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P07751

- SPTN1_CHICK

UniProt

P07751 - SPTN1_CHICK

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Protein

Spectrin alpha chain, non-erythrocytic 1

Gene
SPTAN1, SPTA2
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-calpain By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi2341 – 2352121 Reviewed predictionAdd
BLAST
Calcium bindingi2384 – 2395122 Reviewed predictionAdd
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. cell cortex Source: UniProtKB-SubCell
  2. cytoskeleton Source: UniProtKB-SubCell
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 – 11761Phosphotyrosine By 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.

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.

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 – 102660SH3Add
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 1Add
BLAST
Domaini2371 – 240636EF-hand 2Add
BLAST
Domaini2409 – 244436EF-hand 3Add
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.
Contains 3 EF-hand domains.
Contains 1 SH3 domain.
Contains 20 spectrin repeats.

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: July 9, 2014
This is version 138 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

Similar proteinsi