Q01082 (SPTB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spectrin beta chain, non-erythrocytic 1

Alternative name(s):
Beta-II spectrin
Fodrin beta chain
Spectrin, non-erythroid beta chain 1

Gene names

Name:	SPTBN1
Synonyms:	SPTB2

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	2364 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 to form dimers which can further associate to tetramers. The short form cannot bind to the axonal protein fodaxin. Interacts with ANK2. Ref.9
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cytoplasm › myofibril › sarcomere › M line By similarity. Note: Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes By similarity. Isoform 2: Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity.
Tissue specificity	Isoform 2 is present in brain, lung and kidney (at protein level). Ref.2
Post-translational modification	Isoform 2 is phosphorylated on Ser-8 and Ser-10 By similarity.
Sequence similarities	Belongs to the spectrin family. Contains 2 CH (calponin-homology) domains. Contains 1 PH domain. Contains 17 spectrin repeats.
Sequence caution	The sequence BAD92985.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Actin-binding Calmodulin-binding
Molecular function	Actin capping
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi to plasma membrane protein transport Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL SMAD protein import into nucleus Inferred from electronic annotation. Source: Compara actin filament capping Inferred from electronic annotation. Source: UniProtKB-KW axon guidance Traceable author statement. Source: Reactome common-partner SMAD protein phosphorylation Inferred from electronic annotation. Source: Compara cytokinesis after mitosis Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL membrane assembly Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL protein targeting to plasma membrane Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL
Cellular_component	M band Inferred from electronic annotation. Source: UniProtKB-SubCell axolemma Inferred from sequence or structural similarity. Source: BHF-UCL cuticular plate Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome nucleolus Inferred from direct assay PubMed 9537418. Source: HGNC spectrin Traceable author statement Ref.1. Source: ProtInc spectrin-associated cytoskeleton Non-traceable author statement PubMed 17620337. Source: BHF-UCL
Molecular_function	actin binding Traceable author statement Ref.1. Source: ProtInc ankyrin binding Non-traceable author statement PubMed 17620337. Source: BHF-UCL phospholipid binding Inferred from electronic annotation. Source: InterPro structural constituent of cytoskeleton Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DISC1	Q9NRI5	3	EBI-351561,EBI-529989
SPTA1	P02549	3	EBI-351561,EBI-375617
SPTAN1	Q13813	7	EBI-351561,EBI-351450

Alternative products

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

Isoform Long (identifier: Q01082-1)

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 Short (identifier: Q01082-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2141-2168: MAETVDTSEMVNGATEQRTSSKESSPIP → VSYRSQTYQNYKNFNSRRTASDQPWSGL
     2169-2364: Missing.

Isoform 2 (identifier: Q01082-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MTTTVATDYD...FERSRIKALA → MELQRTSSIS...QLEGRFKQLQ
     2141-2225: MAETVDTSEM...KASSRSWHNV → VSYRSQTYQNYKNFNSRRTASDQPWSGL
     2226-2364: Missing.

Note: Contains a phosphoserine at position 8 (By similarity). Contains a phosphoserine at position 10. Contains a phosphoserine at position 14.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2364

2364

Spectrin beta chain, non-erythrocytic 1

PRO_0000073461

Regions

Domain

1 – 275

275

Actin-binding

Domain

54 – 158

105

CH 1

Domain

173 – 275

103

CH 2

Repeat

276 – 384

109

Spectrin 1

Repeat

385 – 498

114

Spectrin 2

Repeat

499 – 608

110

Spectrin 3

Repeat

609 – 714

106

Spectrin 4

Repeat

715 – 819

105

Spectrin 5

Repeat

820 – 925

106

Spectrin 6

Repeat

926 – 1032

107

Spectrin 7

Repeat

1033 – 1139

107

Spectrin 8

Repeat

1140 – 1245

106

Spectrin 9

Repeat

1246 – 1350

105

Spectrin 10

Repeat

1351 – 1462

112

Spectrin 11

Repeat

1463 – 1562

100

Spectrin 12

Repeat

1563 – 1668

106

Spectrin 13

Repeat

1669 – 1775

107

Spectrin 14

Repeat

1776 – 1881

106

Spectrin 15

Repeat

1882 – 1987

106

Spectrin 16

Repeat

1988 – 2133

146

Spectrin 17

Domain

2197 – 2307

111

PH

Region

1563 – 2093

531

Interaction with ANK2

Amino acid modifications

Modified residue

90

1

N6-acetyllysine Ref.17

Modified residue

257

1

Phosphoserine By similarity

Modified residue

817

1

Phosphoserine Ref.18

Modified residue

825

1

Phosphoserine Ref.18

Modified residue

999

1

Phosphothreonine By similarity

Modified residue

1057

1

Phosphoserine Ref.18

Modified residue

1447

1

Phosphoserine Ref.16

Modified residue

1805

1

Phosphotyrosine By similarity

Modified residue

1815

1

N6-acetyllysine Ref.17

Modified residue

1913

1

N6-acetyllysine Ref.17

Modified residue

1918

1

Phosphoserine By similarity

Modified residue

1989

1

N6-acetyllysine Ref.17

Modified residue

2102

1

Phosphoserine Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.18 Ref.20

Modified residue

2128

1

Phosphoserine Ref.20

Modified residue

2138

1

Phosphoserine Ref.10 Ref.13 Ref.14 Ref.16 Ref.18 Ref.20

Modified residue

2160

1

Phosphoserine Ref.20

Modified residue

2161

1

Phosphoserine Ref.20

Modified residue

2164

1

Phosphoserine Ref.20

Modified residue

2165

1

Phosphoserine Ref.14

Modified residue

2169

1

Phosphoserine Ref.14 Ref.16 Ref.18 Ref.20

Modified residue

2187

1

Phosphothreonine Ref.14

Modified residue

2195

1

Phosphothreonine By similarity

Modified residue

2319

1

Phosphoserine Ref.20

Modified residue

2320

1

Phosphothreonine Ref.14 Ref.18 Ref.20

Modified residue

2328

1

Phosphothreonine Ref.14

Modified residue

2340

1

Phosphoserine Ref.20

Modified residue

2341

1

Phosphoserine Ref.14 Ref.16 Ref.18

Modified residue

2358

1

Phosphoserine By similarity

Glycosylation

2324

1

O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence

1 – 49

49

MTTTV…IKALA → MELQRTSSISGPLSPAYTGQ VPYNYNQLEGRFKQLQ in isoform 2.

VSP_026054

Alternative sequence

2141 – 2225

85

MAETV…SWHNV → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform 2.

VSP_026055

Alternative sequence

2141 – 2168

28

MAETV…SSPIP → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform Short.

VSP_000720

Alternative sequence

2169 – 2364

196

Missing in isoform Short.

VSP_000721

Alternative sequence

2226 – 2364

139

Missing in isoform 2.

VSP_026056

Natural variant

1411

1

D → H. Ref.1 Ref.2
Corresponds to variant rs1052790 [ dbSNP | Ensembl ].

VAR_032641

Experimental info

Sequence conflict

583

1

R → W in BAD92985. Ref.3

Secondary structure

1

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2364

Helix Strand Turn

Details...

Helix

174 – 186

13

Turn

187 – 189

3

Beta strand

196 – 199

4

Helix

200 – 202

3

Helix

206 – 215

10

Helix

217 – 219

3

Helix

222 – 224

3

Helix

230 – 245

16

Helix

253 – 256

4

Beta strand

257 – 260

4

Helix

263 – 277

15

Helix

1697 – 1721

25

Helix

1730 – 1767

38

Helix

1773 – 1826

54

Helix

1836 – 1852

17

Helix

1854 – 1873

20

Helix

1877 – 1935

59

Helix

1943 – 1962

20

Helix

1964 – 1979

16

Helix

1985 – 2014

30

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 1770C3B0EB07B892	FASTA	2,364	274,609
	10 20 30 40 50 60 MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF 70 80 90 100 110 120 TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL 130 140 150 160 170 180 QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL 190 200 210 220 230 240 LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL 250 260 270 280 290 300 AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET 310 320 330 340 350 360 EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG 370 380 390 400 410 420 NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL 430 440 450 460 470 480 EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA 490 500 510 520 530 540 VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI 550 560 570 580 590 600 MDWMDEMKVL VLSQDYGKHL LGVEDLLQKH TLVEADIGIQ AERVRGVNAS AQKFATDGEG 610 620 630 640 650 660 YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI 670 680 690 700 710 720 LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII 730 740 750 760 770 780 YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSS DVGHDEYSTQ 790 800 810 820 830 840 SLVKKHKDVA EEIANYRPTL DTLHEQASAL PQEHAESPDV RGRLSGIEER YKEVAELTRL 850 860 870 880 890 900 RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN 910 920 930 940 950 960 QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY 970 980 990 1000 1010 1020 HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE 1030 1040 1050 1060 1070 1080 KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR 1090 1100 1110 1120 1130 1140 TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL 1150 1160 1170 1180 1190 1200 RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT 1210 1220 1230 1240 1250 1260 LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN 1270 1280 1290 1300 1310 1320 RETASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM 1330 1340 1350 1360 1370 1380 AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN 1390 1400 1410 1420 1430 1440 KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ 1450 1460 1470 1480 1490 1500 SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLNERKHN LLASKEIHQF NRDVEDEILW 1510 1520 1530 1540 1550 1560 VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IVTDSSSLSA 1570 1580 1590 1600 1610 1620 EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHRAQQYYFD AAEAEAWMSE QELYMMSEEK 1630 1640 1650 1660 1670 1680 AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY 1690 1700 1710 1720 1730 1740 AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF 1750 1760 1770 1780 1790 1800 REFARDTGNI GQERVDTVNH LADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI 1810 1820 1830 1840 1850 1860 LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV 1870 1880 1890 1900 1910 1920 RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC ESRRVRLVDT GDKFRFFSMV 1930 1940 1950 1960 1970 1980 RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTTC IELGKSLLAR 1990 2000 2010 2020 2030 2040 KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL 2050 2060 2070 2080 2090 2100 SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP 2110 2120 2130 2140 2150 2160 PSPEPSTKVS EEAESQQQWD TSKGEQVSQN GLPAEQGSPR MAETVDTSEM VNGATEQRTS 2170 2180 2190 2200 2210 2220 SKESSPIPSP TSDRKAKTAL PAQSAATLPA RTQETPSAQM EGFLNRKHEW EAHNKKASSR 2230 2240 2250 2260 2270 2280 SWHNVYCVIN NQEMGFYKDA KTAASGIPYH SEVPVSLKEA VCEVALDYKK KKHVFKLRLN 2290 2300 2310 2320 2330 2340 DGNEYLFQAK DDEEMNTWIQ AISSAISSDK HEVSASTQST PASSRAQTLP TSVVTITSES 2350 2360 SPGKREKDKE KDKEKRFSLF GKKK
	Isoform Short [UniParc]. Checksum: 34F9C77E47199043	FASTA	2,168	253,091
	10 20 30 40 50 60 MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF 70 80 90 100 110 120 TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL 130 140 150 160 170 180 QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL 190 200 210 220 230 240 LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL 250 260 270 280 290 300 AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET 310 320 330 340 350 360 EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG 370 380 390 400 410 420 NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL 430 440 450 460 470 480 EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA 490 500 510 520 530 540 VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI 550 560 570 580 590 600 MDWMDEMKVL VLSQDYGKHL LGVEDLLQKH TLVEADIGIQ AERVRGVNAS AQKFATDGEG 610 620 630 640 650 660 YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI 670 680 690 700 710 720 LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII 730 740 750 760 770 780 YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSS DVGHDEYSTQ 790 800 810 820 830 840 SLVKKHKDVA EEIANYRPTL DTLHEQASAL PQEHAESPDV RGRLSGIEER YKEVAELTRL 850 860 870 880 890 900 RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN 910 920 930 940 950 960 QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY 970 980 990 1000 1010 1020 HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE 1030 1040 1050 1060 1070 1080 KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR 1090 1100 1110 1120 1130 1140 TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL 1150 1160 1170 1180 1190 1200 RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT 1210 1220 1230 1240 1250 1260 LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN 1270 1280 1290 1300 1310 1320 RETASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM 1330 1340 1350 1360 1370 1380 AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN 1390 1400 1410 1420 1430 1440 KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ 1450 1460 1470 1480 1490 1500 SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLNERKHN LLASKEIHQF NRDVEDEILW 1510 1520 1530 1540 1550 1560 VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IVTDSSSLSA 1570 1580 1590 1600 1610 1620 EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHRAQQYYFD AAEAEAWMSE QELYMMSEEK 1630 1640 1650 1660 1670 1680 AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY 1690 1700 1710 1720 1730 1740 AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF 1750 1760 1770 1780 1790 1800 REFARDTGNI GQERVDTVNH LADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI 1810 1820 1830 1840 1850 1860 LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV 1870 1880 1890 1900 1910 1920 RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC ESRRVRLVDT GDKFRFFSMV 1930 1940 1950 1960 1970 1980 RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTTC IELGKSLLAR 1990 2000 2010 2020 2030 2040 KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL 2050 2060 2070 2080 2090 2100 SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP 2110 2120 2130 2140 2150 2160 PSPEPSTKVS EEAESQQQWD TSKGEQVSQN GLPAEQGSPR VSYRSQTYQN YKNFNSRRTA SDQPWSGL
	Isoform 2 [UniParc]. Checksum: 2CA864D7AAC0182C	FASTA	2,155	251,397
	10 20 30 40 50 60 MELQRTSSIS GPLSPAYTGQ VPYNYNQLEG RFKQLQDERE AVQKKTFTKW VNSHLARVSC 70 80 90 100 110 120 RITDLYTDLR DGRMLIKLLE VLSGERLPKP TKGRMRIHCL ENVDKALQFL KEQRVHLENM 130 140 150 160 170 180 GSHDIVDGNH RLTLGLIWTI ILRFQIQDIS VETEDNKEKK SAKDALLLWC QMKTAGYPNV 190 200 210 220 230 240 NIHNFTTSWR DGMAFNALIH KHRPDLIDFD KLKKSNAHYN LQNAFNLAEQ HLGLTKLLDP 250 260 270 280 290 300 EDISVDHPDE KSIITYVVTY YHYFSKMKAL AVEGKRIGKV LDNAIETEKM IEKYESLASD 310 320 330 340 350 360 LLEWIEQTII ILNNRKFANS LVGVQQQLQA FNTYRTVEKP PKFTEKGNLE VLLFTIQSKM 370 380 390 400 410 420 RANNQKVYMP REGKLISDIN KAWERLEKAE HERELALRNE LIRQEKLEQL ARRFDRKAAM 430 440 450 460 470 480 RETWLSENQR LVSQDNFGFD LPAVEAATKK HEAIETDIAA YEERVQAVVA VARELEAENY 490 500 510 520 530 540 HDIKRITARK DNVIRLWEYL LELLRARRQR LEMNLGLQKI FQEMLYIMDW MDEMKVLVLS 550 560 570 580 590 600 QDYGKHLLGV EDLLQKHTLV EADIGIQAER VRGVNASAQK FATDGEGYKP CDPQVIRDRV 610 620 630 640 650 660 AHMEFCYQEL CQLAAERRAR LEESRRLWKF FWEMAEEEGW IREKEKILSS DDYGKDLTSV 670 680 690 700 710 720 MRLLSKHRAF EDEMSGRSGH FEQAIKEGED MIAEEHFGSE KIRERIIYIR EQWANLEQLS 730 740 750 760 770 780 AIRKKRLEEA SLLHQFQADA DDIDAWMLDI LKIVSSSDVG HDEYSTQSLV KKHKDVAEEI 790 800 810 820 830 840 ANYRPTLDTL HEQASALPQE HAESPDVRGR LSGIEERYKE VAELTRLRKQ ALQDTLALYK 850 860 870 880 890 900 MFSEADACEL WIDEKEQWLN NMQIPEKLED LEVIQHRFES LEPEMNNQAS RVAVVNQIAR 910 920 930 940 950 960 QLMHSGHPSE KEIKAQQDKL NTRWSQFREL VDRKKDALLS ALSIQNYHLE CNETKSWIRE 970 980 990 1000 1010 1020 KTKVIESTQD LGNDLAGVMA LQRKLTGMER DLVAIEAKLS DLQKEAEKLE SEHPDQAQAI 1030 1040 1050 1060 1070 1080 LSRLAEISDV WEEMKTTLKN REASLGEASK LQQFLRDLDD FQSWLSRTQT AIASEDMPNT 1090 1100 1110 1120 1130 1140 LTEAEKLLTQ HENIKNEIDN YEEDYQKMRD MGEMVTQGQT DAQYMFLRQR LQALDTGWNE 1150 1160 1170 1180 1190 1200 LHKMWENRQN LLSQSHAYQQ FLRDTKQAEA FLNNQEYVLA HTEMPTTLEG AEAAIKKQED 1210 1220 1230 1240 1250 1260 FMTTMDANEE KINAVVETGR RLVSDGNINS DRIQEKVDSI DDRHRKNRET ASELLMRLKD 1270 1280 1290 1300 1310 1320 NRDLQKFLQD CQELSLWINE KMLTAQDMSY DEARNLHSKW LKHQAFMAEL ASNKEWLDKI 1330 1340 1350 1360 1370 1380 EKEGMQLISE KPETEAVVKE KLTGLHKMWE VLESTTQTKA QRLFDANKAE LFTQSCADLD 1390 1400 1410 1420 1430 1440 KWLHGLESQI QSDDYGKDLT SVNILLKKQQ MLENQMEVRK KEIEELQSQA QALSQEGKST 1450 1460 1470 1480 1490 1500 DEVDSKRLTV QTKFMELLEP LNERKHNLLA SKEIHQFNRD VEDEILWVGE RMPLATSTDH 1510 1520 1530 1540 1550 1560 GHNLQTVQLL IKKNQTLQKE IQGHQPRIDD IFERSQNIVT DSSSLSAEAI RQRLADLKQL 1570 1580 1590 1600 1610 1620 WGLLIEETEK RHRRLEEAHR AQQYYFDAAE AEAWMSEQEL YMMSEEKAKD EQSAVSMLKK 1630 1640 1650 1660 1670 1680 HQILEQAVED YAETVHQLSK TSRALVADSH PESERISMRQ SKVDKLYAGL KDLAEERRGK 1690 1700 1710 1720 1730 1740 LDERHRLFQL NREVDDLEQW IAEREVVAGS HELGQDYEHV TMLQERFREF ARDTGNIGQE 1750 1760 1770 1780 1790 1800 RVDTVNHLAD ELINSGHSDA ATIAEWKDGL NEAWADLLEL IDTRTQILAA SYELHKFYHD 1810 1820 1830 1840 1850 1860 AKEIFGRIQD KHKKLPEELG RDQNTVETLQ RMHTTFEHDI QALGTQVRQL QEDAARLQAA 1870 1880 1890 1900 1910 1920 YAGDKADDIQ KRENEVLEAW KSLLDACESR RVRLVDTGDK FRFFSMVRDL MLWMEDVIRQ 1930 1940 1950 1960 1970 1980 IEAQEKPRDV SSVELLMNNH QGIKAEIDAR NDSFTTCIEL GKSLLARKHY ASEEIKEKLL 1990 2000 2010 2020 2030 2040 QLTEKRKEMI DKWEDRWEWL RLILEVHQFS RDASVAEAWL LGQEPYLSSR EIGQSVDEVE 2050 2060 2070 2080 2090 2100 KLIKRHEAFE KSAATWDERF SALERLTTLE LLEVRRQQEE EERKRRPPSP EPSTKVSEEA 2110 2120 2130 2140 2150 ESQQQWDTSK GEQVSQNGLP AEQGSPRVSY RSQTYQNYKN FNSRRTASDQ PWSGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of human brain cDNA encoding the general isoform of beta-spectrin." Hu R.J., Watanabe M., Bennett V. J. Biol. Chem. 267:18715-18722(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT HIS-1411. Tissue: Brain.
[2]	"A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell bodies and interacts with neurofibromatosis type 2 gene product schwannomin." Chen Y., Yu P., Lu D., Tagle D.A., Cai T. J. Mol. Neurosci. 17:59-70(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, VARIANT HIS-1411.
[3]	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 LONG). Tissue: Brain.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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 2).
[7]	"Cloning of a portion of the chromosomal gene and cDNA for human beta-fodrin, the nonerythroid form of beta-spectrin." Chang J.G., Scarpa A., Eddy R.L., Byers M.G., Harris A.S., Morrow J.S., Watkins P., Shows T.B., Forget B.G. Genomics 17:287-293(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 293-1544.
[8]	"Identification of a novel C-terminal variant of betaII spectrin: two isoforms of betaII spectrin have distinct intracellular locations and activities." Hayes N.V.L., Scott C., Heerkens E., Ohanian V., Maggs A.M., Pinder J.C., Kordeli E., Baines A.J. J. Cell Sci. 113:2023-2034(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2087-2168 (ISOFORM SHORT). Tissue: Skeletal muscle.
[9]	"Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes." Mohler P.J., Yoon W., Bennett V. J. Biol. Chem. 279:40185-40193(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ANK2.
[10]	"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-2102 AND SER-2138, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2138, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2138; SER-2165; SER-2169; THR-2187; THR-2320; THR-2328 AND SER-2341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, MASS SPECTROMETRY.
[16]	"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-1447; SER-2138; SER-2169 AND SER-2341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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-90; LYS-1815; LYS-1913 AND LYS-1989, MASS SPECTROMETRY.
[18]	"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-817; SER-825; SER-1057; SER-2102; SER-2138; SER-2169; THR-2320 AND SER-2341, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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].
[20]	"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-2102; SER-2128; SER-2138; SER-2160; SER-2161; SER-2164; SER-2169; SER-2319; THR-2320 AND SER-2340, MASS SPECTROMETRY.
[21]	"Crystal structure of a calponin homology domain." Carugo K.D., Banuelos S., Saraste M. Nat. Struct. Biol. 4:175-179(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 173-280.
[22]	"Structural comparisons of calponin homology domains: implications for actin binding." Banuelos S., Saraste M., Carugo K.D. Structure 6:1419-1431(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 173-281.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M96803 mRNA. Translation: AAA60580.1.
AF327441 mRNA. Translation: AAO15362.1.
AB209748 mRNA. Translation: BAD92985.1. Different initiation.
AC093110 Genomic DNA. Translation: AAY24229.1.
AC092839 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00147.1.
BC137282 mRNA. Translation: AAI37283.1.
BC137283 mRNA. Translation: AAI37284.1.
S65762 mRNA. Translation: AAB28324.1.
AJ005694 mRNA. Translation: CAA06678.1.
AJ238723 Genomic DNA. Translation: CAB91088.1.

IPI

IPI00005614.
IPI00328230.
IPI00333015.

PIR

A44159.
A47213.

RefSeq

NP_003119.2. NM_003128.2.
NP_842565.2. NM_178313.2.

UniGene

Hs.503178.
Hs.705692.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AA2	X-ray	2.00	A	173-280	[»]
1BKR	X-ray	1.10	A	172-280	[»]
3EDV	X-ray	1.95	A/B	1697-2015	[»]

ProteinModelPortal

Q01082.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33182N.

IntAct

Q01082. 35 interactions.

MINT

MINT-1136298.

STRING

9606.ENSP00000349259.

PTM databases

PhosphoSite

Q01082.

Polymorphism databases

DMDM

116242799.

Proteomic databases

PaxDb

Q01082.

PRIDE

Q01082.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000333896; ENSP00000334156; ENSG00000115306.
ENST00000356805; ENSP00000349259; ENSG00000115306.

GeneID

6711.

KEGG

hsa:6711.

UCSC

uc002rxu.3. human.
uc002rxx.3. human.

Organism-specific databases

CTD

6711.

GeneCards

GC02P054665.

H-InvDB

HIX0002055.

HGNC

HGNC:11275. SPTBN1.

HPA

HPA012685.
HPA013149.

MIM

182790. gene.

neXtProt

NX_Q01082.

PharmGKB

PA36104.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5069.

HOVERGEN

HBG057912.

InParanoid

Q01082.

KO

K06115.

OMA

LWQFYWD.

OrthoDB

EOG4WWRHM.

Enzyme and pathway databases

Pathway_Interaction_DB

tgfbrpathway. TGF-beta receptor signaling.

Reactome

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

Gene expression databases

ArrayExpress

Q01082.

Bgee

Q01082.

CleanEx

HS_SPTBN1.

Genevestigator

Q01082.

GermOnline

ENSG00000115306. Homo sapiens.

Family and domain databases

Gene3D

1.10.418.10. 2 hits.
2.30.29.30. 1 hit.

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001605. PH_dom-spectrin-type.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]

Pfam

PF00307. CH. 2 hits.
PF00169. PH. 1 hit.
PF00435. Spectrin. 17 hits.
[Graphical view]

PIRSF

PIRSF002297. Spectrin_beta_subunit. 1 hit.

PRINTS

PR00683. SPECTRINPH.

SMART

SM00033. CH. 2 hits.
SM00233. PH. 1 hit.
SM00150. SPEC. 17 hits.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.

PROSITE

PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

SPTBN1. human.

EvolutionaryTrace

Q01082.

GenomeRNAi

6711.

NextBio

26172.

SOURCE

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Entry information

Entry name

SPTB2_HUMAN

Accession

Primary (citable) accession number: Q01082
Secondary accession number(s): B2RP63 , O60837, Q16057, Q53R99, Q59ER3, Q8IX99

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 141 of the entry and version 2 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.