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Protein

Alpha-parvin

Gene

PARVA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration.By similarity4 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Angiogenesis, Cell adhesion, Cell shape, Chemotaxis, Cilium biogenesis/degradation

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_20649. Cell-extracellular matrix interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-parvin
Alternative name(s):
Actopaxin
CH-ILKBP
Calponin-like integrin-linked kinase-binding protein
Matrix-remodeling-associated protein 2
Gene namesi
Name:PARVA
Synonyms:MXRA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:14652. PARVA.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • focal adhesion Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32950.

Polymorphism and mutation databases

BioMutaiPARVA.
DMDMi20139236.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 372371Alpha-parvinPRO_0000121580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei8 – 81Phosphoserine1 Publication
Modified residuei14 – 141Phosphoserine1 Publication
Modified residuei19 – 191Phosphoserine3 Publications
Modified residuei28 – 281Phosphoserine1 Publication
Modified residuei62 – 621Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NVD7.
PaxDbiQ9NVD7.
PRIDEiQ9NVD7.

PTM databases

PhosphoSiteiQ9NVD7.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in heart, skeletal muscle, kidney and liver.3 Publications

Gene expression databases

BgeeiQ9NVD7.
CleanExiHS_PARVA.
GenevisibleiQ9NVD7. HS.

Organism-specific databases

HPAiHPA005964.

Interactioni

Subunit structurei

Interacts with TGFB1I1 (By similarity). Interacts with ILK, LIMS1 and PXN (via LD motifs). Interacts with ARHGAP31. Interacts with the actin cytoskeleton.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ILKQ1341811EBI-747655,EBI-747644
MOCOSQ96EN84EBI-747655,EBI-1220583

Protein-protein interaction databases

BioGridi120860. 29 interactions.
IntActiQ9NVD7. 11 interactions.
MINTiMINT-1465264.
STRINGi9606.ENSP00000334008.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi249 – 2568Combined sources
Helixi258 – 27619Combined sources
Helixi277 – 2793Combined sources
Turni286 – 2927Combined sources
Helixi294 – 30310Combined sources
Helixi310 – 3123Combined sources
Helixi320 – 33617Combined sources
Helixi346 – 3505Combined sources
Helixi354 – 36815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K2RNMR-A244-372[»]
2VZCX-ray1.05A/B242-372[»]
2VZDX-ray2.10A/B242-372[»]
2VZGX-ray1.80B242-372[»]
2VZIX-ray2.20B242-372[»]
3KMUX-ray1.80B248-372[»]
3KMWX-ray2.00B248-372[»]
3REPX-ray1.80B248-372[»]
ProteinModelPortaliQ9NVD7.
SMRiQ9NVD7. Positions 246-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NVD7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 201107CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini262 – 369108CH 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 255Interaction with ARHGAP31

Sequence similaritiesi

Belongs to the parvin family.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG303418.
HOGENOMiHOG000247027.
HOVERGENiHBG053517.
InParanoidiQ9NVD7.
KOiK06275.
PhylomeDBiQ9NVD7.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
InterProiIPR001715. CH-domain.
IPR028433. Parvin.
[Graphical view]
PANTHERiPTHR12114. PTHR12114. 1 hit.
PfamiPF00307. CH. 2 hits.
[Graphical view]
PIRSFiPIRSF039131. Parvin. 1 hit.
SMARTiSM00033. CH. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 2 hits.
PROSITEiPS50021. CH. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NVD7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATSPQKSPS VPKSPTPKSP PSRKKDDSFL GKLGGTLARR KKAKEVSELQ
60 70 80 90 100
EEGMNAINLP LSPIPFELDP EDTMLEENEV RTMVDPNSRS DPKLQELMKV
110 120 130 140 150
LIDWINDVLV GERIIVKDLA EDLYDGQVLQ KLFEKLESEK LNVAEVTQSE
160 170 180 190 200
IAQKQKLQTV LEKINETLKL PPRSIKWNVD SVHAKSLVAI LHLLVALSQY
210 220 230 240 250
FRAPIRLPDH VSIQVVVVQK REGILQSRQI QEEITGNTEA LSGRHERDAF
260 270 280 290 300
DTLFDHAPDK LNVVKKTLIT FVNKHLNKLN LEVTELETQF ADGVYLVLLM
310 320 330 340 350
GLLEGYFVPL HSFFLTPDSF EQKVLNVSFA FELMQDGGLE KPKPRPEDIV
360 370
NCDLKSTLRV LYNLFTKYRN VE
Length:372
Mass (Da):42,244
Last modified:October 1, 2000 - v1
Checksum:iF48BB5B1E83F8CEF
GO
Isoform 2 (identifier: Q9NVD7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-182: EKLESEKLNV...RSIKWNVDSV → GRRVECCNGC...KCVEHGITAQ
     183-372: Missing.

Note: No experimental confirmation available.
Show »
Length:182
Mass (Da):20,625
Checksum:iB7D6685D209E628F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111V → A in AAH14535 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei134 – 18249EKLES…NVDSV → GRRVECCNGCVFNCRWLDHL LVARRSYSQFTVAYLEMDYK CVEHGITAQ in isoform 2. 1 PublicationVSP_008884Add
BLAST
Alternative sequencei183 – 372190Missing in isoform 2. 1 PublicationVSP_008885Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237771 mRNA. Translation: AAG27173.1.
AF325830 mRNA. Translation: AAK49911.1.
AK001655 mRNA. Translation: BAA91815.1.
AK022316 mRNA. Translation: BAB14009.1.
BC016713 mRNA. Translation: AAH16713.1.
BC014535 mRNA. Translation: AAH14535.1.
RefSeqiNP_060692.2. NM_018222.4.
UniGeneiHs.432914.

Genome annotation databases

EnsembliENST00000550549; ENSP00000447198; ENSG00000197702.
GeneIDi55742.
KEGGihsa:55742.
UCSCiuc001mkh.3. human. [Q9NVD7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237771 mRNA. Translation: AAG27173.1.
AF325830 mRNA. Translation: AAK49911.1.
AK001655 mRNA. Translation: BAA91815.1.
AK022316 mRNA. Translation: BAB14009.1.
BC016713 mRNA. Translation: AAH16713.1.
BC014535 mRNA. Translation: AAH14535.1.
RefSeqiNP_060692.2. NM_018222.4.
UniGeneiHs.432914.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K2RNMR-A244-372[»]
2VZCX-ray1.05A/B242-372[»]
2VZDX-ray2.10A/B242-372[»]
2VZGX-ray1.80B242-372[»]
2VZIX-ray2.20B242-372[»]
3KMUX-ray1.80B248-372[»]
3KMWX-ray2.00B248-372[»]
3REPX-ray1.80B248-372[»]
ProteinModelPortaliQ9NVD7.
SMRiQ9NVD7. Positions 246-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120860. 29 interactions.
IntActiQ9NVD7. 11 interactions.
MINTiMINT-1465264.
STRINGi9606.ENSP00000334008.

PTM databases

PhosphoSiteiQ9NVD7.

Polymorphism and mutation databases

BioMutaiPARVA.
DMDMi20139236.

Proteomic databases

MaxQBiQ9NVD7.
PaxDbiQ9NVD7.
PRIDEiQ9NVD7.

Protocols and materials databases

DNASUi55742.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000550549; ENSP00000447198; ENSG00000197702.
GeneIDi55742.
KEGGihsa:55742.
UCSCiuc001mkh.3. human. [Q9NVD7-2]

Organism-specific databases

CTDi55742.
GeneCardsiGC11P012398.
HGNCiHGNC:14652. PARVA.
HPAiHPA005964.
MIMi608120. gene.
neXtProtiNX_Q9NVD7.
PharmGKBiPA32950.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG303418.
HOGENOMiHOG000247027.
HOVERGENiHBG053517.
InParanoidiQ9NVD7.
KOiK06275.
PhylomeDBiQ9NVD7.

Enzyme and pathway databases

ReactomeiREACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_20649. Cell-extracellular matrix interactions.

Miscellaneous databases

ChiTaRSiPARVA. human.
EvolutionaryTraceiQ9NVD7.
GeneWikiiPARVA.
GenomeRNAii55742.
NextBioi60703.
PROiQ9NVD7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NVD7.
CleanExiHS_PARVA.
GenevisibleiQ9NVD7. HS.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
InterProiIPR001715. CH-domain.
IPR028433. Parvin.
[Graphical view]
PANTHERiPTHR12114. PTHR12114. 1 hit.
PfamiPF00307. CH. 2 hits.
[Graphical view]
PIRSFiPIRSF039131. Parvin. 1 hit.
SMARTiSM00033. CH. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 2 hits.
PROSITEiPS50021. CH. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily."
    Olski T.M., Noegel A.A., Korenbaum E.
    J. Cell Sci. 114:525-538(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading."
    Tu Y., Huang Y., Zhang Y., Hua Y., Wu C.
    J. Cell Biol. 153:585-598(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ILK; LIMS1 AND WITH ACTIN CYTOSKELETON, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "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.
    , 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] (ISOFORMS 1 AND 2).
    Tissue: Mammary gland.
  4. "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 1).
    Tissue: Brain.
  5. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
    Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
    Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 118-131.
    Tissue: Adipocyte.
  6. "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion."
    Nikolopoulos S.N., Turner C.E.
    J. Cell Biol. 151:1435-1448(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. "Genomic organization and expression profile of the parvin family of focal adhesion proteins in mice and humans."
    Korenbaum E., Olski T.M., Noegel A.A.
    Gene 279:69-79(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival."
    Zhang Y., Chen K., Tu Y., Wu C.
    J. Biol. Chem. 279:41695-41705(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ILK.
  9. "CdGAP associates with actopaxin to regulate integrin-dependent changes in cell morphology and motility."
    LaLonde D.P., Grubinger M., Lamarche-Vane N., Turner C.E.
    Curr. Biol. 16:1375-1385(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGAP31.
  10. "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-28 AND SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Functional genomic screen for modulators of ciliogenesis and cilium length."
    Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
    Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "LNK (SH2B3) is a key regulator of integrin signaling in endothelial cells and targets alpha-parvin to control cell adhesion and migration."
    Devalliere J., Chatelais M., Fitau J., Gerard N., Hulin P., Velazquez L., Turner C.E., Charreau B.
    FASEB J. 26:2592-2606(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly."
    Wang X., Fukuda K., Byeon I.J., Velyvis A., Wu C., Gronenborn A., Qin J.
    J. Biol. Chem. 283:21113-21119(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 244-372 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
  18. "Structural analysis of the interactions between paxillin LD motifs and alpha-parvin."
    Lorenz S., Vakonakis I., Lowe E.D., Campbell I.D., Noble M.E., Hoellerer M.K.
    Structure 16:1521-1531(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 242-372 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
  19. "The pseudoactive site of ILK is essential for its binding to alpha-parvin and localization to focal adhesions."
    Fukuda K., Gupta S., Chen K., Wu C., Qin J.
    Mol. Cell 36:819-830(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 248-372 IN COMPLEX WITH ILK, INTERACTION WITH ILK.

Entry informationi

Entry nameiPARVA_HUMAN
AccessioniPrimary (citable) accession number: Q9NVD7
Secondary accession number(s): Q96C85, Q9HA48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.