 600
LLSRRNALHE RAMKRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA
610 620 630 640 650
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYASDEVA
660 670 680 690 700
ARMNEVISLW KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH
710 720 730 740 750
LASDDYGKDL TSVQNLQKKH ALLEADVAAH QDPIDGITIQ ARQFQDAGHF
760 770 780 790 800
DADNIKKKQE ALVARYEALK DPMVARKQKL ADSLRLQQLF RDIEDEETWI
810 820 830 840 850
REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI KAVTQKGNAM
860 870 880 890 900
VEEGHFAAED VKIKLNELNQ KWDSLKAKAS QRRQDLEDSL QAQQYFADAN
910 920 930 940 950
EAQSWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR
960 970 980 990 1000
EQAQSCRQQV APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST
1010 1020 1030 1040 1050
NKDWWKVEVN DRQGFVPAAY VKKLDPAQSA SRENLLEEQG SIALRQEQID
1060 1070 1080 1090 1100
NQTLITKEVG SVSLRMKQVE ELYHSLLELG EKRKGMLEKS CKKFMLFREA
1110 1120 1130 1140 1150
NELQQWINEK EAALTNEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI
1160 1170 1180 1190 1200
NKVANDLESE GLMAEEVQAV EHQEVYGMMP RDETDSKTVS PWKSARMMVH
1210 1220 1230 1240 1250
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SADEVQRFHR DADETKEWIE
1260 1270 1280 1290 1300
EKNQALNTDN YGHDLASVQA LQRNDEGFER DLAALGDKVN SLGETAQRLI
1310 1320 1330 1340 1350
QSHPELAEDL QEKCTELNQA WSSLGKRADQ RKEKLGDSHD LQRFLSDFRD
1360 1370 1380 1390 1400
LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ
1410 1420 1430 1440 1450
FGQQLLARGH YASPEIKEKL DILDQERTDL EKAWVQRRMM LDQCLELQLF
1460 1470 1480 1490 1500
HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK
1510 1520 1530 1540 1550
IAVLQSFADQ LIAADHYAKG VIANRRNEVL DRWRRLKAQM IEKRSKLGES
1560 1570 1580 1590 1600
QTLQQFSRDV DEIEAWISEK LQTASDESYK DPTNIQLSKL LSKHQKHQAF
1610 1620 1630 1640 1650
EAELHANADR IRGVIEMGNP LIERGACAGS EDAVKARLAA LADQWEFLVQ
1660 1670 1680 1690 1700
KSSEKSQKLK EANKQQNFNT GIKDFDFWLS EVEALLASED YGKDLASVNN
1710 1720 1730 1740 1750
LLKKHQLLEA DISAHEDRLK DLNSQADSLM TSSAFDTSQV KDKRETINGR
1760 1770 1780 1790 1800
FQRIKSMAAA RRAKLNESHR LHQFFRDMDD EESWIKEKKL LVSSEDYGRD
1810 1820 1830 1840 1850
LTGVQNLRKK HKRLEAELAA HEPAIQGVLD TGKKLSDDNT IGKEEIQQRL
1860 1870 1880 1890 1900
AQFVDHWKEL KQLAAARGQR LEESLEYQQF VANVEEEEAW INEKMTLVAS
1910 1920 1930 1940 1950
EDYGDTLAAI QGLLKKHEAF ETDFTVHKDR VNDVCANGED LIKKNNHHVE
1960 1970 1980 1990 2000
NITAKMKGLK GKVSDLEKAA AQRKAKLDEN SAFLQFNWKA DVVESWIGEK
2010 2020 2030 2040 2050
ENSLKTDDYG RDLSSVQTLL TKQETFDAGL QAFQQEGIAN ITALKDQLLA
2060 2070 2080 2090 2100
AKHIQSKAIE VRHASLMKRW NQLLANSAAR KKKLLEAQEH FRKVEDLFLT
2110 2120 2130 2140 2150
FAKKASAFNS WFENAEEDLT DPVRCNSLEE IKALREAHDA FRSSLSSAQA
2160 2170 2180 2190 2200
DFNQLAELDR QIKSFRVASN PYTWFTMEAL EETWRNLQKI IKERELELQK
2210 2220 2230 2240 2250
EQRRQEENDK LRQEFAQHAN AFHQWIQETR TYLLDGSCMV EESGTLESQL
2260 2270 2280 2290 2300
EATKRKHQEI RAMRSQLKKI EDLGAAMEEA LILDNKYTEH STVGLAQQWD
2310 2320 2330 2340 2350
QLDQLGMRMQ HNLEQQIQAR NTTGVTEEAL KEFSMMFKHF DKDKSGRLNH
2360 2370 2380 2390 2400
QEFKSCLRSL GYDLPMVEEG EPDPEFESIL DTVDPNRDGH VSLQEYMAFM
2410 2420 2430 2440 2450
ISRETENVKS SEEIESAFRA LSSERKPYVT KEELYQNLTR EQADYCISHM
2460 2470
KPYMDGKGRE LPSAYDYIEF TRSLFVN
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.
InParanoidi P07751.
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 29, 2014
This is version 140 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