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Q13813

- SPTN1_HUMAN

UniProt

Q13813 - SPTN1_HUMAN

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Protein
Spectrin alpha chain, non-erythrocytic 1
Gene
SPTAN1, NEAS, SPTA2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi2336 – 2347121 Reviewed prediction
Add
BLAST
Calcium bindingi2379 – 2390122 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. actin binding Source: ProtInc
  2. calcium ion binding Source: InterPro
  3. protein binding Source: UniProtKB
  4. structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

  1. actin filament capping Source: UniProtKB-KW
  2. apoptotic process Source: Reactome
  3. axon guidance Source: Reactome
  4. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_22266. Interaction between L1 and Ankyrins.
REACT_23832. Nephrin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin alpha chain, non-erythrocytic 1
Alternative name(s):
Alpha-II spectrin
Fodrin alpha chain
Spectrin, non-erythroid alpha subunit
Gene namesi
Name:SPTAN1
Synonyms:NEAS, SPTA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:11273. SPTAN1.

Subcellular locationi

Cytoplasmcytoskeleton. Cytoplasmcell cortex
Note: Expressed along the cell membrane in podocytes and presumptive tubule cells during glomerulogenesis and is expressed along lateral cell margins in tubule cells By similarity.

GO - Cellular componenti

  1. Z disc Source: Ensembl
  2. cuticular plate Source: Ensembl
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. fascia adherens Source: Ensembl
  6. intracellular membrane-bounded organelle Source: HPA
  7. lateral plasma membrane Source: Ensembl
  8. membrane Source: ProtInc
  9. microtubule cytoskeleton Source: HPA
  10. spectrin Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Epileptic encephalopathy, early infantile, 5 (EIEE5) [MIM:613477]: A disorder characterized by seizures associated with hypsarrhythmia, profound mental retardation with lack of visual attention and speech development, as well as spastic quadriplegia.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2202 – 22021Missing in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 1 Publication
VAR_063886
Natural varianti2303 – 23031R → RM in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 1 Publication
VAR_063887

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

MIMi613477. phenotype.
Orphaneti1934. Early infantile epileptic encephalopathy.
PharmGKBiPA36102.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24722472Spectrin alpha chain, non-erythrocytic 1
PRO_0000073455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei637 – 6371N6-acetyllysine1 Publication
Modified residuei803 – 8031N6-acetyllysine By similarity
Modified residuei982 – 9821Phosphoserine1 Publication
Modified residuei999 – 9991Phosphoserine1 Publication
Modified residuei1041 – 10411Phosphoserine1 Publication
Modified residuei1176 – 11761Phosphotyrosine1 Publication
Modified residuei1217 – 12171Phosphoserine3 Publications
Modified residuei1519 – 15191N6-acetyllysine1 Publication
Modified residuei1647 – 16471Phosphoserine1 Publication
Modified residuei2052 – 20521N6-acetyllysine1 Publication
Modified residuei2421 – 24211N6-acetyllysine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13813.
PaxDbiQ13813.
PRIDEiQ13813.

PTM databases

PhosphoSiteiQ13813.

Expressioni

Gene expression databases

ArrayExpressiQ13813.
BgeeiQ13813.
GenevestigatoriQ13813.

Organism-specific databases

HPAiCAB004581.
HPA007927.

Interactioni

Subunit structurei

Like erythrocyte spectrin, the spectrin-like proteins are capable of forming dimers which can further associate to tetramers. Interacts (via C-terminal spectrin repeats) with TRPC4. Interacts with CALM and EMD. Interacts with isoform 1 of ACP1. Identified in a complex with ACTN4, CASK, IQGAP1, MAGI2, NPHS1 and SPTBN1. Interacts with SHANK3 (via ANK repeats).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EVLQ9UI084EBI-351450,EBI-346653
FANCGO152874EBI-351450,EBI-81610
MLH1P406927EBI-351450,EBI-744248
SPTBN1Q010827EBI-351450,EBI-351561

Protein-protein interaction databases

BioGridi112587. 114 interactions.
DIPiDIP-33141N.
IntActiQ13813. 45 interactions.
MINTiMINT-4999298.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2512
Helixi30 – 6637
Beta strandi74 – 763
Helixi78 – 9417
Helixi97 – 11216
Helixi117 – 14630
Helixi1191 – 121020
Helixi1337 – 136226
Beta strandi1369 – 13713
Helixi1372 – 138918
Helixi1392 – 140716
Helixi1413 – 146654
Helixi1489 – 151325
Helixi1519 – 153921

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FOTX-ray2.45C1172-1211[»]
3F31X-ray2.30A/B1-147[»]
3FB2X-ray2.30A/B1337-1544[»]
ProteinModelPortaliQ13813.
SMRiQ13813. Positions 8-2316, 2320-2470.

Miscellaneous databases

EvolutionaryTraceiQ13813.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati10 – 4233Spectrin 1
Add
BLAST
Repeati44 – 147104Spectrin 2
Add
BLAST
Repeati149 – 253105Spectrin 3
Add
BLAST
Repeati255 – 359105Spectrin 4
Add
BLAST
Repeati361 – 465105Spectrin 5
Add
BLAST
Repeati467 – 571105Spectrin 6
Add
BLAST
Repeati573 – 676104Spectrin 7
Add
BLAST
Repeati678 – 782105Spectrin 8
Add
BLAST
Repeati784 – 888105Spectrin 9
Add
BLAST
Repeati890 – 95566Spectrin 10
Add
BLAST
Domaini967 – 102660SH3
Add
BLAST
Repeati1062 – 108928Spectrin 11
Add
BLAST
Repeati1091 – 116171Spectrin 12
Add
BLAST
Repeati1208 – 123124Spectrin 13
Add
BLAST
Repeati1233 – 1337105Spectrin 14
Add
BLAST
Repeati1339 – 1443105Spectrin 15
Add
BLAST
Repeati1445 – 1549105Spectrin 16
Add
BLAST
Repeati1551 – 1656106Spectrin 17
Add
BLAST
Repeati1658 – 1762105Spectrin 18
Add
BLAST
Repeati1764 – 1868105Spectrin 19
Add
BLAST
Repeati1870 – 1974105Spectrin 20
Add
BLAST
Repeati1976 – 2081106Spectrin 21
Add
BLAST
Repeati2091 – 2195105Spectrin 22
Add
BLAST
Repeati2205 – 2310106Spectrin 23
Add
BLAST
Domaini2323 – 235836EF-hand 1
Add
BLAST
Domaini2366 – 240136EF-hand 2
Add
BLAST
Domaini2404 – 243936EF-hand 3
Add
BLAST

Sequence similaritiesi

Belongs to the spectrin family.
Contains 3 EF-hand domains.
Contains 1 SH3 domain.
Contains 23 spectrin repeats.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG5126.
HOVERGENiHBG059266.
KOiK06114.
OrthoDBiEOG7GXP9K.
PhylomeDBiQ13813.
TreeFamiTF343803.

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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13813-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ     50
RDAEELEKWI QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV 100
KLDETGNLMI SEGHFASETI RTRLMELHRQ WELLLEKMRE KGIKLLQAQK 150
LVQYLRECED VMDWINDKEA IVTSEELGQD LEHVEVLQKK FEEFQTDMAA 200
HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL KGLALQRQGK 250
LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 300
ERDLAALEDK VKALCAEADR LQQSHPLSAT QIQVKREELI TNWEQIRTLA 350
AERHARLNDS YRLQRFLADF RDLTSWVTEM KALINADELA SDVAGAEALL 400
DRHQEHKGEI DAHEDSFKSA DESGQALLAA GHYASDEVRE KLTVLSEERA 450
ALLELWELRR QQYEQCMDLQ LFYRDTEQVD NWMSKQEAFL LNEDLGDSLD 500
SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA MEDVATRRDA 550
LLSRRNALHE RAMRRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 600
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKDEVA 650
ARMNEVISLW KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH 700
LASDDYGKDL TNVQNLQKKH ALLEADVAAH QDRIDGITIQ ARQFQDAGHF 750
DAENIKKKQE ALVARYEALK EPMVARKQKL ADSLRLQQLF RDVEDEETWI 800
REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI KAVTQKGNAM 850
VEEGHFAAED VKAKLHELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN 900
EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR 950
EQAQSCRQQV APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST 1000
NKDWWKVEVN DRQGFVPAAY VKKLDPAQSA SRENLLEEQG SIALRQEQID 1050
NQTRITKEAG SVSLRMKQVE ELYHSLLELG EKRKGMLEKS CKKFMLFREA 1100
NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI 1150
NKVAEDLESE GLMAEEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH 1200
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE 1250
EKNQALNTDN YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAERLI 1300
QSHPESAEDL QEKCTELNQA WSSLGKRADQ RKAKLGDSHD LQRFLSDFRD 1350
LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ 1400
FGQQLLAHGH YASPEIKQKL DILDQERADL EKAWVQRRMM LDQCLELQLF 1450
HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 1500
IAALQAFADQ LIAAGHYAKG DISSRRNEVL DRWRRLKAQM IEKRSKLGES 1550
QTLQQFSRDV DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH 1600
ANADRIRGVI DMGNSLIERG ACAGSEDAVK ARLAALADQW QFLVQKSAEK 1650
SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL LASEDYGKDL ASVNNLLKKH 1700
QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKDKRD TINGRFQKIK 1750
SMAASRRAKL NESHRLHQFF RDMDDEESWI KEKKLLVGSE DYGRDLTGVQ 1800
NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGKEE IQQRLAQFVE 1850
HWKELKQLAA ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD 1900
TLAAIQGLLK KHEAFETDFT VHKDRVNDVC TNGQDLIKKN NHHEENISSK 1950
MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ FNWKADVVES WIGEKENSLK 2000
TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK DQLLAAKHVQ 2050
SKAIEARHAS LMKRWSQLLA NSAARKKKLL EAQSHFRKVE DLFLTFAKKA 2100
SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL 2150
AELDRQIKSF RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ 2200
EENDKLRQEF AQHANAFHQW IQETRTYLLD GSCMVEESGT LESQLEATKR 2250
KHQEIRAMRS QLKKIEDLGA AMEEALILDN KYTEHSTVGL AQQWDQLDQL 2300
GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS GRLNHQEFKS 2350
CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET 2400
ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD 2450
GKGRELPTAF DYVEFTRSLF VN 2472
Length:2,472
Mass (Da):284,539
Last modified:May 2, 2006 - v3
Checksum:i4433BF74EFCEFC8A
GO
Isoform 2 (identifier: Q13813-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1586-1586: Q → QLSKLL

Show »
Length:2,477
Mass (Da):285,094
Checksum:i66DC2E2F50E89E1E
GO
Isoform 3 (identifier: Q13813-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1053-1072: Missing.

Show »
Length:2,452
Mass (Da):282,282
Checksum:iA34BBE6ADCAF5A5C
GO

Sequence cautioni

The sequence BAD93097.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti385 – 3851N → S.
Corresponds to variant rs2227863 [ dbSNP | Ensembl ].
VAR_038513
Natural varianti904 – 9041S → C in a breast cancer sample; somatic mutation. 1 Publication
VAR_035454
Natural varianti1017 – 10171P → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_035455
Natural varianti1300 – 13001I → T.3 Publications
Corresponds to variant rs1048236 [ dbSNP | Ensembl ].
VAR_012227
Natural varianti1794 – 17941R → W in a breast cancer sample; somatic mutation. 1 Publication
VAR_035456
Natural varianti1918 – 19181D → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_035457
Natural varianti2202 – 22021Missing in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 1 Publication
VAR_063886
Natural varianti2303 – 23031R → RM in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 1 Publication
VAR_063887

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1053 – 107220Missing in isoform 3.
VSP_012271Add
BLAST
Alternative sequencei1586 – 15861Q → QLSKLL in isoform 2.
VSP_012270

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501K → N in AAA51790. 1 Publication
Sequence conflicti498 – 4981S → F in AAA51790. 1 Publication
Sequence conflicti737 – 7371I → V in AAA51790. 1 Publication
Sequence conflicti737 – 7371I → V in AAA52468. 1 Publication
Sequence conflicti737 – 7371I → V in AAA51702. 1 Publication
Sequence conflicti1595 – 15951F → R in AAA52468. 1 Publication
Sequence conflicti1595 – 15951F → R in AAA51702. 1 Publication
Sequence conflicti1625 – 16251S → N in AAA51790. 1 Publication
Sequence conflicti1670 – 16712FD → IA in AAA51790. 1 Publication
Sequence conflicti1918 – 19181D → A in AAA51790. 1 Publication
Sequence conflicti1971 – 19722KL → NV in AAA51790. 1 Publication
Sequence conflicti1971 – 19722KL → NV in AAB41498. 1 Publication
Sequence conflicti2163 – 21631A → R in CAA60503. 1 Publication
Sequence conflicti2347 – 23482EF → DG in AAA51790. 1 Publication
Sequence conflicti2448 – 24481Y → I in AAA51790. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05243 mRNA. Translation: AAA51790.1.
U83867 mRNA. Translation: AAB41498.1.
AB191262 mRNA. Translation: BAD52438.1.
AB209860 mRNA. Translation: BAD93097.1. Different initiation.
AL356481 Genomic DNA. Translation: CAH71404.1.
AL356481 Genomic DNA. Translation: CAH71405.1.
BC053521 mRNA. Translation: AAH53521.1.
M24773 mRNA. Translation: AAA52468.1.
M18627 mRNA. Translation: AAA51702.1.
U26396 mRNA. Translation: AAB60364.1.
AF148808 Genomic DNA. Translation: AAF26672.1.
X86901 mRNA. Translation: CAA60503.1.
CCDSiCCDS48036.1. [Q13813-2]
CCDS6905.1. [Q13813-1]
PIRiA35715.
RefSeqiNP_001123910.1. NM_001130438.2. [Q13813-2]
NP_001182461.1. NM_001195532.1. [Q13813-3]
NP_003118.2. NM_003127.3. [Q13813-1]
UniGeneiHs.372331.

Genome annotation databases

EnsembliENST00000372731; ENSP00000361816; ENSG00000197694. [Q13813-1]
ENST00000372739; ENSP00000361824; ENSG00000197694. [Q13813-2]
GeneIDi6709.
KEGGihsa:6709.
UCSCiuc004bvl.4. human. [Q13813-1]
uc004bvm.4. human. [Q13813-2]
uc004bvn.4. human. [Q13813-3]

Polymorphism databases

DMDMi94730425.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05243 mRNA. Translation: AAA51790.1 .
U83867 mRNA. Translation: AAB41498.1 .
AB191262 mRNA. Translation: BAD52438.1 .
AB209860 mRNA. Translation: BAD93097.1 . Different initiation.
AL356481 Genomic DNA. Translation: CAH71404.1 .
AL356481 Genomic DNA. Translation: CAH71405.1 .
BC053521 mRNA. Translation: AAH53521.1 .
M24773 mRNA. Translation: AAA52468.1 .
M18627 mRNA. Translation: AAA51702.1 .
U26396 mRNA. Translation: AAB60364.1 .
AF148808 Genomic DNA. Translation: AAF26672.1 .
X86901 mRNA. Translation: CAA60503.1 .
CCDSi CCDS48036.1. [Q13813-2 ]
CCDS6905.1. [Q13813-1 ]
PIRi A35715.
RefSeqi NP_001123910.1. NM_001130438.2. [Q13813-2 ]
NP_001182461.1. NM_001195532.1. [Q13813-3 ]
NP_003118.2. NM_003127.3. [Q13813-1 ]
UniGenei Hs.372331.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FOT X-ray 2.45 C 1172-1211 [» ]
3F31 X-ray 2.30 A/B 1-147 [» ]
3FB2 X-ray 2.30 A/B 1337-1544 [» ]
ProteinModelPortali Q13813.
SMRi Q13813. Positions 8-2316, 2320-2470.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112587. 114 interactions.
DIPi DIP-33141N.
IntActi Q13813. 45 interactions.
MINTi MINT-4999298.

PTM databases

PhosphoSitei Q13813.

Polymorphism databases

DMDMi 94730425.

Proteomic databases

MaxQBi Q13813.
PaxDbi Q13813.
PRIDEi Q13813.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372731 ; ENSP00000361816 ; ENSG00000197694 . [Q13813-1 ]
ENST00000372739 ; ENSP00000361824 ; ENSG00000197694 . [Q13813-2 ]
GeneIDi 6709.
KEGGi hsa:6709.
UCSCi uc004bvl.4. human. [Q13813-1 ]
uc004bvm.4. human. [Q13813-2 ]
uc004bvn.4. human. [Q13813-3 ]

Organism-specific databases

CTDi 6709.
GeneCardsi GC09P131314.
HGNCi HGNC:11273. SPTAN1.
HPAi CAB004581.
HPA007927.
MIMi 182810. gene.
613477. phenotype.
neXtProti NX_Q13813.
Orphaneti 1934. Early infantile epileptic encephalopathy.
PharmGKBi PA36102.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5126.
HOVERGENi HBG059266.
KOi K06114.
OrthoDBi EOG7GXP9K.
PhylomeDBi Q13813.
TreeFami TF343803.

Enzyme and pathway databases

Reactomei REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_22266. Interaction between L1 and Ankyrins.
REACT_23832. Nephrin interactions.

Miscellaneous databases

ChiTaRSi SPTAN1. human.
EvolutionaryTracei Q13813.
GeneWikii SPTAN1.
GenomeRNAii 6709.
NextBioi 26162.
PROi Q13813.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13813.
Bgeei Q13813.
Genevestigatori Q13813.

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

« Hide 'large scale' publications
  1. "Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin."
    Moon R.T., McMahon A.P.
    J. Biol. Chem. 265:4427-4433(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-1300.
  2. "Brain and muscle express a unique alternative transcript of alphaII spectrin."
    Cianci C.D., Zhang Z., Pradhan D., Morrow J.S.
    Biochemistry 38:15721-15730(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    Tissue: Fetal brain.
  3. "Human full-length cDNA starting with the capped site sequence."
    Kato S.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Aorta.
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Uterus.
  7. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 157-168; 970-981; 990-1002; 1608-1619; 2138-2155 AND 2455-2467, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  8. "Structure and evolution of a non-erythroid spectrin, human alpha-fodrin."
    McMahon A.P., Moon R.T.
    Biochem. Soc. Trans. 15:804-807(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 676-1595 (ISOFORM 1), VARIANT THR-1300.
    Tissue: Lung.
  9. "cDNA cloning, sequencing and chromosome mapping of a non-erythroid spectrin, human alpha-fodrin."
    McMahon A.P., Giebelhaus D.H., Champion J.E., Bailes J.A., Lacey S., Carritt B., Henchman S.K., Moon R.T.
    Differentiation 34:68-78(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 676-1595 (ISOFORM 1), VARIANT THR-1300.
  10. "Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility."
    Stabach P.R., Cianci C.D., Glantz S.B., Zhang Z., Morrow J.S.
    Biochemistry 36:57-65(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 811-1529 (ISOFORMS 1/2), MUTAGENESIS.
  11. "Association and linkage analyses of the nonerythroid alpha-spectrin (SPTAN1) gene on chromosome 9q34 with a large Swedish kindred."
    Murakami N., Speed W.C., Seaman M.I., Zychowski R.L., Wetterberg L., Pakstis A.J., Kidd J.R., Kidd K.K.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1073-1349.
  12. "Cloning, expression and characterization of two putative calcium-binding sites in human non-erythroid alpha-spectrin."
    Lundberg S., Bjoerk J., Loefvenberg L., Backman L.
    Eur. J. Biochem. 230:658-665(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2059-2433 (ISOFORMS 1/2/3).
    Tissue: Fetal liver.
  13. Cited for: INTERACTION WITH ACP1.
  14. "Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane."
    Holaska J.M., Kowalski A.K., Wilson K.L.
    PLoS Biol. 2:1354-1362(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMD.
  15. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "The spectrin cytoskeleton influences the surface expression and activation of human transient receptor potential channel 4 channels."
    Odell A.F., Van Helden D.F., Scott J.L.
    J. Biol. Chem. 283:4395-4407(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRPC4.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1041 AND TYR-1176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-637; LYS-1519; LYS-2052 AND LYS-2421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-982; SER-999; SER-1217 AND SER-1647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity."
    Simonovic M., Zhang Z., Cianci C.D., Steitz T.A., Morrow J.S.
    J. Biol. Chem. 281:34333-34340(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1172-1210 IN COMPLEX WITH CALM.
  26. Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-904; SER-1017; TRP-1794 AND ASN-1918.
  27. "Dominant-negative mutations in alpha-II spectrin cause West syndrome with severe cerebral hypomyelination, spastic quadriplegia, and developmental delay."
    Saitsu H., Tohyama J., Kumada T., Egawa K., Hamada K., Okada I., Mizuguchi T., Osaka H., Miyata R., Furukawa T., Haginoya K., Hoshino H., Goto T., Hachiya Y., Yamagata T., Saitoh S., Nagai T., Nishiyama K.
    , Nishimura A., Miyake N., Komada M., Hayashi K., Hirai S., Ogata K., Kato M., Fukuda A., Matsumoto N.
    Am. J. Hum. Genet. 86:881-891(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EIEE5 GLU-2202 DEL AND MET-2303 INS, CHARACTERIZATION OF VARIANTS EIEE5 GLU-2202 DEL AND MET-2303 INS.

Entry informationi

Entry nameiSPTN1_HUMAN
AccessioniPrimary (citable) accession number: Q13813
Secondary accession number(s): Q13186
, Q15324, Q16606, Q59EF1, Q5VXV5, Q5VXV6, Q7Z6M5, Q9P0V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 2, 2006
Last modified: September 3, 2014
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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