Q13813 (SPTN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spectrin alpha chain, non-erythrocytic 1

Alternative name(s):
Alpha-II spectrin
Fodrin alpha chain
Spectrin, non-erythroid alpha subunit

Gene names

Name:	SPTAN1
Synonyms:	NEAS, SPTA2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2472 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Like erythrocyte spectrin, the spectrin-like proteins are capable of forming dimers which can further associate to tetramers. Interacts with isoform 1 of ACP1. Interacts with CALM and EMD. Interacts (via C-terminal spectrin repeats) with TRPC4. Identified in a complex with ACTN4, CASK, IQGAP1, MAGI2, NPHS1 and SPTBN1 By similarity. Ref.14 Ref.15 Ref.17
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › cell 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.
Post-translational modification	Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by calpain in vitro By similarity.
Involvement in disease	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. Ref.26
Sequence similarities	Belongs to the spectrin family. Contains 3 EF-hand domains. Contains 1 SH3 domain. Contains 23 spectrin repeats.
Sequence caution	The sequence BAD93097.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Epilepsy Mental retardation
Domain	Repeat SH3 domain
Ligand	Actin-binding Calcium Calmodulin-binding Metal-binding
Molecular function	Actin capping
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin filament capping Inferred from electronic annotation. Source: UniProtKB-KW axon guidance Traceable author statement. Source: Reactome cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome
Cellular_component	Z disc Inferred from electronic annotation. Source: Compara cuticular plate Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome fascia adherens Inferred from electronic annotation. Source: Compara intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA lateral plasma membrane Inferred from electronic annotation. Source: Compara membrane Traceable author statement Ref.1. Source: ProtInc microtubule cytoskeleton Inferred from direct assay. Source: HPA spectrin Traceable author statement Ref.1. Source: ProtInc
Molecular_function	actin binding Traceable author statement Ref.1. Source: ProtInc calcium ion binding Inferred from electronic annotation. Source: InterPro structural constituent of cytoskeleton Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MLH1	P40692	7	EBI-351450,EBI-744248
SPTBN1	Q01082	7	EBI-351450,EBI-351561

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13813-1)

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.

Isoform 2 (identifier: Q13813-2)

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

Isoform 3 (identifier: Q13813-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2472

2472

Spectrin alpha chain, non-erythrocytic 1

PRO_0000073455

Regions

Repeat

10 – 42

33

Spectrin 1

Repeat

44 – 147

104

Spectrin 2

Repeat

149 – 253

105

Spectrin 3

Repeat

255 – 359

105

Spectrin 4

Repeat

361 – 465

105

Spectrin 5

Repeat

467 – 571

105

Spectrin 6

Repeat

573 – 676

104

Spectrin 7

Repeat

678 – 782

105

Spectrin 8

Repeat

784 – 888

105

Spectrin 9

Repeat

890 – 955

66

Spectrin 10

Domain

967 – 1026

60

SH3

Repeat

1062 – 1089

28

Spectrin 11

Repeat

1091 – 1161

71

Spectrin 12

Repeat

1208 – 1231

24

Spectrin 13

Repeat

1233 – 1337

105

Spectrin 14

Repeat

1339 – 1443

105

Spectrin 15

Repeat

1445 – 1549

105

Spectrin 16

Repeat

1551 – 1656

106

Spectrin 17

Repeat

1658 – 1762

105

Spectrin 18

Repeat

1764 – 1868

105

Spectrin 19

Repeat

1870 – 1974

105

Spectrin 20

Repeat

1976 – 2081

106

Spectrin 21

Repeat

2091 – 2195

105

Spectrin 22

Repeat

2205 – 2310

106

Spectrin 23

Domain

2323 – 2358

36

EF-hand 1

Domain

2366 – 2401

36

EF-hand 2

Domain

2404 – 2439

36

EF-hand 3

Calcium binding

2336 – 2347

12

1 Potential

Calcium binding

2379 – 2390

12

2 Potential

Sites

Site

1176 – 1177

2

Cleavage; by mu-calpain

Amino acid modifications

Modified residue

637

1

N6-acetyllysine Ref.20

Modified residue

667

1

Phosphothreonine By similarity

Modified residue

982

1

Phosphoserine Ref.21

Modified residue

999

1

Phosphoserine Ref.21

Modified residue

1029

1

Phosphoserine By similarity

Modified residue

1031

1

Phosphoserine By similarity

Modified residue

1041

1

Phosphoserine Ref.19

Modified residue

1176

1

Phosphotyrosine Ref.19

Modified residue

1217

1

Phosphoserine Ref.16 Ref.21 Ref.23

Modified residue

1519

1

N6-acetyllysine Ref.20

Modified residue

1647

1

Phosphoserine Ref.21

Modified residue

2052

1

N6-acetyllysine Ref.20

Modified residue

2421

1

N6-acetyllysine Ref.20

Natural variations

Alternative sequence

1053 – 1072

20

Missing in isoform 3.

VSP_012271

Alternative sequence

1586

1

Q → QLSKLL in isoform 2.

VSP_012270

Natural variant

385

1

N → S.
Corresponds to variant rs2227863 [ dbSNP | Ensembl ].

VAR_038513

Natural variant

904

1

S → C in a breast cancer sample; somatic mutation. Ref.25

VAR_035454

Natural variant

1017

1

P → S in a breast cancer sample; somatic mutation. Ref.25

VAR_035455

Natural variant

1300

1

I → T. Ref.1 Ref.8 Ref.9
Corresponds to variant rs1048236 [ dbSNP | Ensembl ].

VAR_012227

Natural variant

1794

1

R → W in a breast cancer sample; somatic mutation. Ref.25

VAR_035456

Natural variant

1918

1

D → N in a breast cancer sample; somatic mutation. Ref.25

VAR_035457

Natural variant

2202

1

Missing in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. Ref.26

VAR_063886

Natural variant

2303

1

R → RM in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. Ref.26

VAR_063887

Experimental info

Sequence conflict

150

1

K → N in AAA51790. Ref.1

Sequence conflict

498

1

S → F in AAA51790. Ref.1

Sequence conflict

737

1

I → V in AAA51790. Ref.1

Sequence conflict

737

1

I → V in AAA52468. Ref.8

Sequence conflict

737

1

I → V in AAA51702. Ref.9

Sequence conflict

1595

1

F → R in AAA52468. Ref.8

Sequence conflict

1595

1

F → R in AAA51702. Ref.9

Sequence conflict

1625

1

S → N in AAA51790. Ref.1

Sequence conflict

1670 – 1671

2

FD → IA in AAA51790. Ref.1

Sequence conflict

1918

1

D → A in AAA51790. Ref.1

Sequence conflict

1971 – 1972

2

KL → NV in AAA51790. Ref.1

Sequence conflict

1971 – 1972

2

KL → NV in AAB41498. Ref.2

Sequence conflict

2163

1

A → R in CAA60503. Ref.13

Sequence conflict

2347 – 2348

2

EF → DG in AAA51790. Ref.1

Sequence conflict

2448

1

Y → I in AAA51790. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

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2472

Helix Strand Turn

Details...

Helix

14 – 25

12

Helix

30 – 66

37

Beta strand

74 – 76

3

Helix

78 – 94

17

Helix

97 – 112

16

Helix

117 – 146

30

Helix

1191 – 1210

20

Helix

1337 – 1362

26

Beta strand

1369 – 1371

3

Helix

1372 – 1389

18

Helix

1392 – 1407

16

Helix

1413 – 1466

54

Helix

1489 – 1513

25

Helix

1519 – 1539

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 2, 2006. Version 3. Checksum: 4433BF74EFCEFC8A	FASTA	2,472	284,539
	10 20 30 40 50 60 MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI 70 80 90 100 110 120 QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI 130 140 150 160 170 180 RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD 190 200 210 220 230 240 LEHVEVLQKK FEEFQTDMAA HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL 250 260 270 280 290 300 KGLALQRQGK LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 310 320 330 340 350 360 ERDLAALEDK VKALCAEADR LQQSHPLSAT QIQVKREELI TNWEQIRTLA AERHARLNDS 370 380 390 400 410 420 YRLQRFLADF RDLTSWVTEM KALINADELA SDVAGAEALL DRHQEHKGEI DAHEDSFKSA 430 440 450 460 470 480 DESGQALLAA GHYASDEVRE KLTVLSEERA ALLELWELRR QQYEQCMDLQ LFYRDTEQVD 490 500 510 520 530 540 NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA 550 560 570 580 590 600 MEDVATRRDA LLSRRNALHE RAMRRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 610 620 630 640 650 660 YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKDEVA ARMNEVISLW 670 680 690 700 710 720 KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH 730 740 750 760 770 780 ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL 790 800 810 820 830 840 ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI 850 860 870 880 890 900 KAVTQKGNAM VEEGHFAAED VKAKLHELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN 910 920 930 940 950 960 EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV 970 980 990 1000 1010 1020 APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY 1030 1040 1050 1060 1070 1080 VKKLDPAQSA SRENLLEEQG SIALRQEQID NQTRITKEAG SVSLRMKQVE ELYHSLLELG 1090 1100 1110 1120 1130 1140 EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL 1150 1160 1170 1180 1190 1200 KANESRLKDI NKVAEDLESE GLMAEEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH 1210 1220 1230 1240 1250 1260 TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN 1270 1280 1290 1300 1310 1320 YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAERLI QSHPESAEDL QEKCTELNQA 1330 1340 1350 1360 1370 1380 WSSLGKRADQ RKAKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER 1390 1400 1410 1420 1430 1440 HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKQKL DILDQERADL EKAWVQRRMM 1450 1460 1470 1480 1490 1500 LDQCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 1510 1520 1530 1540 1550 1560 IAALQAFADQ LIAAGHYAKG DISSRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV 1570 1580 1590 1600 1610 1620 DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH ANADRIRGVI DMGNSLIERG 1630 1640 1650 1660 1670 1680 ACAGSEDAVK ARLAALADQW QFLVQKSAEK SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL 1690 1700 1710 1720 1730 1740 LASEDYGKDL ASVNNLLKKH QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKDKRD 1750 1760 1770 1780 1790 1800 TINGRFQKIK SMAASRRAKL NESHRLHQFF RDMDDEESWI KEKKLLVGSE DYGRDLTGVQ 1810 1820 1830 1840 1850 1860 NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGKEE IQQRLAQFVE HWKELKQLAA 1870 1880 1890 1900 1910 1920 ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD TLAAIQGLLK KHEAFETDFT 1930 1940 1950 1960 1970 1980 VHKDRVNDVC TNGQDLIKKN NHHEENISSK MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ 1990 2000 2010 2020 2030 2040 FNWKADVVES WIGEKENSLK TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK 2050 2060 2070 2080 2090 2100 DQLLAAKHVQ SKAIEARHAS LMKRWSQLLA NSAARKKKLL EAQSHFRKVE DLFLTFAKKA 2110 2120 2130 2140 2150 2160 SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL AELDRQIKSF 2170 2180 2190 2200 2210 2220 RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ EENDKLRQEF AQHANAFHQW 2230 2240 2250 2260 2270 2280 IQETRTYLLD GSCMVEESGT LESQLEATKR KHQEIRAMRS QLKKIEDLGA AMEEALILDN 2290 2300 2310 2320 2330 2340 KYTEHSTVGL AQQWDQLDQL GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS 2350 2360 2370 2380 2390 2400 GRLNHQEFKS CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET 2410 2420 2430 2440 2450 2460 ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD GKGRELPTAF 2470 DYVEFTRSLF VN
	Isoform 2 [UniParc]. Checksum: 66DC2E2F50E89E1E	FASTA	2,477	285,094
	10 20 30 40 50 60 MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI 70 80 90 100 110 120 QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI 130 140 150 160 170 180 RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD 190 200 210 220 230 240 LEHVEVLQKK FEEFQTDMAA HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL 250 260 270 280 290 300 KGLALQRQGK LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 310 320 330 340 350 360 ERDLAALEDK VKALCAEADR LQQSHPLSAT QIQVKREELI TNWEQIRTLA AERHARLNDS 370 380 390 400 410 420 YRLQRFLADF RDLTSWVTEM KALINADELA SDVAGAEALL DRHQEHKGEI DAHEDSFKSA 430 440 450 460 470 480 DESGQALLAA GHYASDEVRE KLTVLSEERA ALLELWELRR QQYEQCMDLQ LFYRDTEQVD 490 500 510 520 530 540 NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA 550 560 570 580 590 600 MEDVATRRDA LLSRRNALHE RAMRRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 610 620 630 640 650 660 YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKDEVA ARMNEVISLW 670 680 690 700 710 720 KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH 730 740 750 760 770 780 ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL 790 800 810 820 830 840 ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI 850 860 870 880 890 900 KAVTQKGNAM VEEGHFAAED VKAKLHELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN 910 920 930 940 950 960 EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV 970 980 990 1000 1010 1020 APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY 1030 1040 1050 1060 1070 1080 VKKLDPAQSA SRENLLEEQG SIALRQEQID NQTRITKEAG SVSLRMKQVE ELYHSLLELG 1090 1100 1110 1120 1130 1140 EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL 1150 1160 1170 1180 1190 1200 KANESRLKDI NKVAEDLESE GLMAEEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH 1210 1220 1230 1240 1250 1260 TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN 1270 1280 1290 1300 1310 1320 YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAERLI QSHPESAEDL QEKCTELNQA 1330 1340 1350 1360 1370 1380 WSSLGKRADQ RKAKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER 1390 1400 1410 1420 1430 1440 HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKQKL DILDQERADL EKAWVQRRMM 1450 1460 1470 1480 1490 1500 LDQCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 1510 1520 1530 1540 1550 1560 IAALQAFADQ LIAAGHYAKG DISSRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV 1570 1580 1590 1600 1610 1620 DEIEAWISEK LQTASDESYK DPTNIQLSKL LSKHQKHQAF EAELHANADR IRGVIDMGNS 1630 1640 1650 1660 1670 1680 LIERGACAGS EDAVKARLAA LADQWQFLVQ KSAEKSQKLK EANKQQNFNT GIKDFDFWLS 1690 1700 1710 1720 1730 1740 EVEALLASED YGKDLASVNN LLKKHQLLEA DISAHEDRLK DLNSQADSLM TSSAFDTSQV 1750 1760 1770 1780 1790 1800 KDKRDTINGR FQKIKSMAAS RRAKLNESHR LHQFFRDMDD EESWIKEKKL LVGSEDYGRD 1810 1820 1830 1840 1850 1860 LTGVQNLRKK HKRLEAELAA HEPAIQGVLD TGKKLSDDNT IGKEEIQQRL AQFVEHWKEL 1870 1880 1890 1900 1910 1920 KQLAAARGQR LEESLEYQQF VANVEEEEAW INEKMTLVAS EDYGDTLAAI QGLLKKHEAF 1930 1940 1950 1960 1970 1980 ETDFTVHKDR VNDVCTNGQD LIKKNNHHEE NISSKMKGLN GKVSDLEKAA AQRKAKLDEN 1990 2000 2010 2020 2030 2040 SAFLQFNWKA DVVESWIGEK ENSLKTDDYG RDLSSVQTLL TKQETFDAGL QAFQQEGIAN 2050 2060 2070 2080 2090 2100 ITALKDQLLA AKHVQSKAIE ARHASLMKRW SQLLANSAAR KKKLLEAQSH FRKVEDLFLT 2110 2120 2130 2140 2150 2160 FAKKASAFNS WFENAEEDLT DPVRCNSLEE IKALREAHDA FRSSLSSAQA DFNQLAELDR 2170 2180 2190 2200 2210 2220 QIKSFRVASN PYTWFTMEAL EETWRNLQKI IKERELELQK EQRRQEENDK LRQEFAQHAN 2230 2240 2250 2260 2270 2280 AFHQWIQETR TYLLDGSCMV EESGTLESQL EATKRKHQEI RAMRSQLKKI EDLGAAMEEA 2290 2300 2310 2320 2330 2340 LILDNKYTEH STVGLAQQWD QLDQLGMRMQ HNLEQQIQAR NTTGVTEEAL KEFSMMFKHF 2350 2360 2370 2380 2390 2400 DKDKSGRLNH QEFKSCLRSL GYDLPMVEEG EPDPEFEAIL DTVDPNRDGH VSLQEYMAFM 2410 2420 2430 2440 2450 2460 ISRETENVKS SEEIESAFRA LSSEGKPYVT KEELYQNLTR EQADYCVSHM KPYVDGKGRE 2470 LPTAFDYVEF TRSLFVN
	Isoform 3 [UniParc]. Checksum: A34BBE6ADCAF5A5C	FASTA	2,452	282,282
	10 20 30 40 50 60 MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI 70 80 90 100 110 120 QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI 130 140 150 160 170 180 RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD 190 200 210 220 230 240 LEHVEVLQKK FEEFQTDMAA HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL 250 260 270 280 290 300 KGLALQRQGK LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 310 320 330 340 350 360 ERDLAALEDK VKALCAEADR LQQSHPLSAT QIQVKREELI TNWEQIRTLA AERHARLNDS 370 380 390 400 410 420 YRLQRFLADF RDLTSWVTEM KALINADELA SDVAGAEALL DRHQEHKGEI DAHEDSFKSA 430 440 450 460 470 480 DESGQALLAA GHYASDEVRE KLTVLSEERA ALLELWELRR QQYEQCMDLQ LFYRDTEQVD 490 500 510 520 530 540 NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA 550 560 570 580 590 600 MEDVATRRDA LLSRRNALHE RAMRRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 610 620 630 640 650 660 YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKDEVA ARMNEVISLW 670 680 690 700 710 720 KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH 730 740 750 760 770 780 ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL 790 800 810 820 830 840 ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI 850 860 870 880 890 900 KAVTQKGNAM VEEGHFAAED VKAKLHELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN 910 920 930 940 950 960 EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV 970 980 990 1000 1010 1020 APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY 1030 1040 1050 1060 1070 1080 VKKLDPAQSA SRENLLEEQG SIALRQEQID NQYHSLLELG EKRKGMLEKS CKKFMLFREA 1090 1100 1110 1120 1130 1140 NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI NKVAEDLESE 1150 1160 1170 1180 1190 1200 GLMAEEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH TVATFNSIKE LNERWRSLQQ 1210 1220 1230 1240 1250 1260 LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN YGHDLASVQA LQRKHEGFER 1270 1280 1290 1300 1310 1320 DLAALGDKVN SLGETAERLI QSHPESAEDL QEKCTELNQA WSSLGKRADQ RKAKLGDSHD 1330 1340 1350 1360 1370 1380 LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ 1390 1400 1410 1420 1430 1440 FGQQLLAHGH YASPEIKQKL DILDQERADL EKAWVQRRMM LDQCLELQLF HRDCEQAENW 1450 1460 1470 1480 1490 1500 MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK IAALQAFADQ LIAAGHYAKG 1510 1520 1530 1540 1550 1560 DISSRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV DEIEAWISEK LQTASDESYK 1570 1580 1590 1600 1610 1620 DPTNIQSKHQ KHQAFEAELH ANADRIRGVI DMGNSLIERG ACAGSEDAVK ARLAALADQW 1630 1640 1650 1660 1670 1680 QFLVQKSAEK SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL LASEDYGKDL ASVNNLLKKH 1690 1700 1710 1720 1730 1740 QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKDKRD TINGRFQKIK SMAASRRAKL 1750 1760 1770 1780 1790 1800 NESHRLHQFF RDMDDEESWI KEKKLLVGSE DYGRDLTGVQ NLRKKHKRLE AELAAHEPAI 1810 1820 1830 1840 1850 1860 QGVLDTGKKL SDDNTIGKEE IQQRLAQFVE HWKELKQLAA ARGQRLEESL EYQQFVANVE 1870 1880 1890 1900 1910 1920 EEEAWINEKM TLVASEDYGD TLAAIQGLLK KHEAFETDFT VHKDRVNDVC TNGQDLIKKN 1930 1940 1950 1960 1970 1980 NHHEENISSK MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ FNWKADVVES WIGEKENSLK 1990 2000 2010 2020 2030 2040 TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK DQLLAAKHVQ SKAIEARHAS 2050 2060 2070 2080 2090 2100 LMKRWSQLLA NSAARKKKLL EAQSHFRKVE DLFLTFAKKA SAFNSWFENA EEDLTDPVRC 2110 2120 2130 2140 2150 2160 NSLEEIKALR EAHDAFRSSL SSAQADFNQL AELDRQIKSF RVASNPYTWF TMEALEETWR 2170 2180 2190 2200 2210 2220 NLQKIIKERE LELQKEQRRQ EENDKLRQEF AQHANAFHQW IQETRTYLLD GSCMVEESGT 2230 2240 2250 2260 2270 2280 LESQLEATKR KHQEIRAMRS QLKKIEDLGA AMEEALILDN KYTEHSTVGL AQQWDQLDQL 2290 2300 2310 2320 2330 2340 GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS GRLNHQEFKS CLRSLGYDLP 2350 2360 2370 2380 2390 2400 MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET ENVKSSEEIE SAFRALSSEG 2410 2420 2430 2440 2450 KPYVTKEELY QNLTREQADY CVSHMKPYVD GKGRELPTAF DYVEFTRSLF VN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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]	Erratum McMahon A.P., Giebelhaus D.H., Champion J.E., Bailes J.A., Lacey S., Carritt B., Henchman S.K., Moon R.T. Differentiation 34:241-241(1987)
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain." Nicolas G., Fournier C.M., Galand C., Malbert-Colas L., Bournier O., Kroviarski Y., Bourgeois M., Camonis J.H., Dhermy D., Grandchamp B., Lecomte M.-C. Mol. Cell. Biol. 22:3527-3536(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ACP1.
[15]	"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.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
[24]	"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.
[25]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-904; SER-1017; TRP-1794 AND ASN-1918.
[26]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00843765.
IPI00844215.
IPI00871535.

PIR

A35715.

RefSeq

NP_001123910.1. NM_001130438.2.
NP_001182461.1. NM_001195532.1.
NP_003118.2. NM_003127.3.

UniGene

Hs.372331.
Hs.732303.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FOT	X-ray	2.45	C	1172-1210	[»]
3F31	X-ray	2.30	A/B	1-147	[»]
3FB2	X-ray	2.30	A/B	1337-1544	[»]

ProteinModelPortal

Q13813.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33141N.

IntAct

Q13813. 28 interactions.

MINT

MINT-4999298.

PTM databases

PhosphoSite

Q13813.

Polymorphism databases

DMDM

94730425.

Proteomic databases

PaxDb

Q13813.

PRIDE

Q13813.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000372731; ENSP00000361816; ENSG00000197694.
ENST00000372739; ENSP00000361824; ENSG00000197694.

GeneID

6709.

KEGG

hsa:6709.

UCSC

uc004bvl.4. human.
uc004bvm.4. human.
uc004bvn.4. human.

Organism-specific databases

CTD

6709.

GeneCards

GC09P131314.

HGNC

HGNC:11273. SPTAN1.

HPA

CAB004581.
HPA007927.

MIM

182810. gene.
613477. phenotype.

neXtProt

NX_Q13813.

Orphanet

1934. Early infantile epileptic encephalopathy.

PharmGKB

PA36102.

GenAtlas

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Phylogenomic databases

eggNOG

COG5126.

HOVERGEN

HBG059266.

KO

K06114.

OMA

MELHRQW.

OrthoDB

EOG4JT04J.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.
faspathway. FAS signaling pathway (CD95).

Reactome

REACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.
REACT_127416. Developmental Biology.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

Q13813.

Bgee

Q13813.

Genevestigator

Q13813.

GermOnline

ENSG00000197694. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 2 hits.

InterPro

IPR011992. EF-hand-like_dom.
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]

Pfam

PF13499. EF_hand_5. 1 hit.
PF08726. efhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.

SMART

SM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SPTAN1. human.

EvolutionaryTrace

Q13813.

GenomeRNAi

6709.

NextBio

26162.

SOURCE

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Entry information

Entry name

SPTN1_HUMAN

Accession

Primary (citable) accession number: Q13813
Secondary accession number(s): Q13186 , Q15324, Q16606, Q59EF1, Q5VXV5, Q5VXV6, Q7Z6M5, Q9P0V0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 2, 2006
Last modified:	May 1, 2013
This is version 146 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.