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Q8NF91 (SYNE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nesprin-1
Alternative name(s):
Enaptin
Myocyte nuclear envelope protein 1
Short name=Myne-1
Nuclear envelope spectrin repeat protein 1
Synaptic nuclear envelope protein 1
Short name=Syne-1
Gene names
Name:SYNE1
Synonyms:C6orf98, KIAA0796, KIAA1262, KIAA1756, MYNE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length8797 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. May be involved in the maintenance of nuclear organization and structural integrity. Connects nuclei to the cytoskeleton by interacting with the nuclear envelope and with F-actin in the cytoplasm. May be required for centrosome migration to the apical cell surface during early ciliogenesis. Ref.1 Ref.18

Subunit structure

Dimer. Core component of the LINC complex which is composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN domain-containing proteins interact with A-type lamins of the nuclear lamina, while at the other end of the complex, nesprins interact with unique cytoskeletal components. Interacts with SYNE3. May interact with MUSK By similarity. Interacts with F-actin via its N-terminal domain By similarity. Interacts with EMD and LMNA in vitro. Ref.15 Ref.18 Ref.21

Subcellular location

Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side Potential. Nucleus. Nucleus envelope. Cytoplasmcytoskeleton. Cytoplasmmyofibrilsarcomere. Note: The largest part of the protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. In skeletal and smooth muscles, a significant amount is found in the sarcomeres. In myoblasts, relocalized from the nuclear envelope to the nucleus and cytoplasm during cell differentiation. Ref.1 Ref.2 Ref.13

Tissue specificity

Expressed in HeLa, A431, A172 and HaCaT cells (at protein level). Widely expressed. Highly expressed in skeletal and smooth muscles, heart, spleen, peripheral blood leukocytes, pancreas, cerebellum, stomach, kidney and placenta. Ref.1 Ref.3 Ref.13 Ref.21

Domain

The KASH domain, which contains a transmembrane domain, mediates the nuclear envelope targeting and is involved in the binding to SUN1 and SUN2 through recognition of their SUN domains. Ref.18

Involvement in disease

Spinocerebellar ataxia, autosomal recessive, 8 (SCAR8) [MIM:610743]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR8 is an autosomal recessive form.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17

Emery-Dreifuss muscular dystrophy 4, autosomal dominant (EDMD4) [MIM:612998]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Sequence similarities

Belongs to the nesprin family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 12 HAT repeats.

Contains 1 KASH domain.

Contains 31 spectrin repeats.

Sequence caution

The sequence AAC02992.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAL38031.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAM95335.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin.

The sequence BAB71097.1 differs from that shown. Reason: Chimeric cDNA.

The sequence BAC04284.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAD28486.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Emery-Dreifuss muscular dystrophy
Neurodegeneration
   DomainCoiled coil
Repeat
Transmembrane
Transmembrane helix
   LigandActin-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi organization

Inferred from direct assay Ref.6. Source: UniProtKB

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeletal anchoring at nuclear membrane

Inferred from direct assay Ref.18. Source: UniProtKB

muscle cell differentiation

Inferred from direct assay Ref.1. Source: UniProtKB

nuclear matrix anchoring at nuclear membrane

Inferred from direct assay Ref.13. Source: UniProtKB

nucleus organization

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.6. Source: UniProtKB

SUN-KASH complex

Inferred from direct assay Ref.18. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from direct assay Ref.1. Source: UniProtKB

nuclear envelope

Inferred from direct assay Ref.1. Source: UniProtKB

nuclear membrane

Inferred from direct assay. Source: HPA

nuclear outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

postsynaptic membrane

Inferred from direct assay PubMed 10878022. Source: UniProtKB

sarcomere

Inferred from direct assay Ref.2. Source: MGI

   Molecular_functionactin binding

Inferred from direct assay Ref.2. Source: UniProtKB

actin filament binding

Inferred from sequence or structural similarity. Source: UniProtKB

lamin binding

Inferred from physical interaction Ref.13. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 22632968. Source: IntAct

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NF91-1)

Also known as: Nesprin-1 Giant; Enaptin;

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: Q8NF91-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-5476: Missing.
Isoform 3 (identifier: Q8NF91-3)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1-7838: Missing.
     8325-8325: S → SDVMIPESPEAYVKLTENAIKNTS
Isoform 4 (identifier: Q8NF91-4)

The sequence of this isoform differs from the canonical sequence as follows:
     103-103: K → KSMHRGSP
     3620-3641: Missing.
     3912-3967: Missing.
     8325-8325: S → SDVMIPESPEAYVKLTENAIKNTS
Isoform 5 (identifier: Q8NF91-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1437-1443: DIKTMEM → EYVIDKS
     1444-8797: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q8NF91-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1702-1725: LQNEVVSQASFYSKLLQLKESLFS → SSRKCEEGKNKMLFVTVTLFKIIK
     1726-8797: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q8NF91-7)

The sequence of this isoform differs from the canonical sequence as follows:
     5571-5580: TLLEESKEID → VTLGKIIFKK
     5581-8797: Missing.
Note: No experimental confirmation available.
Isoform 8 (identifier: Q8NF91-8)

Also known as: Beta 2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-5585: Missing.
Isoform 9 (identifier: Q8NF91-9)

Also known as: Alpha 2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-7843: Missing.
     7844-7874: AKASHESKASEIEYKLGKVNDRWQHLLDLIA → MVVAEDLSALRMAEDGCVDADLPDCNCDVTR
     8325-8325: S → SDVMIPESPEAYVKLTENAIKNTS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 87978797Nesprin-1
PRO_0000163591

Regions

Topological domain1 – 87468746Cytoplasmic Potential
Transmembrane8747 – 876721Helical; Anchor for type IV membrane protein; Potential
Topological domain8768 – 879730Perinuclear space Potential
Domain1 – 289289Actin-binding
Domain27 – 134108CH 1
Domain178 – 283106CH 2
Repeat592 – 62433HAT 1
Repeat1103 – 113533HAT 2
Repeat1425 – 145733HAT 3
Repeat1630 – 165223Spectrin 1
Repeat1655 – 1762108Spectrin 2
Repeat2176 – 220833HAT 4
Repeat2339 – 240567Spectrin 3
Repeat2406 – 2512107Spectrin 4
Repeat2515 – 2615101Spectrin 5
Repeat2705 – 274440HAT 5
Repeat3173 – 3277105Spectrin 6
Repeat3348 – 338639Spectrin 7
Repeat3361 – 340040HAT 6
Repeat3492 – 351019Spectrin 8
Repeat3555 – 358834HAT 7
Repeat3816 – 390792Spectrin 9
Repeat3967 – 403367Spectrin 10
Repeat4146 – 423893Spectrin 11
Repeat4261 – 433777Spectrin 12
Repeat4486 – 455974Spectrin 13
Repeat4750 – 477526Spectrin 14
Repeat4993 – 503543Spectrin 15
Repeat5101 – 5208108Spectrin 16
Repeat5569 – 562961Spectrin 17
Repeat5632 – 569059Spectrin 18
Repeat5738 – 579962Spectrin 19
Repeat5963 – 6070108Spectrin 20
Repeat6774 – 680633HAT 8
Repeat6795 – 6904110Spectrin 21
Repeat7001 – 703333HAT 9
Repeat7022 – 7127106Spectrin 22
Repeat7162 – 723069Spectrin 23
Repeat7211 – 725040HAT 10
Repeat7352 – 7453102Spectrin 24
Repeat7456 – 7560105Spectrin 25
Repeat7542 – 757433HAT 11
Repeat7697 – 777781Spectrin 26
Repeat7780 – 7882103Spectrin 27
Repeat7885 – 7996112Spectrin 28
Repeat7975 – 800733HAT 12
Repeat7999 – 8105107Spectrin 29
Repeat8108 – 8212105Spectrin 30
Repeat8440 – 8547108Spectrin 31
Domain8738 – 879760KASH
Coiled coil327 – 34721 Potential
Coiled coil433 – 46331 Potential
Coiled coil625 – 65026 Potential
Coiled coil817 – 84428 Potential
Coiled coil925 – 95531 Potential
Coiled coil991 – 101121 Potential
Coiled coil1197 – 121721 Potential
Coiled coil1270 – 1447178 Potential
Coiled coil1549 – 157729 Potential
Coiled coil1810 – 183021 Potential
Coiled coil1899 – 193436 Potential
Coiled coil1969 – 203567 Potential
Coiled coil2086 – 210621 Potential
Coiled coil2166 – 2270105 Potential
Coiled coil2606 – 263631 Potential
Coiled coil2780 – 280728 Potential
Coiled coil2944 – 299249 Potential
Coiled coil3773 – 381341 Potential
Coiled coil4101 – 413030 Potential
Coiled coil4590 – 461122 Potential
Coiled coil4852 – 487221 Potential
Coiled coil4913 – 494533 Potential
Coiled coil5293 – 531321 Potential
Coiled coil5350 – 5459110 Potential
Coiled coil6420 – 643819 Potential
Coiled coil6524 – 661087 Potential
Coiled coil6693 – 671220 Potential
Coiled coil8327 – 840175 Potential
Coiled coil8630 – 866233 Potential
Compositional bias8663 – 872967Ser-rich

Amino acid modifications

Modified residue82231Phosphoserine Ref.16
Modified residue82741Phosphothreonine Ref.16
Modified residue82771Phosphoserine Ref.16
Modified residue82801Phosphoserine Ref.16
Modified residue83051Phosphoserine By similarity

Natural variations

Alternative sequence1 – 78437843Missing in isoform 9.
VSP_007133
Alternative sequence1 – 78387838Missing in isoform 3.
VSP_007132
Alternative sequence1 – 55855585Missing in isoform 8.
VSP_007131
Alternative sequence1 – 54765476Missing in isoform 2.
VSP_007130
Alternative sequence1031K → KSMHRGSP in isoform 4.
VSP_007134
Alternative sequence1437 – 14437DIKTMEM → EYVIDKS in isoform 5.
VSP_007135
Alternative sequence1444 – 87977354Missing in isoform 5.
VSP_007136
Alternative sequence1702 – 172524LQNEV…ESLFS → SSRKCEEGKNKMLFVTVTLF KIIK in isoform 6.
VSP_007137
Alternative sequence1726 – 87977072Missing in isoform 6.
VSP_007138
Alternative sequence3620 – 364122Missing in isoform 4.
VSP_007139
Alternative sequence3912 – 396756Missing in isoform 4.
VSP_007140
Alternative sequence5571 – 558010TLLEESKEID → VTLGKIIFKK in isoform 7.
VSP_007141
Alternative sequence5581 – 87973217Missing in isoform 7.
VSP_007142
Alternative sequence7844 – 787431AKASH…LDLIA → MVVAEDLSALRMAEDGCVDA DLPDCNCDVTR in isoform 9.
VSP_007143
Alternative sequence83251S → SDVMIPESPEAYVKLTENAI KNTS in isoform 3, isoform 4 and isoform 9.
VSP_007144
Natural variant6551Q → R Found in a patient with mild intellectual disability, spastic paraplegia, axon neuropathy and leukoencephalopathy; unknown pathological significance. Ref.24
Corresponds to variant rs9397509 [ dbSNP | Ensembl ].
VAR_056211
Natural variant8851L → V.
Corresponds to variant rs17082709 [ dbSNP | Ensembl ].
VAR_056212
Natural variant10351V → A.
Corresponds to variant rs214976 [ dbSNP | Ensembl ].
VAR_056213
Natural variant20301S → G.
Corresponds to variant rs35763277 [ dbSNP | Ensembl ].
VAR_056214
Natural variant27951A → V.
Corresponds to variant rs214950 [ dbSNP | Ensembl ].
VAR_056215
Natural variant30881A → T Found in a patient with mild intellectual disability, spastic paraplegia, axon neuropathy and leukoencephalopathy; unknown pathological significance. Ref.24
VAR_070561
Natural variant36711V → M in a colorectal cancer sample; somatic mutation. Ref.22
VAR_036250
Natural variant38741K → T.
Corresponds to variant rs13210127 [ dbSNP | Ensembl ].
VAR_056216
Natural variant38921L → S Found in a patient with mild intellectual disability, spastic paraplegia, axon neuropathy and leukoencephalopathy; unknown pathological significance. Ref.24
VAR_070562
Natural variant39541S → T.
Corresponds to variant rs7775119 [ dbSNP | Ensembl ].
VAR_056217
Natural variant40601E → D.
Corresponds to variant rs4645434 [ dbSNP | Ensembl ].
VAR_056218
Natural variant41211K → N.
Corresponds to variant rs28385621 [ dbSNP | Ensembl ].
VAR_056219
Natural variant41211K → R.
Corresponds to variant rs9479297 [ dbSNP | Ensembl ].
VAR_056220
Natural variant42031E → K.
Corresponds to variant rs2130262 [ dbSNP | Ensembl ].
VAR_056221
Natural variant42101E → D in a colorectal cancer sample; somatic mutation. Ref.22
VAR_036251
Natural variant42231R → H in a colorectal cancer sample; somatic mutation. Ref.22
VAR_036252
Natural variant45461V → I.
Corresponds to variant rs4870093 [ dbSNP | Ensembl ].
VAR_056222
Natural variant45961S → T. Ref.2 Ref.10
Corresponds to variant rs6911096 [ dbSNP | Ensembl ].
VAR_056223
Natural variant49441L → M.
Corresponds to variant rs2306916 [ dbSNP | Ensembl ].
VAR_056224
Natural variant50151L → M. Ref.2 Ref.10
Corresponds to variant rs2306916 [ dbSNP | Ensembl ].
VAR_056225
Natural variant53771M → L.
Corresponds to variant rs35987150 [ dbSNP | Ensembl ].
VAR_056226
Natural variant54261T → M.
Corresponds to variant rs2306914 [ dbSNP | Ensembl ].
VAR_056227
Natural variant55071L → R in a colorectal cancer sample; somatic mutation. Ref.22
VAR_036253
Natural variant65661M → I.
Corresponds to variant rs35654757 [ dbSNP | Ensembl ].
VAR_056228
Natural variant66641T → I.
Corresponds to variant rs35079654 [ dbSNP | Ensembl ].
VAR_056229
Natural variant69511Q → H.
Corresponds to variant rs3945783 [ dbSNP | Ensembl ].
VAR_056230
Natural variant73021F → V. Ref.1 Ref.2 Ref.4 Ref.11
Corresponds to variant rs2147377 [ dbSNP | Ensembl ].
VAR_056231
Natural variant75061S → G.
Corresponds to variant rs35763277 [ dbSNP | Ensembl ].
VAR_056232
Natural variant80951R → H in EDMD4. Ref.23
VAR_062974
Natural variant81611N → H.
Corresponds to variant rs36215251 [ dbSNP | Ensembl ].
VAR_056233
Natural variant81681A → S.
Corresponds to variant rs17082236 [ dbSNP | Ensembl ].
VAR_056234
Natural variant83231G → A. Ref.1 Ref.2 Ref.4 Ref.11 Ref.13
Corresponds to variant rs2252755 [ dbSNP | Ensembl ].
VAR_015548
Natural variant83871V → L in EDMD4. Ref.23
VAR_062975
Natural variant84611E → K in EDMD4. Ref.23
Corresponds to variant rs119103248 [ dbSNP | Ensembl ].
VAR_062976
Natural variant84681R → H in a colorectal cancer sample; somatic mutation. Ref.22
VAR_036254
Natural variant86871T → I.
Corresponds to variant rs35591210 [ dbSNP | Ensembl ].
VAR_056235
Natural variant87411L → M.
Corresponds to variant rs2295190 [ dbSNP | Ensembl ].
VAR_056236

Experimental info

Mutagenesis8758 – 87636Missing: Abolishes the nuclear envelope targeting, induces a cytoplasmic localization. Ref.1
Sequence conflict981F → L in AAN60442. Ref.2
Sequence conflict4941S → P in AAM95335. Ref.6
Sequence conflict14401T → P in CAD28486. Ref.9
Sequence conflict30961N → D in BAB71097. Ref.7
Sequence conflict55261A → T in AAL33798. Ref.1
Sequence conflict55641E → K in AAL33798. Ref.1
Sequence conflict57351E → A in AAN03486. Ref.3
Sequence conflict65491K → E in AAL33798. Ref.1
Sequence conflict65491K → E in AAN60442. Ref.2
Sequence conflict65491K → E in AAO27774. Ref.4
Sequence conflict66261L → P in AAL33798. Ref.1
Sequence conflict66261L → P in AAN60442. Ref.2
Sequence conflict66261L → P in AAO27774. Ref.4
Sequence conflict66451E → V in AAL33798. Ref.1
Sequence conflict66451E → V in AAN60442. Ref.2
Sequence conflict66451E → V in AAO27774. Ref.4
Sequence conflict69231I → T in AAL33798. Ref.1
Sequence conflict69231I → T in AAN60442. Ref.2
Sequence conflict69231I → T in AAO27774. Ref.4
Sequence conflict69291V → A in AAL33798. Ref.1
Sequence conflict69291V → A in AAN60442. Ref.2
Sequence conflict69291V → A in AAO27774. Ref.4
Sequence conflict70751E → D in AAL33798. Ref.1
Sequence conflict70751E → D in AAN60442. Ref.2
Sequence conflict70751E → D in AAO27774. Ref.4
Sequence conflict70911N → T in AAL33798. Ref.1
Sequence conflict70911N → T in AAN60442. Ref.2
Sequence conflict70911N → T in AAO27774. Ref.4

Secondary structure

...... 8797
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Nesprin-1 Giant) (Enaptin) [UniParc].

Last modified November 28, 2012. Version 4.
Checksum: 02A53B8AFBF34A17

FASTA8,7971,011,086
        10         20         30         40         50         60 
MATSRGASRC PRDIANVMQR LQDEQEIVQK RTFTKWINSH LAKRKPPMVV DDLFEDMKDG 

        70         80         90        100        110        120 
VKLLALLEVL SGQKLPCEQG RRMKRIHAVA NIGTALKFLE GRKIKLVNIN STDIADGRPS 

       130        140        150        160        170        180 
IVLGLMWTII LYFQIEELTS NLPQLQSLSS SASSVDSIVS SETPSPPSKR KVTTKIQGNA 

       190        200        210        220        230        240 
KKALLKWVQY TAGKQTGIEV KDFGKSWRSG VAFHSVIHAI RPELVDLETV KGRSNRENLE 

       250        260        270        280        290        300 
DAFTIAETEL GIPRLLDPED VDVDKPDEKS IMTYVAQFLK HYPDIHNAST DGQEDDEILP 

       310        320        330        340        350        360 
GFPSFANSVQ NFKREDRVIF KEMKVWIEQF ERDLTRAQMV ESNLQDKYQS FKHFRVQYEM 

       370        380        390        400        410        420 
KRKQIEHLIQ PLHRDGKLSL DQALVKQSWD RVTSRLFDWH IQLDKSLPAP LGTIGAWLYR 

       430        440        450        460        470        480 
AEVALREEIT VQQVHEETAN TIQRKLEQHK DLLQNTDAHK RAFHEIYRTR SVNGIPVPPD 

       490        500        510        520        530        540 
QLEDMAERFH FVSSTSELHL MKMEFLELKY RLLSLLVLAE SKLKSWIIKY GRRESVEQLL 

       550        560        570        580        590        600 
QNYVSFIENS KFFEQYEVTY QILKQTAEMY VKADGSVEEA ENVMKFMNET TAQWRNLSVE 

       610        620        630        640        650        660 
VRSVRSMLEE VISNWDRYGN TVASLQAWLE DAEKMLNQSE NAKKDFFRNL PHWIQQHTAM 

       670        680        690        700        710        720 
NDAGNFLIET CDEMVSRDLK QQLLLLNGRW RELFMEVKQY AQADEMDRMK KEYTDCVVTL 

       730        740        750        760        770        780 
SAFATEAHKK LSEPLEVSFM NVKLLIQDLE DIEQRVPVMD AQYKIITKTA HLITKESPQE 

       790        800        810        820        830        840 
EGKEMFATMS KLKEQLTKVK ECYSPLLYES QQLLIPLEEL EKQMTSFYDS LGKINEIITV 

       850        860        870        880        890        900 
LEREAQSSAL FKQKHQELLA CQENCKKTLT LIEKGSQSVQ KFVTLSNVLK HFDQTRLQRQ 

       910        920        930        940        950        960 
IADIHVAFQS MVKKTGDWKK HVETNSRLMK KFEESRAELE KVLRIAQEGL EEKGDPEELL 

       970        980        990       1000       1010       1020 
RRHTEFFSQL DQRVLNAFLK ACDELTDILP EQEQQGLQEA VRKLHKQWKD LQGEAPYHLL 

      1030       1040       1050       1060       1070       1080 
HLKIDVEKNR FLASVEECRT ELDRETKLMP QEGSEKIIKE HRVFFSDKGP HHLCEKRLQL 

      1090       1100       1110       1120       1130       1140 
IEELCVKLPV RDPVRDTPGT CHVTLKELRA AIDSTYRKLM EDPDKWKDYT SRFSEFSSWI 

      1150       1160       1170       1180       1190       1200 
STNETQLKGI KGEAIDTANH GEVKRAVEEI RNGVTKRGET LSWLKSRLKV LTEVSSENEA 

      1210       1220       1230       1240       1250       1260 
QKQGDELAKL SSSFKALVTL LSEVEKMLSN FGDCVQYKEI VKNSLEELIS GSKEVQEQAE 

      1270       1280       1290       1300       1310       1320 
KILDTENLFE AQQLLLHHQQ KTKRISAKKR DVQQQIAQAQ QGEGGLPDRG HEELRKLEST 

      1330       1340       1350       1360       1370       1380 
LDGLERSRER QERRIQVTLR KWERFETNKE TVVRYLFQTG SSHERFLSFS SLESLSSELE 

      1390       1400       1410       1420       1430       1440 
QTKEFSKRTE SIAVQAENLV KEASEIPLGP QNKQLLQQQA KSIKEQVKKL EDTLEEDIKT 

      1450       1460       1470       1480       1490       1500 
MEMVKTKWDH FGSNFETLSV WITEKEKELN ALETSSSAMD MQISQIKVTI QEIESKLSSI 

      1510       1520       1530       1540       1550       1560 
VGLEEEAQSF AQFVTTGESA RIKAKLTQIR RYGEELREHA QCLEGTILGH LSQQQKFEEN 

      1570       1580       1590       1600       1610       1620 
LRKIQQSVSE FEDKLAVPIK ICSSATETYK VLQEHMDLCQ ALESLSSAIT AFSASARKVV 

      1630       1640       1650       1660       1670       1680 
NRDSCVQEAA ALQQQYEDIL RRAKERQTAL ENLLAHWQRL EKELSSFLTW LERGEAKASS 

      1690       1700       1710       1720       1730       1740 
PEMDISADRV KVEGELQLIQ ALQNEVVSQA SFYSKLLQLK ESLFSVASKD DVKMMKLHLE 

      1750       1760       1770       1780       1790       1800 
QLDERWRDLP QIINKRINFL QSVVAEHQQF DELLLSFSVW IKLFLSELQT TSEISIMDHQ 

      1810       1820       1830       1840       1850       1860 
VALTRHKDHA AEVESKKGEL QSLQGHLAKL GSLGRAEDLH LLQGKAEDCF QLFEEASQVV 

      1870       1880       1890       1900       1910       1920 
ERRQLALSHL AEFLQSHASL SGILRQLRQT VEATNSMNKN ESDLIEKDLN DALQNAKALE 

      1930       1940       1950       1960       1970       1980 
SAAVSLDGIL SKAQYHLKIG SSEQRTSCRA TADQLCGEVE RIQNLLGTKQ SEADALAVLK 

      1990       2000       2010       2020       2030       2040 
KAFQDQKEEL LKSIEDIEER TDKERLKEPT RQALQQRLRV FNQLEDELNS HEHELCWLKD 

      2050       2060       2070       2080       2090       2100 
KAKQIAQKDV AFAPEVDREI NRLEVTWDDT KRLIHENQGQ CCGLIDLMRE YQNLKSAVSK 

      2110       2120       2130       2140       2150       2160 
VLENASSVIV TRTTIKDQED LKWAFSKHET AKNKMNYKQK DLDNFTSKGK HLLSELKKIH 

      2170       2180       2190       2200       2210       2220 
SSDFSLVKTD MESTVDKWLD VSEKLEENMD RLRVSLSIWD DVLSTRDEIE GWSNNCVPQM 

      2230       2240       2250       2260       2270       2280 
AENISNLDNH LRAEELLKEF ESEVKNKALR LEELHSKVND LKELTKNLET PPDLQFIEAD 

      2290       2300       2310       2320       2330       2340 
LMQKLEHAKE ITEVAKGTLK DFTAQSTQVE KFINDITTWF TKVEESLMNC AQNETCEALK 

      2350       2360       2370       2380       2390       2400 
KVKDIQKELQ SQQSNISSTQ ENLNSLCRKY HSAELESLGR AMTGLIKKHE AVSQLCSKTQ 

      2410       2420       2430       2440       2450       2460 
ASLQESLEKH FSESMQEFQE WFLGAKAAAK ESSDRTGDSK VLEAKLHDLQ NILDSVSDGQ 

      2470       2480       2490       2500       2510       2520 
SKLDAVTQEG QTLYAHLSKQ IVSSIQEQIT KANEEFQAFL KQCLKDKQAL QDCASELGSF 

      2530       2540       2550       2560       2570       2580 
EDQHRKLNLW IHEMEERFNT ENLGESKQHI PEKKNEVHKV EMFLGELLAA RESLDKLSQR 

      2590       2600       2610       2620       2630       2640 
GQLLSEEGHG AGQEGRLCSQ LLTSHQNLLR MTKEKLRSCQ VALQEHEALE EALQSMWFWV 

      2650       2660       2670       2680       2690       2700 
KAIQDRLACA ESTLGSKDTL EKRLSQIQDI LLMKGEGEVK LNMAIGKGEQ ALRSSNKEGQ 

      2710       2720       2730       2740       2750       2760 
RVIQTQLETL KEVWADIMSS SVHAQSTLES VISQWNDYVE RKNQLEQWME SVDQKIEHPL 

      2770       2780       2790       2800       2810       2820 
QPQPGLKEKF VLLDHLQSIL SEAEDHTRAL HRLIAKSREL YEKTEDESFK DTAQEELKTQ 

      2830       2840       2850       2860       2870       2880 
FNDIMTVAKE KMRKVEEIVK DHLMYLDAVH EFTDWLHSAK EELHRWSDMS GDSSATQKKL 

      2890       2900       2910       2920       2930       2940 
SKIKELIDSR EIGASRLSRV ESLAPEVKQN TTASGCELMH TEMQALRADW KQWEDSVFQT 

      2950       2960       2970       2980       2990       3000 
QSCLENLVSQ MALSEQEFSG QVAQLEQALE QFSALLKTWA QQLTLLEGKN TDEEIVECWH 

      3010       3020       3030       3040       3050       3060 
KGQEILDALQ KAEPRTEDLK SQLNELCRFS RDLSTYSGKV SGLIKEYNCL CLQASKGCQN 

      3070       3080       3090       3100       3110       3120 
KEQILQQRFR KAFRDFQQWL VNAKITTAKC FDIPQNISEV STSLQKIQEF LSESENGQHK 

      3130       3140       3150       3160       3170       3180 
LNMMLSKGEL LSTLLTKEKA KGIQAKVTAA KEDWKNFHSN LHQKESALEN LKIQMKDFEV 

      3190       3200       3210       3220       3230       3240 
SAEPIQDWLS KTEKMVHESS NRLYDLPAKR REQQKLQSVL EEIHCYEPQL NRLKEKAQQL 

      3250       3260       3270       3280       3290       3300 
WEGQAASKSF RHRVSQLSSQ YLALSNLTKE KVSRLDRIVA EHNQFSLGIK ELQDWMTDAI 

      3310       3320       3330       3340       3350       3360 
HMLDSYCHPT SDKSVLDSRT LKLEALLSVK QEKEIQMKMI VTRGESVLQN TSPEGIPTIQ 

      3370       3380       3390       3400       3410       3420 
QQLQSVKDMW ASLLSAGIRC KSQLEGALSK WTSYQDGVRQ FSGWMDSMEA NLNESERQHA 

      3430       3440       3450       3460       3470       3480 
ELRDKTTMLG KAKLLNEEVL SYSSLLETIE VKGAGMTEHY VTQLELQDLQ ERYRAIQERA 

      3490       3500       3510       3520       3530       3540 
KEAVTKSEKL VRLHQEYQRD LKAFEVWLGQ EQEKLDQYSV LEGDAHTHET TLRDLQELQV 

      3550       3560       3570       3580       3590       3600 
HCAEGQALLN SVLHTREDVI PSGIPQAEDR ALESLRQDWQ AYQHRLSETR TQFNNVVNKL 

      3610       3620       3630       3640       3650       3660 
RLMEQKFQQV DEWLKTAEEK VSPRTRRQSN RATKEIQLHQ MKKWHEEVTA YRDEVEEVGA 

      3670       3680       3690       3700       3710       3720 
RAQEILDESH VNSRMGCQAT QLTSRYQALL LQVLEQIKFL EEEIQSLEES ESSLSSYSDW 

      3730       3740       3750       3760       3770       3780 
YGSTHKNFKN VATKIDKVDT VMMGKKLKTL EVLLKDMEKG HSLLKSAREK GERAVKYLEE 

      3790       3800       3810       3820       3830       3840 
GEAERLRKEI HDHMEQLKEL TSTVRKEHMT LEKGLHLAKE FSDKCKALTQ WIAEYQEILH 

      3850       3860       3870       3880       3890       3900 
VPEEPKMELY EKKAQLSKYK SLQQTVLSHE PSVKSVREKG EALLELVQDV TLKDKIDQLQ 

      3910       3920       3930       3940       3950       3960 
SDYQDLCSIG KEHVFSLEAK VKDHEDYNSE LQEVEKWLLQ MSGRLVAPDL LETSSLETIT 

      3970       3980       3990       4000       4010       4020 
QQLAHHKAMM EEIAGFEDRL NNLQMKGDTL IGQCADHLQA KLKQNVHAHL QGTKDSYSAI 

      4030       4040       4050       4060       4070       4080 
CSTAQRMYQS LEHELQKHVS RQDTLQQCQA WLSAVQPDLE PSPQPPLSRA EAIKQVKHFR 

      4090       4100       4110       4120       4130       4140 
ALQEQARTYL DLLCSMCDLS NASVKTTAKD IQQTEQTIEQ KLVQAQNLTQ GWEEIKHLKS 

      4150       4160       4170       4180       4190       4200 
ELWIYLQDAD QQLQNMKRRH SELELNIAQN MVSQVKDFVK KLQSKQASVN TIIEKVNKLT 

      4210       4220       4230       4240       4250       4260 
KKEESPEHKE INHLNDQWLD LCRQSNNLCL QREEDLQRTR DYHDCMNVVE VFLEKFTTEW 

      4270       4280       4290       4300       4310       4320 
DNLARSDAES TAVHLEALKK LALALQERKY AIEDLKDQKQ KMIEHLNLDD KELVKEQTSH 

      4330       4340       4350       4360       4370       4380 
LEQRWFQLED LIKRKIQVSV TNLEELNVVQ SRFQELMEWA EEQQPNIAEA LKQSPPPDMA 

      4390       4400       4410       4420       4430       4440 
QNLLMDHLAI CSELEAKQML LKSLIKDADR VMADLGLNER QVIQKALSDA QSHVNCLSDL 

      4450       4460       4470       4480       4490       4500 
VGQRRKYLNK ALSEKTQFLM AVFQATSQIQ QHERKIMFRE HICLLPDDVS KQVKTCKSAQ 

      4510       4520       4530       4540       4550       4560 
ASLKTYQNEV TGLWAQGREL MKEVTEQEKS EVLGKLQELQ SVYDSVLQKC SHRLQELEKN 

      4570       4580       4590       4600       4610       4620 
LVSRKHFKED FDKACHWLKQ ADIVTFPEIN LMNESSELHT QLAKYQNILE QSPEYENLLL 

      4630       4640       4650       4660       4670       4680 
TLQRTGQTIL PSLNEVDHSY LSEKLNALPR QFNVIVALAK DKFYKVQEAI LARKEYASLI 

      4690       4700       4710       4720       4730       4740 
ELTTQSLSEL EAQFLRMSKV PTDLAVEEAL SLQDGCRAIL DEVAGLGEAV DELNQKKEGF 

      4750       4760       4770       4780       4790       4800 
RSTGQPWQPD KMLHLVTLYH RLKRQTEQRV SLLEDTTSAY QEHEKMCQQL ERQLKSVKEE 

      4810       4820       4830       4840       4850       4860 
QSKVNEETLP AEEKLKMYHS LAGSLQDSGI VLKRVTIHLE DLAPHLDPLA YEKARHQIQS 

      4870       4880       4890       4900       4910       4920 
WQGELKLLTS AIGETVTECE SRMVQSIDFQ TEMSRSLDWL RRVKAELSGP VYLDLNLQDI 

      4930       4940       4950       4960       4970       4980 
QEEIRKIQIH QEEVQSSLRI MNALSHKEKE KFTKAKELIS ADLEHSLAEL SELDGDIQEA 

      4990       5000       5010       5020       5030       5040 
LRTRQATLTE IYSQCQRYYQ VFQAANDWLE DAQELLQLAG NGLDVESAEE NLKSHMEFFS 

      5050       5060       5070       5080       5090       5100 
TEDQFHSNLE ELHSLVATLD PLIKPTGKED LEQKVASLEL RSQRMSRDSG AQVDLLQRCT 

      5110       5120       5130       5140       5150       5160 
AQWHDYQKAR EEVIELMNDT EKKLSEFSLL KTSSSHEAEE KLSEHKALVS VVNSFHEKIV 

      5170       5180       5190       5200       5210       5220 
ALEEKASQLE KTGNDASKAT LSRSMTTVWQ RWTRLRAVAQ DQEKILEDAV DEWTGFNNKV 

      5230       5240       5250       5260       5270       5280 
KKATEMIDQL QDKLPGSSAE KASKAELLTL LEYHDTFVLE LEQQQSALGM LRQQTLSMLQ 

      5290       5300       5310       5320       5330       5340 
DGAAPTPGEE PPLMQEITAM QDRCLNMQEK VKTNGKLVKQ ELKDREMVET QINSVKCWVQ 

      5350       5360       5370       5380       5390       5400 
ETKEYLGNPT IEIDAQLEEL QILLTEATNH RQNIEKMAEE QKEKYLGLYT ILPSELSLQL 

      5410       5420       5430       5440       5450       5460 
AEVALDLKIR DQIQDKIKEV EQSKATSQEL SRQIQKLAKD LTTILTKLKA KTDNVVQAKT 

      5470       5480       5490       5500       5510       5520 
DQKVLGEELD GCNSKLMELD AAVQKFLEQN GQLGKPLAKK IGKLTELHQQ TIRQAENRLS 

      5530       5540       5550       5560       5570       5580 
KLNQAASHLE EYNEMLELIL KWIEKAKVLA HGTIAWNSAS QLREQYILHQ TLLEESKEID 

      5590       5600       5610       5620       5630       5640 
SELEAMTEKL QYLTSVYCTE KMSQQVAELG RETEELRQMI KIRLQNLQDA AKDMKKFEAE 

      5650       5660       5670       5680       5690       5700 
LKKLQAALEQ AQATLTSPEV GRLSLKEQLS HRQHLLSEME SLKPKVQAVQ LCQSALRIPE 

      5710       5720       5730       5740       5750       5760 
DVVASLPLCH AALRLQEEAS RLQHTAIQQC NIMQEAVVQY EQYEQEMKHL QQLIEGAHRE 

      5770       5780       5790       5800       5810       5820 
IEDKPVATSN IQELQAQISR HEELAQKIKG YQEQIASLNS KCKMLTMKAK HATMLLTVTE 

      5830       5840       5850       5860       5870       5880 
VEGLAEGTED LDGELLPTPS AHPSVVMMTA GRCHTLLSPV TEESGEEGTN SEISSPPACR 

      5890       5900       5910       5920       5930       5940 
SPSPVANTDA SVNQDIAYYQ ALSAERLQTD AAKIHPSTSA SQEFYEPGLE PSATAKLGDL 

      5950       5960       5970       5980       5990       6000 
QRSWETLKNV ISEKQRTLYE ALERQQKYQD SLQSISTKME AIELKLSESP EPGRSPESQM 

      6010       6020       6030       6040       6050       6060 
AEHQALMDEI LMLQDEINEL QSSLAEELVS ESCEADPAEQ LALQSTLTVL AERMSTIRMK 

      6070       6080       6090       6100       6110       6120 
ASGKRQLLEE KLNDQLEEQR QEQALQRYRC EADELDSWLL STKATLDTAL SPPKEPMDME 

      6130       6140       6150       6160       6170       6180 
AQLMDCQNML VEIEQKVVAL SELSVHNENL LLEGKAHTKD EAEQLAGKLR RLKGSLLELQ 

      6190       6200       6210       6220       6230       6240 
RALHDKQLNM QGTAQEKEES DVDLTATQSP GVQEWLAQAR TTWTQQRQSS LQQQKELEQE 

      6250       6260       6270       6280       6290       6300 
LAEQKSLLRS VASRGEEILI QHSAAETSGD AGEKPDVLSQ ELGMEGEKSS AEDQMRMKWE 

      6310       6320       6330       6340       6350       6360 
SLHQEFSTKQ KLLQNVLEQE QEQVLYSRPN RLLSGVPLYK GDVPTQDKSA VTSLLDGLNQ 

      6370       6380       6390       6400       6410       6420 
AFEEVSSQSG GAKRQSIHLE QKLYDGVSAT STWLDDVEER LFVATALLPE ETETCLFNQE 

      6430       6440       6450       6460       6470       6480 
ILAKDIKEMS EEMDKNKNLF SQAFPENGDN RDVIEDTLGC LLGRLSLLDS VVNQRCHQMK 

      6490       6500       6510       6520       6530       6540 
ERLQQILNFQ NDLKVLFTSL ADNKYIILQK LANVFEQPVA EQIEAIQQAE DGLKEFDAGI 

      6550       6560       6570       6580       6590       6600 
IELKRRGDKL QVEQPSMQEL SKLQDMYDEL MMIIGSRRSG LNQNLTLKSQ YERALQDLAD 

      6610       6620       6630       6640       6650       6660 
LLETGQEKMA GDQKIIVSSK EEIQQLLDKH KEYFQGLESH MILTETLFRK IISFAVQKET 

      6670       6680       6690       6700       6710       6720 
QFHTELMAQA SAVLKRAHKR GVELEYILET WSHLDEDQQE LSRQLEVVES SIPSVGLVEE 

      6730       6740       6750       6760       6770       6780 
NEDRLIDRIT LYQHLKSSLN EYQPKLYQVL DDGKRLLISI SCSDLESQLN QLGECWLSNT 

      6790       6800       6810       6820       6830       6840 
NKMSKELHRL ETILKHWTRY QSESADLIHW LQSAKDRLEF WTQQSVTVPQ ELEMVRDHLN 

      6850       6860       6870       6880       6890       6900 
AFLEFSKEVD AQSSLKSSVL STGNQLLRLK KVDTATLRSE LSRIDSQWTD LLTNIPAVQE 

      6910       6920       6930       6940       6950       6960 
KLHQLQMDKL PSRHAISEVM SWISLMENVI QKDEDNIKNS IGYKAIHEYL QKYKGFKIDI 

      6970       6980       6990       7000       7010       7020 
NCKQLTVDFV NQSVLQISSQ DVESKRSDKT DFAEQLGAMN KSWQILQGLV TEKIQLLEGL 

      7030       7040       7050       7060       7070       7080 
LESWSEYENN VQCLKTWFET QEKRLKQQHR IGDQASVQNA LKDCQDLEDL IKAKEKEVEK 

      7090       7100       7110       7120       7130       7140 
IEQNGLALIQ NKKEDVSSIV MSTLRELGQT WANLDHMVGQ LKILLKSVLD QWSSHKVAFD 

      7150       7160       7170       7180       7190       7200 
KINSYLMEAR YSLSRFRLLT GSLEAVQVQV DNLQNLQDDL EKQERSLQKF GSITNQLLKE 

      7210       7220       7230       7240       7250       7260 
CHPPVTETLT NTLKEVNMRW NNLLEEIAEQ LQSSKALLQL WQRYKDYSKQ CASTVQQQED 

      7270       7280       7290       7300       7310       7320 
RTNELLKAAT NKDIADDEVA TWIQDCNDLL KGLGTVKDSL FFLHELGEQL KQQVDASAAS 

      7330       7340       7350       7360       7370       7380 
AIQSDQLSLS QHLCALEQAL CKQQTSLQAG VLDYETFAKS LEALEAWIVE AEEILQGQDP 

      7390       7400       7410       7420       7430       7440 
SHSSDLSTIQ ERMEELKGQM LKFSSMAPDL DRLNELGYRL PLNDKEIKRM QNLNRHWSLI 

      7450       7460       7470       7480       7490       7500 
SSQTTERFSK LQSFLLQHQT FLEKCETWME FLVQTEQKLA VEISGNYQHL LEQQRAHELF 

      7510       7520       7530       7540       7550       7560 
QAEMFSRQQI LHSIIIDGQR LLEQGQVDDR DEFNLKLTLL SNQWQGVIRR AQQRRGIIDS 

      7570       7580       7590       7600       7610       7620 
QIRQWQRYRE MAEKLRKWLV EVSYLPMSGL GSVPIPLQQA RTLFDEVQFK EKVFLRQQGS 

      7630       7640       7650       7660       7670       7680 
YILTVEAGKQ LLLSADSGAE AALQAELAEI QEKWKSASMR LEEQKKKLAF LLKDWEKCEK 

      7690       7700       7710       7720       7730       7740 
GIADSLEKLR TFKKKLSQSL PDHHEELHAE QMRCKELENA VGSWTDDLTQ LSLLKDTLSA 

      7750       7760       7770       7780       7790       7800 
YISADDISIL NERVELLQRQ WEELCHQLSL RRQQIGERLN EWAVFSEKNK ELCEWLTQME 

      7810       7820       7830       7840       7850       7860 
SKVSQNGDIL IEEMIEKLKK DYQEEIAIAQ ENKIQLQQMG ERLAKASHES KASEIEYKLG 

      7870       7880       7890       7900       7910       7920 
KVNDRWQHLL DLIAARVKKL KETLVAVQQL DKNMSSLRTW LAHIESELAK PIVYDSCNSE 

      7930       7940       7950       7960       7970       7980 
EIQRKLNEQQ ELQRDIEKHS TGVASVLNLC EVLLHDCDAC ATDAECDSIQ QATRNLDRRW 

      7990       8000       8010       8020       8030       8040 
RNICAMSMER RLKIEETWRL WQKFLDDYSR FEDWLKSSER TAAFPSSSGV IYTVAKEELK 

      8050       8060       8070       8080       8090       8100 
KFEAFQRQVH ECLTQLELIN KQYRRLAREN RTDSACSLKQ MVHEGNQRWD NLQKRVTSIL 

      8110       8120       8130       8140       8150       8160 
RRLKHFIGQR EEFETARDSI LVWLTEMDLQ LTNIEHFSEC DVQAKIKQLK AFQQEISLNH 

      8170       8180       8190       8200       8210       8220 
NKIEQIIAQG EQLIEKSEPL DAAIIEEELD ELRRYCQEVF GRVERYHKKL IRLPLPDDEH 

      8230       8240       8250       8260       8270       8280 
DLSDRELELE DSAALSDLHW HDRSADSLLS PQPSSNLSLS LAQPLRSERS GRDTPASVDS 

      8290       8300       8310       8320       8330       8340 
IPLEWDHDYD LSRDLESAMS RALPSEDEEG QDDKDFYLRG AVGLSGDHSA LESQIRQLGK 

      8350       8360       8370       8380       8390       8400 
ALDDSRFQIQ QTENIIRSKT PTGPELDTSY KGYMKLLGEC SSSIDSVKRL EHKLKEEEES 

      8410       8420       8430       8440       8450       8460 
LPGFVNLHST ETQTAGVIDR WELLQAQALS KELRMKQNLQ KWQQFNSDLN SIWAWLGDTE 

      8470       8480       8490       8500       8510       8520 
EELEQLQRLE LSTDIQTIEL QIKKLKELQK AVDHRKAIIL SINLCSPEFT QADSKESRDL 

      8530       8540       8550       8560       8570       8580 
QDRLSQMNGR WDRVCSLLEE WRGLLQDALM QCQGFHEMSH GLLLMLENID RRKNEIVPID 

      8590       8600       8610       8620       8630       8640 
SNLDAEILQD HHKQLMQIKH ELLESQLRVA SLQDMSCQLL VNAEGTDCLE AKEKVHVIGN 

      8650       8660       8670       8680       8690       8700 
RLKLLLKEVS RHIKELEKLL DVSSSQQDLS SWSSADELDT SGSVSPTSGR STPNRQKTPR 

      8710       8720       8730       8740       8750       8760 
GKCSLSQPGP SVSSPHSRST KGGSDSSLSE PGPGRSGRGF LFRVLRAALP LQLLLLLLIG 

      8770       8780       8790 
LACLVPMSEE DYSCALSNNF ARSFHPMLRY TNGPPPL 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: DEAC32C9FD296ABD
Show »

FASTA3,321380,360
Isoform 3 (Alpha) [UniParc].

Checksum: 332A6E5ABA5A2248
Show »

FASTA982112,393
Isoform 4 [UniParc].

Checksum: 2D846CDD4BC30A8D
Show »

FASTA8,7491,005,239
Isoform 5 [UniParc].

Checksum: 01D6C47A6D74C395
Show »

FASTA1,443167,250
Isoform 6 [UniParc].

Checksum: 1ED934CA22A45E49
Show »

FASTA1,725199,267
Isoform 7 [UniParc].

Checksum: EEDEA59F5A4DBD2A
Show »

FASTA5,580642,672
Isoform 8 (Beta 2) [UniParc].

Checksum: 9D23ECB198DE3636
Show »

FASTA3,212367,873
Isoform 9 (Alpha 2) [UniParc].

Checksum: 621DAF9F731FEC9F
Show »

FASTA977111,583

References

« Hide 'large scale' references
[1]"Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues."
Zhang Q., Skepper J.N., Yang F., Davies J.D., Hegyi L., Roberts R.G., Weissberg P.L., Ellis J.A., Shanahan C.M.
J. Cell Sci. 114:4485-4498(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 8758-LEU--CYS-8763, VARIANTS VAL-7302 AND ALA-8323.
Tissue: Heart, Placenta, Skeletal muscle, Spleen and Testis.
[2]"The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300."
Zhang Q., Ragnauth C., Greener M.J., Shanahan C.M., Roberts R.G.
Genomics 80:473-481(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANTS THR-4596; MET-5015; VAL-7302 AND ALA-8323.
Tissue: Heart, Spleen and Testis.
[3]"Enaptin, a giant actin-binding protein, is an element of the nuclear membrane and the actin cytoskeleton."
Padmakumar V.C., Abraham S., Braune S., Noegel A.A., Tunggal B., Karakesisoglou I., Korenbaum E.
Exp. Cell Res. 295:330-339(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY.
Tissue: Cerebellum.
[4]Zhang Q., Shanahan C.M.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8 AND 9), VARIANTS VAL-7302 AND ALA-8323.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Golgi localization of Syne-1."
Gough L.L., Fan J., Chu S., Winnick S., Beck K.A.
Mol. Biol. Cell 14:2410-2424(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-856 (ISOFORM 1).
Tissue: Kidney.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-778 AND 2901-3476 (ISOFORM 1).
Tissue: Adrenal gland and Teratocarcinoma.
[8]"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-8797 (ISOFORM 5).
Tissue: Brain.
[9]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 743-8797 (ISOFORM 6).
Tissue: Brain.
[10]"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4219-8797 (ISOFORM 7), VARIANTS THR-4596 AND MET-5015.
Tissue: Brain.
[11]"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6922-8797 (ISOFORM 1), VARIANTS VAL-7302 AND ALA-8323.
Tissue: Brain.
[12]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[13]"Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C."
Mislow J.M.K., Kim M.S., Davis D.B., McNally E.M.
J. Cell Sci. 115:61-70(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7631-8797 (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ALA-8323.
[14]Ma F.-R., Zhu L.-P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8406-8797 (ISOFORM 1).
[15]"Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro."
Mislow J.M., Holaska J.M., Kim M.S., Lee K.K., Segura-Totten M., Wilson K.L., McNally E.M.
FEBS Lett. 525:135-140(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH EMD AND LMNA.
[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-8223; THR-8274; SER-8277 AND SER-8280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Mutations in SYNE1 lead to a newly discovered form of autosomal recessive cerebellar ataxia."
Gros-Louis F., Dupre N., Dion P., Fox M.A., Laurent S., Verreault S., Sanes J.R., Bouchard J.-P., Rouleau G.A.
Nat. Genet. 39:80-85(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SCAR8.
[18]"Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness."
Stewart-Hutchinson P.J., Hale C.M., Wirtz D., Hodzic D.
Exp. Cell Res. 314:1892-1905(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN, INTERACTION WITH SUN1 AND SUN2.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"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].
[21]"Cytoskeletal interactions at the nuclear envelope mediated by nesprins."
Taranum S., Sur I., Muller R., Lu W., Rashmi R.N., Munck M., Neumann S., Karakesisoglou I., Noegel A.A.
Int. J. Cell Biol. 2012:736524-736524(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH SYNE3.
[22]"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. expand/collapse author list , 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 COLORECTAL CANCER [LARGE SCALE ANALYSIS] MET-3671; ASP-4210; HIS-4223; ARG-5507 AND HIS-8468.
[23]"Nesprin-1 and -2 are involved in the pathogenesis of Emery Dreifuss muscular dystrophy and are critical for nuclear envelope integrity."
Zhang Q., Bethmann C., Worth N.F., Davies J.D., Wasner C., Feuer A., Ragnauth C.D., Yi Q., Mellad J.A., Warren D.T., Wheeler M.A., Ellis J.A., Skepper J.N., Vorgerd M., Schlotter-Weigel B., Weissberg P.L., Roberts R.G., Wehnert M., Shanahan C.M.
Hum. Mol. Genet. 16:2816-2833(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EDMD4 HIS-8095; LEU-8387 AND LYS-8461.
[24]"Identification of pathogenic gene variants in small families with intellectually disabled siblings by exome sequencing."
Schuurs-Hoeijmakers J.H., Vulto-van Silfhout A.T., Vissers L.E., van de Vondervoort I.I., van Bon B.W., de Ligt J., Gilissen C., Hehir-Kwa J.Y., Neveling K., del Rosario M., Hira G., Reitano S., Vitello A., Failla P., Greco D., Fichera M., Galesi O., Kleefstra T. expand/collapse author list , Greally M.T., Ockeloen C.W., Willemsen M.H., Bongers E.M., Janssen I.M., Pfundt R., Veltman J.A., Romano C., Willemsen M.A., van Bokhoven H., Brunner H.G., de Vries B.B., de Brouwer A.P.
J. Med. Genet. 50:802-811(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-655; THR-3088 AND SER-3892.
+Additional computationally mapped references.

Web resources

Wikipedia

Enaptin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY061755 mRNA. Translation: AAL33798.1.
AY061756 mRNA. Translation: AAL33799.1.
AF495910 mRNA. Translation: AAN60442.1.
AF535142 mRNA. Translation: AAN03486.1.
AY184203 mRNA. Translation: AAO27771.1.
AY184206 mRNA. Translation: AAO27774.1.
AL049548 Genomic DNA. No translation available.
AL136079 Genomic DNA. No translation available.
AL589963 Genomic DNA. No translation available.
AL591507 Genomic DNA. No translation available.
AL450401, AL078582, AL138832 Genomic DNA. Translation: CAI40728.1.
AL450401 expand/collapse EMBL AC list , AL078582, AL138832, AL357081 Genomic DNA. Translation: CAI40729.1.
AL357081 expand/collapse EMBL AC list , AL078582, AL138832, AL450401 Genomic DNA. Translation: CAI41322.1.
AL078582, AL138832, AL450401 Genomic DNA. Translation: CAI42283.1.
AL078582 expand/collapse EMBL AC list , AL138832, AL357081, AL450401 Genomic DNA. Translation: CAI42284.1.
AL138832, AL078582, AL450401 Genomic DNA. Translation: CAI42785.1.
AL138832 expand/collapse EMBL AC list , AL078582, AL357081, AL450401 Genomic DNA. Translation: CAI42786.1.
AY135172 mRNA. Translation: AAM95335.1. Sequence problems.
AY183142 mRNA. Translation: AAO23669.1.
AK056122 mRNA. Translation: BAB71097.1. Sequence problems.
AK094094 mRNA. Translation: BAC04284.1. Different initiation.
AB051543 mRNA. Translation: BAB21847.1.
AL713682 mRNA. Translation: CAD28486.2. Different initiation.
AB033088 mRNA. Translation: BAA86576.1.
AB018339 mRNA. Translation: BAA34516.2.
AF444779 mRNA. Translation: AAL38031.1. Different initiation.
AF043290 mRNA. Translation: AAC02992.2. Different initiation.
CCDSCCDS5235.1. [Q8NF91-4]
CCDS5236.2. [Q8NF91-1]
RefSeqNP_149062.1. NM_033071.3.
NP_892006.3. NM_182961.3. [Q8NF91-1]
XP_006715482.1. XM_006715419.1. [Q8NF91-1]
UniGeneHs.12967.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DXRX-ray2.32B8769-8797[»]
ProteinModelPortalQ8NF91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116928. 26 interactions.
IntActQ8NF91. 17 interactions.
MINTMINT-6489007.

PTM databases

PhosphoSiteQ8NF91.

Polymorphism databases

DMDM425906075.

Proteomic databases

MaxQBQ8NF91.
PaxDbQ8NF91.
PRIDEQ8NF91.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367253; ENSP00000356222; ENSG00000131018. [Q8NF91-6]
ENST00000367255; ENSP00000356224; ENSG00000131018. [Q8NF91-1]
ENST00000413186; ENSP00000414510; ENSG00000131018. [Q8NF91-5]
ENST00000423061; ENSP00000396024; ENSG00000131018.
GeneID23345.
KEGGhsa:23345.
UCSCuc003qos.4. human. [Q8NF91-2]
uc003qot.4. human. [Q8NF91-4]
uc003qou.4. human. [Q8NF91-1]
uc003qow.3. human. [Q8NF91-6]

Organism-specific databases

CTD23345.
GeneCardsGC06M152485.
GeneReviewsSYNE1.
HGNCHGNC:17089. SYNE1.
HPAHPA019113.
MIM608441. gene.
610743. phenotype.
612998. phenotype.
neXtProtNX_Q8NF91.
Orphanet98853. Autosomal dominant Emery-Dreifuss muscular dystrophy.
88644. Autosomal recessive ataxia, Beauce type.
319332. Autosomal recessive myogenic arthrogryposis multiplex congenita.
PharmGKBPA134975331.
HUGESearch...
Search...
Search...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOVERGENHBG066187.
OMAMKWESLH.
OrthoDBEOG72JWF7.
TreeFamTF329280.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ8NF91.
BgeeQ8NF91.
GenevestigatorQ8NF91.

Family and domain databases

Gene3D1.10.418.10. 2 hits.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR012315. KASH.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamPF00307. CH. 2 hits.
PF10541. KASH. 1 hit.
PF00435. Spectrin. 10 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00150. SPEC. 45 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 2 hits.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS51049. KASH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSYNE1. human.
GeneWikiEnaptin.
GenomeRNAi23345.
NextBio45305.
PROQ8NF91.
SOURCESearch...

Entry information

Entry nameSYNE1_HUMAN
AccessionPrimary (citable) accession number: Q8NF91
Secondary accession number(s): E7EQI5 expand/collapse secondary AC list , O94890, Q5JV19, Q5JV22, Q8N9P7, Q8TCP1, Q8WWW6, Q8WWW7, Q8WXF6, Q96N17, Q9C0A7, Q9H525, Q9H526, Q9NS36, Q9NU50, Q9UJ06, Q9UJ07, Q9ULF8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: November 28, 2012
Last modified: July 9, 2014
This is version 137 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM