Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q8WZ42 (TITIN_HUMAN)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Titin

Gene

TTN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase.1 Publication

Miscellaneous

In some isoforms, after the PEVK repeat region there is a long PEVK duplicated region. On account of this region, it has been very difficult to sequence the whole protein. The length of this region (ranging from 183 to 2174 residues), may be a key elastic element of titin.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+

Enzyme regulationi

Full activation of the protein kinase domain requires both phosphorylation of Tyr-32341, preventing it from blocking the catalytic aspartate residue, and binding of Ca/CALM to the C-terminal regulatory tail of the molecule which results in ATP binding to the kinase.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei32207ATPPROSITE-ProRule annotation1
Active sitei32298Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32184 – 32192ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • actin filament binding Source: BHF-UCL
  • actinin binding Source: BHF-UCL
  • ATP binding Source: UniProtKB-KW
  • calcium ion binding Source: BHF-UCL
  • calmodulin binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • muscle alpha-actinin binding Source: BHF-UCL
  • protease binding Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • protein self-association Source: BHF-UCL
  • protein serine/threonine kinase activity Source: UniProtKB
  • protein tyrosine kinase activity Source: MGI
  • structural constituent of muscle Source: BHF-UCL
  • structural molecule activity conferring elasticity Source: BHF-UCL
  • telethonin binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cardiac muscle contraction Source: BHF-UCL
  • cardiac muscle fiber development Source: BHF-UCL
  • cardiac muscle hypertrophy Source: BHF-UCL
  • cardiac muscle tissue morphogenesis Source: BHF-UCL
  • cardiac myofibril assembly Source: BHF-UCL
  • detection of muscle stretch Source: MGI
  • mitotic chromosome condensation Source: BHF-UCL
  • muscle contraction Source: UniProtKB
  • muscle filament sliding Source: Reactome
  • platelet degranulation Source: Reactome
  • positive regulation of gene expression Source: CAFA
  • positive regulation of protein secretion Source: CAFA
  • protein kinase A signaling Source: CAFA
  • regulation of catalytic activity Source: BHF-UCL
  • regulation of protein kinase activity Source: BHF-UCL
  • response to calcium ion Source: BHF-UCL
  • sarcomere organization Source: BHF-UCL
  • sarcomerogenesis Source: BHF-UCL
  • skeletal muscle myosin thick filament assembly Source: BHF-UCL
  • skeletal muscle thin filament assembly Source: BHF-UCL
  • striated muscle contraction Source: UniProtKB
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionCalmodulin-binding, Kinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-390522 Striated Muscle Contraction
SignaLinkiQ8WZ42
SIGNORiQ8WZ42

Protein family/group databases

MoonDBiQ8WZ42 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
Titin (EC:2.7.11.1)
Alternative name(s):
Connectin
Rhabdomyosarcoma antigen MU-RMS-40.14
Gene namesi
Name:TTN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000155657.24
HGNCiHGNC:12403 TTN
MIMi188840 gene
neXtProtiNX_Q8WZ42

Subcellular locationi

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Hereditary myopathy with early respiratory failure (HMERF)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant, adult-onset myopathy with early respiratory muscle involvement.
See also OMIM:603689
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_026634279R → W in HMERF; disrupts NBR1-binding. 1 PublicationCorresponds to variant dbSNP:rs138060032EnsemblClinVar.1
Cardiomyopathy, familial hypertrophic 9 (CMH9)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.
See also OMIM:613765
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_026687740R → L in CMH9. 1 PublicationCorresponds to variant dbSNP:rs28933405EnsemblClinVar.1
Cardiomyopathy, dilated 1G (CMD1G)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
See also OMIM:604145
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02668554V → M in CMD1G; affects interaction with TCAP/telethonin. 1 PublicationCorresponds to variant dbSNP:rs139517732EnsemblClinVar.1
Natural variantiVAR_026688743A → V in CMD1G; affects interaction with TCAP/telethonin. 1 PublicationCorresponds to variant dbSNP:rs267607157EnsemblClinVar.1
Natural variantiVAR_026689976W → R in CMD1G. 1 PublicationCorresponds to variant dbSNP:rs267607155EnsemblClinVar.1
Natural variantiVAR_0266903799S → Y in CMD1G. 1 Publication1
Natural variantiVAR_0266924465S → N in CMD1G. 1 PublicationCorresponds to variant dbSNP:rs281864908Ensembl.1
Natural variantiVAR_02669332996R → Q in CMD1G. 1 PublicationCorresponds to variant dbSNP:rs199642423Ensembl.1
Tardive tibial muscular dystrophy (TMD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant, late-onset distal myopathy. Muscle weakness and atrophy are usually confined to the anterior compartment of the lower leg, in particular the tibialis anterior muscle. Clinical symptoms usually occur at age 35-45 years or much later.
See also OMIM:600334
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02669434306I → N in TMD. 1 PublicationCorresponds to variant dbSNP:rs281864928Ensembl.1
Natural variantiVAR_02669534315L → P in TMD. 1 PublicationCorresponds to variant dbSNP:rs267607156Ensembl.1
Limb-girdle muscular dystrophy 2J (LGMD2J)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive degenerative myopathy characterized by progressive weakness of the pelvic and shoulder girdle muscles. Severe disability is observed within 20 years of onset.
See also OMIM:608807
Salih myopathy (SALMY)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive, early-onset muscular disorder characterized by dilated cardiomyopathy, delayed motor development with generalized muscle weakness predominantly affecting proximal and distal lower limbs. Skeletal muscle biopsies show minicore-like lesions with mitochondrial depletion and sarcomere disorganization, centralized nuclei, and type 1 fiber predominance. Dystrophic changes become apparent in the second decade. Cardiac muscle biopsies show disruption of myocardial architecture, nuclear hypertrophy, and endomysial fibrosis. Sudden death may occurr due to cardiomyopathy.
See also OMIM:611705

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi32207K → A: Disrupts catalytic activity. 1 Publication1
Mutagenesisi32341Y → E: No phosphorylation on tyrosine. 1 Publication1

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Limb-girdle muscular dystrophy

Organism-specific databases

DisGeNETi7273
GeneReviewsiTTN
MalaCardsiTTN
MIMi600334 phenotype
603689 phenotype
604145 phenotype
608807 phenotype
611705 phenotype
613765 phenotype
OpenTargetsiENSG00000155657
Orphaneti178148 Antenatal multiminicore disease with arthrogryposis multiplex congenita
169186 Autosomal recessive centronuclear myopathy
140922 Autosomal recessive limb-girdle muscular dystrophy type 2J
324604 Classic multiminicore myopathy
289377 Early-onset myopathy with fatal cardiomyopathy
293899 Familial isolated arrhythmogenic ventricular dysplasia, biventricular form
293888 Familial isolated arrhythmogenic ventricular dysplasia, left dominant form
293910 Familial isolated arrhythmogenic ventricular dysplasia, right dominant form
154 Familial isolated dilated cardiomyopathy
155 Familial isolated hypertrophic cardiomyopathy
178464 Hereditary proximal myopathy with early respiratory failure
609 Tibial muscular dystrophy
PharmGKBiPA37067

Polymorphism and mutation databases

BioMutaiTTN

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002393111 – 34350TitinAdd BLAST34350

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei263PhosphoserineBy similarity1
Modified residuei265PhosphoserineBy similarity1
Modified residuei267PhosphothreonineBy similarity1
Disulfide bondi964 ↔ 1015PROSITE-ProRule annotation
Disulfide bondi1724 ↔ 1777PROSITE-ProRule annotation
Disulfide bondi2109 ↔ 2134PROSITE-ProRule annotation1 Publication
Disulfide bondi2196 ↔ 2246PROSITE-ProRule annotation
Disulfide bondi3259 ↔ 3311PROSITE-ProRule annotation
Disulfide bondi4404 ↔ 4455PROSITE-ProRule annotation
Disulfide bondi4499 ↔ 4550PROSITE-ProRule annotation
Disulfide bondi4592 ↔ 4643PROSITE-ProRule annotation
Disulfide bondi4686 ↔ 4737PROSITE-ProRule annotation
Disulfide bondi4779 ↔ 4830PROSITE-ProRule annotation
Disulfide bondi5061 ↔ 5112PROSITE-ProRule annotation
Disulfide bondi5248 ↔ 5299PROSITE-ProRule annotation
Disulfide bondi5623 ↔ 5674PROSITE-ProRule annotation
Disulfide bondi5810 ↔ 5861PROSITE-ProRule annotation
Disulfide bondi5903 ↔ 5954PROSITE-ProRule annotation
Disulfide bondi6185 ↔ 6236PROSITE-ProRule annotation
Disulfide bondi6372 ↔ 6423PROSITE-ProRule annotation
Disulfide bondi6465 ↔ 6516PROSITE-ProRule annotation
Disulfide bondi6748 ↔ 6799PROSITE-ProRule annotation
Modified residuei6920PhosphoserineBy similarity1
Disulfide bondi7027 ↔ 7078PROSITE-ProRule annotation
Disulfide bondi7123 ↔ 7174PROSITE-ProRule annotation
Disulfide bondi7219 ↔ 7270PROSITE-ProRule annotation
Disulfide bondi7313 ↔ 7364PROSITE-ProRule annotation
Disulfide bondi7406 ↔ 7457PROSITE-ProRule annotation
Disulfide bondi7689 ↔ 7740PROSITE-ProRule annotation
Disulfide bondi7968 ↔ 8019PROSITE-ProRule annotation
Disulfide bondi8064 ↔ 8115PROSITE-ProRule annotation
Disulfide bondi8160 ↔ 8211PROSITE-ProRule annotation
Disulfide bondi8254 ↔ 8305PROSITE-ProRule annotation
Disulfide bondi8347 ↔ 8398PROSITE-ProRule annotation
Disulfide bondi8630 ↔ 8681PROSITE-ProRule annotation
Disulfide bondi8909 ↔ 8960PROSITE-ProRule annotation
Disulfide bondi9005 ↔ 9056PROSITE-ProRule annotation
Disulfide bondi9101 ↔ 9152PROSITE-ProRule annotation
Modified residuei9122PhosphoserineBy similarity1
Disulfide bondi9294 ↔ 9345PROSITE-ProRule annotation
Disulfide bondi9693 ↔ 9743PROSITE-ProRule annotation
Modified residuei11503PhosphoserineBy similarity1
Modified residuei12007PhosphothreonineBy similarity1
Modified residuei12009PhosphoserineBy similarity1
Modified residuei12022PhosphoserineBy similarity1
Disulfide bondi12067 ↔ 12117PROSITE-ProRule annotation
Disulfide bondi12611 ↔ 12660PROSITE-ProRule annotation
Disulfide bondi12966 ↔ 13016PROSITE-ProRule annotation
Disulfide bondi13233 ↔ 13283PROSITE-ProRule annotation
Disulfide bondi13322 ↔ 13372PROSITE-ProRule annotation
Disulfide bondi13411 ↔ 13461PROSITE-ProRule annotation
Disulfide bondi13771 ↔ 13821PROSITE-ProRule annotation
Modified residuei30443PhosphothreonineBy similarity1
Disulfide bondi31481 ↔ 31532PROSITE-ProRule annotation
Modified residuei32341Phosphotyrosine1 Publication1
Disulfide bondi32516 ↔ 32568PROSITE-ProRule annotation
Modified residuei33245PhosphoserineBy similarity1
Modified residuei33247PhosphoserineBy similarity1
Modified residuei33602PhosphoserineBy similarity1
Modified residuei33614PhosphoserineBy similarity1
Disulfide bondi33664 ↔ 33718PROSITE-ProRule annotation

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ8WZ42
MaxQBiQ8WZ42
PaxDbiQ8WZ42
PeptideAtlasiQ8WZ42
PRIDEiQ8WZ42
ProteomicsDBi75209
75210 [Q8WZ42-10]
75211 [Q8WZ42-11]
75212 [Q8WZ42-2]
75213 [Q8WZ42-3]
75214 [Q8WZ42-4]
75215 [Q8WZ42-5]
75216 [Q8WZ42-6]
75217 [Q8WZ42-7]
75218 [Q8WZ42-8]
75219 [Q8WZ42-9]

PTM databases

CarbonylDBiQ8WZ42
iPTMnetiQ8WZ42
PhosphoSitePlusiQ8WZ42
SwissPalmiQ8WZ42

Expressioni

Tissue specificityi

Isoforms 3, 7 and 8 are expressed in cardiac muscle. Isoform 4 is expressed in vertebrate skeletal muscle. Isoform 6 is expressed in skeletal muscle (at protein level).2 Publications

Gene expression databases

BgeeiENSG00000155657
ExpressionAtlasiQ8WZ42 baseline and differential
GenevisibleiQ8WZ42 HS

Organism-specific databases

HPAiCAB022682
HPA007042
HPA030048

Interactioni

Subunit structurei

Interacts with MYOM1, MYOM2, tropomyosin and myosin. Interacts with actin, primarily via the PEVK domains and with MYPN (By similarity). Interacts with FHL2, NEB, CRYAB, LMNA/lamin-A and LMNB/lamin-B. Interacts with TCAP/telethonin and/or ANK1 isoform Mu17/ank1.5, via the first two N-terminal immunoglobulin domains. Interacts with TRIM63 and TRIM55, through several domains including immunoglobulin domains 141 and 142. Interacts with ANKRD1, ANKRD2 and ANKRD23, via the region between immunoglobulin domains 77 and 78 and interacts with CAPN3, via immunoglobulin domain 79. Interacts with NBR1 through the protein kinase domain. Interacts with CALM/calmodulin. Isoform 6 interacts with OBSCN isoform 3. Interacts with CMYA5.By similarity13 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin filament binding Source: BHF-UCL
  • actinin binding Source: BHF-UCL
  • calmodulin binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • muscle alpha-actinin binding Source: BHF-UCL
  • protease binding Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • protein self-association Source: BHF-UCL
  • telethonin binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi113124, 70 interactors
ComplexPortaliCPX-101 Titin-Telethonin complex
CORUMiQ8WZ42
DIPiDIP-33449N
IntActiQ8WZ42, 95 interactors
MINTiQ8WZ42
STRINGi9606.ENSP00000343764

Structurei

Secondary structure

134350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Beta strandi15 – 18Combined sources4
Beta strandi23 – 33Combined sources11
Beta strandi36 – 45Combined sources10
Turni48 – 50Combined sources3
Beta strandi55 – 59Combined sources5
Beta strandi62 – 69Combined sources8
Helixi72 – 74Combined sources3
Beta strandi76 – 84Combined sources9
Beta strandi87 – 98Combined sources12
Beta strandi102 – 108Combined sources7
Beta strandi113 – 116Combined sources4
Beta strandi119 – 131Combined sources13
Beta strandi134 – 139Combined sources6
Beta strandi142 – 144Combined sources3
Beta strandi147 – 155Combined sources9
Beta strandi158 – 166Combined sources9
Helixi168 – 170Combined sources3
Beta strandi172 – 180Combined sources9
Beta strandi183 – 194Combined sources12
Beta strandi2076 – 2082Combined sources7
Beta strandi2087 – 2090Combined sources4
Beta strandi2095 – 2105Combined sources11
Beta strandi2108 – 2113Combined sources6
Beta strandi2122 – 2130Combined sources9
Beta strandi2133 – 2138Combined sources6
Helixi2143 – 2145Combined sources3
Beta strandi2147 – 2155Combined sources9
Beta strandi2158 – 2169Combined sources12
Beta strandi2797 – 2799Combined sources3
Beta strandi2804 – 2807Combined sources4
Beta strandi2812 – 2820Combined sources9
Beta strandi2826 – 2829Combined sources4
Beta strandi2838 – 2845Combined sources8
Beta strandi2848 – 2853Combined sources6
Helixi2858 – 2860Combined sources3
Beta strandi2862 – 2868Combined sources7
Beta strandi2871 – 2880Combined sources10
Beta strandi2884 – 2886Combined sources3
Beta strandi2891 – 2894Combined sources4
Beta strandi2899 – 2907Combined sources9
Beta strandi2914 – 2916Combined sources3
Beta strandi2924 – 2932Combined sources9
Beta strandi2935 – 2940Combined sources6
Helixi2945 – 2947Combined sources3
Beta strandi2949 – 2955Combined sources7
Beta strandi2958 – 2967Combined sources10
Beta strandi2971 – 2973Combined sources3
Beta strandi2978 – 2981Combined sources4
Beta strandi2986 – 2994Combined sources9
Beta strandi3000 – 3003Combined sources4
Beta strandi3012 – 3019Combined sources8
Beta strandi3022 – 3027Combined sources6
Helixi3032 – 3034Combined sources3
Beta strandi3036 – 3042Combined sources7
Beta strandi3045 – 3053Combined sources9
Beta strandi9582 – 9587Combined sources6
Beta strandi9592 – 9595Combined sources4
Beta strandi9600 – 9608Combined sources9
Beta strandi9616 – 9619Combined sources4
Beta strandi9628 – 9635Combined sources8
Beta strandi9638 – 9643Combined sources6
Helixi9648 – 9650Combined sources3
Beta strandi9652 – 9658Combined sources7
Beta strandi9661 – 9670Combined sources10
Beta strandi12680 – 12682Combined sources3
Beta strandi12687 – 12690Combined sources4
Beta strandi12691 – 12693Combined sources3
Beta strandi12695 – 12705Combined sources11
Beta strandi12709 – 12712Combined sources4
Beta strandi12719 – 12722Combined sources4
Beta strandi12723 – 12728Combined sources6
Beta strandi12731 – 12736Combined sources6
Helixi12741 – 12743Combined sources3
Beta strandi12745 – 12751Combined sources7
Beta strandi12754 – 12763Combined sources10
Beta strandi14223 – 14228Combined sources6
Beta strandi14232 – 14240Combined sources9
Beta strandi14252 – 14259Combined sources8
Beta strandi14275 – 14281Combined sources7
Beta strandi14288 – 14296Combined sources9
Beta strandi14308 – 14314Combined sources7
Beta strandi22291 – 22296Combined sources6
Beta strandi22299 – 22303Combined sources5
Beta strandi22319 – 22324Combined sources6
Beta strandi22340 – 22345Combined sources6
Beta strandi22354 – 22361Combined sources8
Beta strandi22367 – 22377Combined sources11
Helixi22381 – 22384Combined sources4
Beta strandi22883 – 22890Combined sources8
Beta strandi22895 – 22900Combined sources6
Beta strandi22912 – 22919Combined sources8
Beta strandi22926 – 22932Combined sources7
Beta strandi22934 – 22939Combined sources6
Beta strandi22947 – 22956Combined sources10
Beta strandi22970 – 22972Combined sources3
Beta strandi22982 – 22987Combined sources6
Beta strandi22992 – 22996Combined sources5
Beta strandi23009 – 23016Combined sources8
Beta strandi23023 – 23035Combined sources13
Beta strandi23043 – 23052Combined sources10
Beta strandi31458 – 31464Combined sources7
Beta strandi31469 – 31472Combined sources4
Beta strandi31475 – 31487Combined sources13
Beta strandi31490 – 31495Combined sources6
Beta strandi31498 – 31500Combined sources3
Beta strandi31504 – 31520Combined sources17
Helixi31524 – 31526Combined sources3
Beta strandi31528 – 31535Combined sources8
Beta strandi31540 – 31555Combined sources16
Beta strandi31563 – 31568Combined sources6
Beta strandi31573 – 31583Combined sources11
Beta strandi31586 – 31591Combined sources6
Beta strandi31600 – 31606Combined sources7
Beta strandi31608 – 31617Combined sources10
Helixi31620 – 31623Combined sources4
Beta strandi31625 – 31632Combined sources8
Beta strandi31637 – 31647Combined sources11
Beta strandi31856 – 31859Combined sources4
Beta strandi31864 – 31867Combined sources4
Beta strandi31872 – 31879Combined sources8
Beta strandi31885 – 31890Combined sources6
Beta strandi31893 – 31895Combined sources3
Beta strandi31899 – 31907Combined sources9
Turni31908 – 31910Combined sources3
Beta strandi31911 – 31916Combined sources6
Helixi31921 – 31923Combined sources3
Beta strandi31925 – 31933Combined sources9
Beta strandi31936 – 31952Combined sources17
Helixi31956 – 31959Combined sources4
Beta strandi31961 – 31967Combined sources7
Beta strandi31973 – 31982Combined sources10
Beta strandi31985 – 31992Combined sources8
Beta strandi31997 – 32000Combined sources4
Beta strandi32002 – 32005Combined sources4
Beta strandi32007 – 32013Combined sources7
Helixi32020 – 32022Combined sources3
Beta strandi32024 – 32032Combined sources9
Beta strandi32035 – 32046Combined sources12
Beta strandi32053 – 32059Combined sources7
Beta strandi32065 – 32070Combined sources6
Beta strandi32076 – 32078Combined sources3
Beta strandi32080 – 32089Combined sources10
Beta strandi32095 – 32108Combined sources14
Beta strandi32116 – 32125Combined sources10
Turni32175 – 32177Combined sources3
Beta strandi32178 – 32186Combined sources9
Beta strandi32188 – 32197Combined sources10
Turni32198 – 32201Combined sources4
Beta strandi32202 – 32209Combined sources8
Helixi32214 – 32228Combined sources15
Beta strandi32237 – 32243Combined sources7
Beta strandi32246 – 32251Combined sources6
Helixi32259 – 32263Combined sources5
Beta strandi32265 – 32267Combined sources3
Helixi32272 – 32291Combined sources20
Helixi32301 – 32303Combined sources3
Beta strandi32304 – 32310Combined sources7
Beta strandi32314 – 32316Combined sources3
Beta strandi32330 – 32336Combined sources7
Helixi32338 – 32340Combined sources3
Helixi32343 – 32346Combined sources4
Helixi32353 – 32369Combined sources17
Helixi32379 – 32388Combined sources10
Helixi32395 – 32398Combined sources4
Helixi32403 – 32410Combined sources8
Helixi32417 – 32419Combined sources3
Helixi32423 – 32428Combined sources6
Helixi32430 – 32433Combined sources4
Helixi32436 – 32438Combined sources3
Helixi32447 – 32457Combined sources11
Helixi32466 – 32472Combined sources7
Beta strandi32474 – 32476Combined sources3
Beta strandi32483 – 32489Combined sources7
Beta strandi32504 – 32506Combined sources3
Beta strandi32512 – 32520Combined sources9
Beta strandi32526 – 32531Combined sources6
Beta strandi32538 – 32547Combined sources10
Beta strandi32550 – 32555Combined sources6
Helixi32560 – 32562Combined sources3
Beta strandi32564 – 32571Combined sources8
Beta strandi32576 – 32585Combined sources10
Turni32586 – 32588Combined sources3
Turni33294 – 33297Combined sources4
Beta strandi33299 – 33305Combined sources7
Beta strandi33310 – 33313Combined sources4
Beta strandi33318 – 33328Combined sources11
Beta strandi33331 – 33336Combined sources6
Beta strandi33345 – 33352Combined sources8
Beta strandi33355 – 33360Combined sources6
Helixi33365 – 33367Combined sources3
Beta strandi33369 – 33377Combined sources9
Beta strandi33380 – 33391Combined sources12
Beta strandi33489 – 33492Combined sources4
Beta strandi33497 – 33503Combined sources7
Beta strandi33509 – 33512Combined sources4
Beta strandi33514 – 33516Combined sources3
Beta strandi33523 – 33526Combined sources4
Beta strandi33532 – 33538Combined sources7
Beta strandi33540 – 33547Combined sources8
Beta strandi33556 – 33560Combined sources5
Beta strandi33571 – 33577Combined sources7
Beta strandi33777 – 33783Combined sources7
Beta strandi33788 – 33794Combined sources7
Beta strandi33796 – 33806Combined sources11
Beta strandi33809 – 33814Combined sources6
Beta strandi33821 – 33830Combined sources10
Beta strandi33833 – 33838Combined sources6
Helixi33843 – 33845Combined sources3
Beta strandi33847 – 33855Combined sources9
Beta strandi33858 – 33869Combined sources12
Beta strandi34059 – 34071Combined sources13
Beta strandi34078 – 34088Combined sources11
Beta strandi34091 – 34096Combined sources6
Turni34104 – 34106Combined sources3
Beta strandi34107 – 34112Combined sources6
Beta strandi34115 – 34122Combined sources8
Helixi34125 – 34127Combined sources3
Beta strandi34129 – 34136Combined sources8
Beta strandi34138 – 34148Combined sources11
Beta strandi34254 – 34258Combined sources5
Beta strandi34263 – 34268Combined sources6
Beta strandi34271 – 34283Combined sources13
Beta strandi34286 – 34291Combined sources6
Helixi34300 – 34302Combined sources3
Beta strandi34304 – 34308Combined sources5
Beta strandi34310 – 34319Combined sources10
Helixi34322 – 34324Combined sources3
Beta strandi34326 – 34334Combined sources9
Beta strandi34337 – 34348Combined sources12

3D structure databases

DisProtiDP00072
ProteinModelPortaliQ8WZ42
SMRiQ8WZ42
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WZ42

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 96Ig-like 1Add BLAST91
Domaini104 – 192Ig-like 2Add BLAST89
Repeati417 – 462Z-repeat 1Add BLAST46
Repeati466 – 511Z-repeat 2Add BLAST46
Repeati512 – 554Z-repeat 3Add BLAST43
Repeati555 – 600Z-repeat 4Add BLAST46
Repeati601 – 646Z-repeat 5Add BLAST46
Repeati647 – 691Z-repeat 6Add BLAST45
Repeati692 – 740Z-repeat 7Add BLAST49
Domaini943 – 1031Ig-like 3Add BLAST89
Domaini1082 – 1172Ig-like 4Add BLAST91
Domaini1291 – 1382Ig-like 5Add BLAST92
Domaini1457 – 1546Ig-like 6Add BLAST90
Domaini1556 – 1646Ig-like 7Add BLAST91
Domaini1703 – 1793Ig-like 8Add BLAST91
Domaini1841 – 1928Ig-like 9Add BLAST88
Domaini2078 – 2167Ig-like 10Add BLAST90
Domaini2171 – 2262Ig-like 11Add BLAST92
Domaini2264 – 2354Ig-like 12Add BLAST91
Domaini2353 – 2443Ig-like 13Add BLAST91
Domaini2430 – 2529Ig-like 14Add BLAST100
Domaini2620 – 2703Ig-like 15Add BLAST84
Domaini2880 – 2965Ig-like 16Add BLAST86
Domaini2968 – 3050Ig-like 17Add BLAST83
Domaini3058 – 3141Ig-like 18Add BLAST84
Domaini3239 – 3327Ig-like 19Add BLAST89
Domaini3344 – 3432Ig-like 20Add BLAST89
Domaini3503 – 3586Ig-like 21Add BLAST84
Domaini3621 – 3712Ig-like 22Add BLAST92
Domaini4289 – 4376Ig-like 23Add BLAST88
Domaini4383 – 4471Ig-like 24Add BLAST89
Domaini4478 – 4566Ig-like 25Add BLAST89
Domaini4571 – 4659Ig-like 26Add BLAST89
Domaini4664 – 4753Ig-like 27Add BLAST90
Domaini4758 – 4846Ig-like 28Add BLAST89
Domaini4851 – 4936Ig-like 29Add BLAST86
Domaini4943 – 5032Ig-like 30Add BLAST90
Domaini5040 – 5128Ig-like 31Add BLAST89
Domaini5133 – 5221Ig-like 32Add BLAST89
Domaini5225 – 5314Ig-like 33Add BLAST90
Domaini5320 – 5408Ig-like 34Add BLAST89
Domaini5413 – 5501Ig-like 35Add BLAST89
Domaini5505 – 5594Ig-like 36Add BLAST90
Domaini5602 – 5690Ig-like 37Add BLAST89
Domaini5695 – 5783Ig-like 38Add BLAST89
Domaini5788 – 5877Ig-like 39Add BLAST90
Domaini5882 – 5970Ig-like 40Add BLAST89
Domaini5975 – 6063Ig-like 41Add BLAST89
Domaini6067 – 6156Ig-like 42Add BLAST90
Domaini6164 – 6252Ig-like 43Add BLAST89
Domaini6257 – 6347Ig-like 44Add BLAST91
Domaini6350 – 6440Ig-like 45Add BLAST91
Domaini6444 – 6534Ig-like 46Add BLAST91
Domaini6537 – 6626Ig-like 47Add BLAST90
Domaini6630 – 6721Ig-like 48Add BLAST92
Domaini6727 – 6815Ig-like 49Add BLAST89
Domaini6820 – 6908Ig-like 50Add BLAST89
Domaini6912 – 7001Ig-like 51Add BLAST90
Domaini7005 – 7093Ig-like 52Add BLAST89
Domaini7102 – 7190Ig-like 53Add BLAST89
Domaini7198 – 7286Ig-like 54Add BLAST89
Domaini7291 – 7380Ig-like 55Add BLAST90
Domaini7385 – 7473Ig-like 56Add BLAST89
Domaini7478 – 7567Ig-like 57Add BLAST90
Domaini7571 – 7662Ig-like 58Add BLAST92
Domaini7668 – 7756Ig-like 59Add BLAST89
Domaini7761 – 7849Ig-like 60Add BLAST89
Domaini7853 – 7942Ig-like 61Add BLAST90
Domaini7946 – 8035Ig-like 62Add BLAST90
Domaini8042 – 8133Ig-like 63Add BLAST92
Domaini8138 – 8229Ig-like 64Add BLAST92
Domaini8232 – 8321Ig-like 65Add BLAST90
Domaini8326 – 8414Ig-like 66Add BLAST89
Domaini8419 – 8508Ig-like 67Add BLAST90
Domaini8512 – 8603Ig-like 68Add BLAST92
Domaini8609 – 8697Ig-like 69Add BLAST89
Domaini8702 – 8790Ig-like 70Add BLAST89
Domaini8794 – 8883Ig-like 71Add BLAST90
Domaini8888 – 8976Ig-like 72Add BLAST89
Domaini8984 – 9074Ig-like 73Add BLAST91
Domaini9079 – 9168Ig-like 74Add BLAST90
Domaini9176 – 9265Ig-like 75Add BLAST90
Domaini9272 – 9361Ig-like 76Add BLAST90
Domaini9366 – 9470Ig-like 77Add BLAST105
Domaini9660 – 9755Ig-like 78Add BLAST96
Domaini9760 – 9851Ig-like 79Add BLAST92
Repeati10216 – 10242PEVK 1Add BLAST27
Repeati10244 – 10270PEVK 2Add BLAST27
Repeati10272 – 10298PEVK 3Add BLAST27
Repeati10300 – 10326PEVK 4Add BLAST27
Repeati10327 – 10353PEVK 5Add BLAST27
Repeati10355 – 10381PEVK 6Add BLAST27
Repeati10508 – 10534PEVK 7Add BLAST27
Repeati10536 – 10562PEVK 8Add BLAST27
Repeati10592 – 10618PEVK 9Add BLAST27
Repeati10878 – 10904PEVK 10Add BLAST27
Repeati10906 – 10930PEVK 11Add BLAST25
Repeati10932 – 10958PEVK 12Add BLAST27
Repeati10960 – 10986PEVK 13Add BLAST27
Repeati10987 – 11014PEVK 14Add BLAST28
Repeati11363 – 11396PEVK 15Add BLAST34
Repeati11397 – 11421PEVK 16Add BLAST25
Repeati11453 – 11479PEVK 17Add BLAST27
Repeati11481 – 11507PEVK 18Add BLAST27
Repeati11509 – 11535PEVK 19Add BLAST27
Repeati11537 – 11563PEVK 20Add BLAST27
Repeati11565 – 11591PEVK 21Add BLAST27
Repeati11657 – 11683PEVK 22Add BLAST27
Repeati11703 – 11729PEVK 23Add BLAST27
Repeati11745 – 11771PEVK 24Add BLAST27
Repeati11775 – 11801PEVK 25Add BLAST27
Repeati11836 – 11862PEVK 26Add BLAST27
Repeati11864 – 11890PEVK 27Add BLAST27
Repeati11893 – 11919PEVK 28Add BLAST27
Repeati11929 – 11955PEVK 29Add BLAST27
Repeati11966 – 11992PEVK 30Add BLAST27
Repeati11996 – 12022PEVK 31Add BLAST27
Domaini12041 – 12133Ig-like 80Add BLAST93
Domaini12138 – 12222Ig-like 81Add BLAST85
Domaini12233 – 12318Ig-like 82Add BLAST86
Domaini12499 – 12584Ig-like 83Add BLAST86
Domaini12590 – 12672Ig-like 84Add BLAST83
Domaini12766 – 12850Ig-like 85Add BLAST85
Domaini12945 – 13032Ig-like 86Add BLAST88
Domaini13120 – 13206Ig-like 87Add BLAST87
Domaini13210 – 13295Ig-like 88Add BLAST86
Domaini13299 – 13384Ig-like 89Add BLAST86
Domaini13388 – 13478Ig-like 90Add BLAST91
Domaini13479 – 13562Ig-like 91Add BLAST84
Domaini13565 – 13655Ig-like 92Add BLAST91
Domaini13659 – 13748Ig-like 93Add BLAST90
Domaini13749 – 13833Ig-like 94Add BLAST85
Domaini13927 – 14012Ig-like 95Add BLAST86
Domaini14019 – 14114Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST96
Domaini14120 – 14215Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini14221 – 14316Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST96
Domaini14417 – 14513Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST97
Domaini14517 – 14614Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST98
Domaini14615 – 14708Ig-like 96Add BLAST94
Domaini14713 – 14806Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST94
Domaini14812 – 14907Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST96
Domaini14913 – 15007Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST95
Domaini15010 – 15107Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST98
Domaini15113 – 15207Fibronectin type-III 10PROSITE-ProRule annotationAdd BLAST95
Domaini15214 – 15310Fibronectin type-III 11PROSITE-ProRule annotationAdd BLAST97
Domaini15314 – 15402Ig-like 97Add BLAST<