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UniProtKB - Q13813 (SPTN1_HUMAN)

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Protein

Spectrin alpha chain, non-erythrocytic 1

Gene

SPTAN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi2336 – 23471PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi2379 – 23902PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • actin binding Source: ProtInc
  • cadherin binding Source: BHF-UCL
  • calcium ion binding Source: InterPro
  • calmodulin binding Source: UniProtKB-KW
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • structural constituent of cytoskeleton Source: ProtInc
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActin capping, Actin-binding, Calmodulin-binding
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-264870 Caspase-mediated cleavage of cytoskeletal proteins
R-HSA-373753 Nephrin family interactions
R-HSA-375165 NCAM signaling for neurite out-growth
R-HSA-445095 Interaction between L1 and Ankyrins
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6798695 Neutrophil degranulation
R-HSA-6807878 COPI-mediated anterograde transport
SIGNORiQ13813

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000197694.13
HGNCiHGNC:11273 SPTAN1
MIMi182810 gene
neXtProtiNX_Q13813

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Epileptic encephalopathy, early infantile, 5 (EIEE5)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by seizures associated with hypsarrhythmia, profound mental retardation with lack of visual attention and speech development, as well as spastic quadriplegia.
See also OMIM:613477
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0638862202Missing in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 2 Publications1
Natural variantiVAR_0638872304M → MRM in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 1 Publication1

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

DisGeNETi6709
MalaCardsiSPTAN1
MIMi613477 phenotype
OpenTargetsiENSG00000197694
Orphaneti3451 West syndrome
PharmGKBiPA36102

Polymorphism and mutation databases

BioMutaiSPTAN1
DMDMi94730425

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000734551 – 2472Spectrin alpha chain, non-erythrocytic 1Add BLAST2472

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei587PhosphoserineBy similarity1
Modified residuei637N6-acetyllysineCombined sources1
Modified residuei803N6-acetyllysineBy similarity1
Modified residuei924PhosphoserineBy similarity1
Modified residuei982PhosphoserineCombined sources1
Modified residuei999PhosphoserineCombined sources1
Modified residuei1029PhosphoserineBy similarity1
Modified residuei1031PhosphoserineCombined sources1
Modified residuei1041PhosphoserineCombined sources1
Modified residuei1176PhosphotyrosineCombined sources1
Modified residuei1190PhosphoserineBy similarity1
Modified residuei1207PhosphoserineCombined sources1
Modified residuei1217PhosphoserineCombined sources1
Modified residuei1291PhosphoserineBy similarity1
Modified residuei1306PhosphoserineCombined sources1
Modified residuei1323PhosphoserineCombined sources1
Modified residuei1338PhosphoserineCombined sources1
Modified residuei1519N6-acetyllysineCombined sources1
Modified residuei1550PhosphoserineCombined sources1
Modified residuei1557PhosphoserineCombined sources1
Modified residuei1578PhosphoserineCombined sources1
Modified residuei1615PhosphoserineCombined sources1
Modified residuei1647PhosphoserineCombined sources1
Modified residuei2020PhosphothreonineCombined sources1
Modified residuei2052N6-acetyllysineCombined sources1
Modified residuei2421N6-acetyllysineCombined sources1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1176 – 1177Cleavage; by mu-calpain2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13813
MaxQBiQ13813
PaxDbiQ13813
PeptideAtlasiQ13813
PRIDEiQ13813
ProteomicsDBi59689
59690 [Q13813-2]
59691 [Q13813-3]

PTM databases

CarbonylDBiQ13813
iPTMnetiQ13813
PhosphoSitePlusiQ13813
SwissPalmiQ13813

Expressioni

Gene expression databases

BgeeiENSG00000197694
ExpressionAtlasiQ13813 baseline and differential
GenevisibleiQ13813 HS

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).4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin binding Source: ProtInc
  • cadherin binding Source: BHF-UCL
  • calmodulin binding Source: UniProtKB-KW
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi112587, 184 interactors
CORUMiQ13813
DIPiDIP-33141N
IntActiQ13813, 111 interactors
MINTiQ13813
STRINGi9606.ENSP00000361824

Structurei

Secondary structure

12472
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 25Combined sources12
Helixi30 – 66Combined sources37
Beta strandi74 – 76Combined sources3
Helixi78 – 94Combined sources17
Helixi97 – 112Combined sources16
Helixi117 – 146Combined sources30
Turni967 – 969Combined sources3
Beta strandi971 – 974Combined sources4
Beta strandi993 – 998Combined sources6
Beta strandi1001 – 1009Combined sources9
Beta strandi1012 – 1017Combined sources6
Helixi1018 – 1020Combined sources3
Beta strandi1021 – 1023Combined sources3
Helixi1191 – 1210Combined sources20
Helixi1337 – 1362Combined sources26
Beta strandi1369 – 1371Combined sources3
Helixi1372 – 1389Combined sources18
Helixi1392 – 1407Combined sources16
Helixi1413 – 1466Combined sources54
Helixi1480 – 1487Combined sources8
Helixi1489 – 1513Combined sources25
Helixi1519 – 1539Combined sources21

3D structure databases

ProteinModelPortaliQ13813
SMRiQ13813
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13813

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati45 – 146Spectrin 1Sequence analysisAdd BLAST102
Repeati150 – 251Spectrin 2Sequence analysisAdd BLAST102
Repeati256 – 358Spectrin 3Sequence analysisAdd BLAST103
Repeati361 – 465Spectrin 4Sequence analysisAdd BLAST105
Repeati468 – 570Spectrin 5Sequence analysisAdd BLAST103
Repeati574 – 676Spectrin 6Sequence analysisAdd BLAST103
Repeati679 – 781Spectrin 7Sequence analysisAdd BLAST103
Repeati785 – 888Spectrin 8Sequence analysisAdd BLAST104
Repeati891 – 969Spectrin 9Sequence analysisAdd BLAST79
Domaini967 – 1026SH3PROSITE-ProRule annotationAdd BLAST60
Repeati1096 – 1166Spectrin 10Sequence analysisAdd BLAST71
Repeati1233 – 1336Spectrin 11Sequence analysisAdd BLAST104
Repeati1339 – 1442Spectrin 12Sequence analysis1 PublicationAdd BLAST104
Repeati1446 – 1549Spectrin 13Sequence analysis1 PublicationAdd BLAST104
Repeati1552 – 1656Spectrin 14Sequence analysisAdd BLAST105
Repeati1659 – 1762Spectrin 15Sequence analysisAdd BLAST104
Repeati1764 – 1868Spectrin 16Sequence analysisAdd BLAST105
Repeati1871 – 1974Spectrin 17Sequence analysisAdd BLAST104
Repeati1978 – 2081Spectrin 18Sequence analysisAdd BLAST104
Repeati2092 – 2194Spectrin 19Sequence analysisAdd BLAST103
Repeati2206 – 2310Spectrin 20Sequence analysisAdd BLAST105
Domaini2323 – 2358EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini2366 – 2401EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini2404 – 2439EF-hand 3PROSITE-ProRule annotationAdd BLAST36

Sequence similaritiesi

Belongs to the spectrin family.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG0035 Eukaryota
COG5069 LUCA
GeneTreeiENSGT00760000118813
HOVERGENiHBG059266
InParanoidiQ13813
KOiK06114
PhylomeDBiQ13813
TreeFamiTF343803

Family and domain databases

CDDicd00051 EFh, 1 hit
cd11808 SH3_Alpha_Spectrin, 1 hit
InterProiView protein in InterPro
IPR035825 Alpha_Spectrin_SH3
IPR011992 EF-hand-dom_pair
IPR014837 EF-hand_Ca_insen
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR018159 Spectrin/alpha-actinin
IPR002017 Spectrin_repeat
PfamiView protein in Pfam
PF13499 EF-hand_7, 1 hit
PF08726 EFhand_Ca_insen, 1 hit
PF00018 SH3_1, 1 hit
PF00435 Spectrin, 20 hits
PRINTSiPR00452 SH3DOMAIN
SMARTiView protein in SMART
SM00054 EFh, 2 hits
SM00326 SH3, 1 hit
SM00150 SPEC, 20 hits
SUPFAMiSSF47473 SSF47473, 1 hit
SSF50044 SSF50044, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 2 hits
PS50222 EF_HAND_2, 3 hits
PS50002 SH3, 1 hit

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ 
        60         70         80         90        100
RDAEELEKWI QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV 
       110        120        130        140        150
KLDETGNLMI SEGHFASETI RTRLMELHRQ WELLLEKMRE KGIKLLQAQK 
       160        170        180        190        200
LVQYLRECED VMDWINDKEA IVTSEELGQD LEHVEVLQKK FEEFQTDMAA 
       210        220        230        240        250
HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL KGLALQRQGK 
       260        270        280        290        300
LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 
       310        320        330        340        350
ERDLAALEDK VKALCAEADR LQQSHPLSAT QIQVKREELI TNWEQIRTLA 
       360        370        380        390        400
AERHARLNDS YRLQRFLADF RDLTSWVTEM KALINADELA SDVAGAEALL 
       410        420        430        440        450
DRHQEHKGEI DAHEDSFKSA DESGQALLAA GHYASDEVRE KLTVLSEERA 
       460        470        480        490        500
ALLELWELRR QQYEQCMDLQ LFYRDTEQVD NWMSKQEAFL LNEDLGDSLD 
       510        520        530        540        550
SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA MEDVATRRDA 
       560        570        580        590        600
LLSRRNALHE RAMRRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 
       610        620        630        640        650
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKDEVA 
       660        670        680        690        700
ARMNEVISLW KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH 
       710        720        730        740        750
LASDDYGKDL TNVQNLQKKH ALLEADVAAH QDRIDGITIQ ARQFQDAGHF 
       760        770        780        790        800
DAENIKKKQE ALVARYEALK EPMVARKQKL ADSLRLQQLF RDVEDEETWI 
       810        820        830        840        850
REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI KAVTQKGNAM 
       860        870        880        890        900
VEEGHFAAED VKAKLHELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN 
       910        920        930        940        950
EAESWMREKE 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
NQTRITKEAG SVSLRMKQVE ELYHSLLELG EKRKGMLEKS CKKFMLFREA 
      1110       1120       1130       1140       1150
NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI 
      1160       1170       1180       1190       1200
NKVAEDLESE GLMAEEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH 
      1210       1220       1230       1240       1250
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE 
      1260       1270       1280       1290       1300
EKNQALNTDN YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAERLI 
      1310       1320       1330       1340       1350
QSHPESAEDL QEKCTELNQA WSSLGKRADQ RKAKLGDSHD LQRFLSDFRD 
      1360       1370       1380       1390       1400
LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ 
      1410       1420       1430       1440       1450
FGQQLLAHGH YASPEIKQKL DILDQERADL EKAWVQRRMM LDQCLELQLF 
      1460       1470       1480       1490       1500
HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 
      1510       1520       1530       1540       1550
IAALQAFADQ LIAAGHYAKG DISSRRNEVL DRWRRLKAQM IEKRSKLGES 
      1560       1570       1580       1590       1600
QTLQQFSRDV DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH 
      1610       1620       1630       1640       1650
ANADRIRGVI DMGNSLIERG ACAGSEDAVK ARLAALADQW QFLVQKSAEK 
      1660       1670       1680       1690       1700
SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL LASEDYGKDL ASVNNLLKKH 
      1710       1720       1730       1740       1750
QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKDKRD TINGRFQKIK 
      1760       1770       1780       1790       1800
SMAASRRAKL NESHRLHQFF RDMDDEESWI KEKKLLVGSE DYGRDLTGVQ 
      1810       1820       1830       1840       1850
NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGKEE IQQRLAQFVE 
      1860       1870       1880       1890       1900
HWKELKQLAA ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD 
      1910       1920       1930       1940       1950
TLAAIQGLLK KHEAFETDFT VHKDRVNDVC TNGQDLIKKN NHHEENISSK 
      1960       1970       1980       1990       2000
MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ FNWKADVVES WIGEKENSLK 
      2010       2020       2030       2040       2050
TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK DQLLAAKHVQ 
      2060       2070       2080       2090       2100
SKAIEARHAS LMKRWSQLLA NSAARKKKLL EAQSHFRKVE DLFLTFAKKA 
      2110       2120       2130       2140       2150
SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL 
      2160       2170       2180       2190       2200
AELDRQIKSF RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ 
      2210       2220       2230       2240       2250
EENDKLRQEF AQHANAFHQW IQETRTYLLD GSCMVEESGT LESQLEATKR 
      2260       2270       2280       2290       2300
KHQEIRAMRS QLKKIEDLGA AMEEALILDN KYTEHSTVGL AQQWDQLDQL 
      2310       2320       2330       2340       2350
GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS GRLNHQEFKS 
      2360       2370       2380       2390       2400
CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET 
      2410       2420       2430       2440       2450
ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD 
      2460       2470 
GKGRELPTAF DYVEFTRSLF VN
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti150K → N in AAA51790 (PubMed:2307671).Curated1
Sequence conflicti498S → F in AAA51790 (PubMed:2307671).Curated1
Sequence conflicti737I → V in AAA51790 (PubMed:2307671).Curated1
Sequence conflicti737I → V in AAA52468 (PubMed:3691949).Curated1
Sequence conflicti737I → V in AAA51702 (PubMed:3038643).Curated1
Sequence conflicti1595F → R in AAA52468 (PubMed:3691949).Curated1
Sequence conflicti1595F → R in AAA51702 (PubMed:3038643).Curated1
Sequence conflicti1625S → N in AAA51790 (PubMed:2307671).Curated1
Sequence conflicti1670 – 1671FD → IA in AAA51790 (PubMed:2307671).Curated2
Sequence conflicti1918D → A in AAA51790 (PubMed:2307671).Curated1
Sequence conflicti1971 – 1972KL → NV in AAA51790 (PubMed:2307671).Curated2
Sequence conflicti1971 – 1972KL → NV in AAB41498 (PubMed:10625438).Curated2
Sequence conflicti2163A → R in CAA60503 (PubMed:7607240).Curated1
Sequence conflicti2347 – 2348EF → DG in AAA51790 (PubMed:2307671).Curated2
Sequence conflicti2448Y → I in AAA51790 (PubMed:2307671).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_038513385N → S. Corresponds to variant dbSNP:rs2227863EnsemblClinVar.1
Natural variantiVAR_035454904S → C in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0354551017P → S in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0122271300I → T3 PublicationsCorresponds to variant dbSNP:rs1048236EnsemblClinVar.1
Natural variantiVAR_0354561794R → W in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0354571918D → N in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0638862202Missing in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 2 Publications1
Natural variantiVAR_0638872304M → MRM in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0122711053 – 1072Missing in isoform 3. 2 PublicationsAdd BLAST20
Alternative sequenceiVSP_0122701586Q → QLSKLL in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 No translation available.
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]
CCDS75914.1 [Q13813-3]
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

EnsembliENST00000358161; ENSP00000350882; ENSG00000197694 [Q13813-3]
ENST00000372731; ENSP00000361816; ENSG00000197694 [Q13813-1]
ENST00000372739; ENSP00000361824; ENSG00000197694 [Q13813-2]
GeneIDi6709
KEGGihsa:6709
UCSCiuc004bvl.5 human [Q13813-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSPTN1_HUMAN
AccessioniPrimary (citable) accession number: Q13813
Secondary accession number(s): Q13186
, Q15324, Q16606, Q59EF1, Q5VXV5, Q5VXV6, Q7Z6M5, Q9P0V0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 2, 2006
Last modified: July 18, 2018
This is version 203 of the entry and version 3 of the sequence. See 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

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