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Protein

SPARC-like protein 1

Gene

SPARCL1

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

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi635 – 64612PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
SPARC-like protein 1
Alternative name(s):
High endothelial venule protein
Short name:
Hevin
MAST 9
Gene namesi
Name:SPARCL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:11220. SPARCL1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36056.

Polymorphism and mutation databases

BioMutaiSPARCL1.
DMDMi259016170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 664648SPARC-like protein 1PRO_0000020312Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi31 – 311O-linked (GalNAc...)1 Publication
Glycosylationi40 – 401O-linked (GalNAc...)1 Publication
Glycosylationi44 – 441O-linked (GalNAc...)1 Publication
Modified residuei76 – 761PhosphoserineBy similarity
Modified residuei84 – 841PhosphoserineBy similarity
Modified residuei92 – 921PhosphoserineBy similarity
Glycosylationi116 – 1161O-linked (GalNAc...)1 Publication
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence analysis
Modified residuei171 – 1711PhosphoserineBy similarity
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence analysis
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence analysis
Modified residuei272 – 2721PhosphoserineBy similarity
Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence analysis
Glycosylationi331 – 3311O-linked (GalNAc...)
Modified residuei358 – 3581PhosphoserineBy similarity
Modified residuei365 – 3651PhosphoserineBy similarity
Glycosylationi398 – 3981O-linked (GalNAc...)2 Publications
Glycosylationi412 – 4121N-linked (GlcNAc...)1 Publication
Modified residuei420 – 4201PhosphoserineBy similarity
Disulfide bondi433 ↔ 444PROSITE-ProRule annotation
Disulfide bondi438 ↔ 454PROSITE-ProRule annotation
Disulfide bondi456 ↔ 490PROSITE-ProRule annotation
Disulfide bondi462 ↔ 483PROSITE-ProRule annotation
Disulfide bondi472 ↔ 509PROSITE-ProRule annotation
Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence analysis
Disulfide bondi515 ↔ 626PROSITE-ProRule annotation
Disulfide bondi634 ↔ 650PROSITE-ProRule annotation

Post-translational modificationi

N- and O-glycosylated. O-glycosylated with a core 1 or possibly core 8 glycan.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ14515.
PRIDEiQ14515.

PTM databases

iPTMnetiQ14515.
PhosphoSiteiQ14515.
UniCarbKBiQ14515.

Expressioni

Tissue specificityi

Highly expressed in lymph node, brain, heart, lung, skeletal muscle, ovary, small intestine, and colon, with lower levels in placenta, pancreas, testis, spleen, and thymus, and no expression in kidney, liver, and peripheral blood leukocytes.

Gene expression databases

BgeeiQ14515.
CleanExiHS_SPARCL1.
ExpressionAtlasiQ14515. baseline and differential.
GenevisibleiQ14515. HS.

Organism-specific databases

HPAiCAB026225.

Interactioni

Protein-protein interaction databases

BioGridi113992. 3 interactions.
IntActiQ14515. 3 interactions.
STRINGi9606.ENSP00000282470.

Structurei

3D structure databases

ProteinModelPortaliQ14515.
SMRiQ14515. Positions 433-663.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini432 – 45423Follistatin-likeAdd
BLAST
Domaini450 – 51162Kazal-likePROSITE-ProRule annotationAdd
BLAST
Domaini622 – 65736EF-handPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 3410O-glycosylated at one additional site

Sequence similaritiesi

Belongs to the SPARC family.Curated
Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 1 follistatin-like domain.Curated
Contains 1 Kazal-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4004. Eukaryota.
ENOG41101WW. LUCA.
GeneTreeiENSGT00510000046787.
HOGENOMiHOG000063702.
HOVERGENiHBG079212.
InParanoidiQ14515.
OMAiHCVCQDP.
OrthoDBiEOG738059.
PhylomeDBiQ14515.
TreeFamiTF319356.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR001999. Osteonectin_CS.
IPR016359. SPARC-like_p1.
IPR019577. SPARC/Testican_Ca-bd-dom.
[Graphical view]
PfamiPF09289. FOLN. 1 hit.
PF00050. Kazal_1. 1 hit.
PF10591. SPARC_Ca_bdg. 1 hit.
[Graphical view]
PIRSFiPIRSF002574. SPARC-like_p1. 1 hit.
SMARTiSM00274. FOLN. 1 hit.
SM00280. KAZAL. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS51465. KAZAL_2. 1 hit.
PS00612. OSTEONECTIN_1. 1 hit.
PS00613. OSTEONECTIN_2. 1 hit.
[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: Q14515-1) [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
MKTGLFFLCL LGTAAAIPTN ARLLSDHSKP TAETVAPDNT AIPSLRAEAE
60 70 80 90 100
ENEKETAVST EDDSHHKAEK SSVLKSKEES HEQSAEQGKS SSQELGLKDQ
110 120 130 140 150
EDSDGHLSVN LEYAPTEGTL DIKEDMSEPQ EKKLSENTDF LAPGVSSFTD
160 170 180 190 200
SNQQESITKR EENQEQPRNY SHHQLNRSSK HSQGLRDQGN QEQDPNISNG
210 220 230 240 250
EEEEEKEPGE VGTHNDNQER KTELPREHAN SKQEEDNTQS DDILEESDQP
260 270 280 290 300
TQVSKMQEDE FDQGNQEQED NSNAEMEEEN ASNVNKHIQE TEWQSQEGKT
310 320 330 340 350
GLEAISNHKE TEEKTVSEAL LMEPTDDGNT TPRNHGVDDD GDDDGDDGGT
360 370 380 390 400
DGPRHSASDD YFIPSQAFLE AERAQSIAYH LKIEEQREKV HENENIGTTE
410 420 430 440 450
PGEHQEAKKA ENSSNEEETS SEGNMRVHAV DSCMSFQCKR GHICKADQQG
460 470 480 490 500
KPHCVCQDPV TCPPTKPLDQ VCGTDNQTYA SSCHLFATKC RLEGTKKGHQ
510 520 530 540 550
LQLDYFGACK SIPTCTDFEV IQFPLRMRDW LKNILMQLYE ANSEHAGYLN
560 570 580 590 600
EKQRNKVKKI YLDEKRLLAG DHPIDLLLRD FKKNYHMYVY PVHWQFSELD
610 620 630 640 650
QHPMDRVLTH SELAPLRASL VPMEHCITRF FEECDPNKDK HITLKEWGHC
660
FGIKEEDIDE NLLF
Length:664
Mass (Da):75,208
Last modified:September 22, 2009 - v2
Checksum:i0750B0080FDB96B6
GO
Isoform 2 (identifier: Q14515-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-125: Missing.

Note: No experimental confirmation available.
Show »
Length:539
Mass (Da):61,760
Checksum:i94C860ABF8B60ADA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51L → P in CAA60386 (Ref. 2) Curated
Sequence conflicti46 – 461R → W in CAA60386 (Ref. 2) Curated
Sequence conflicti116 – 1161T → S in CAA57650 (PubMed:7600298).Curated
Sequence conflicti127 – 1271S → I in CAA60386 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491A → D.1 Publication
Corresponds to variant rs13051 [ dbSNP | Ensembl ].
VAR_016107
Natural varianti106 – 1061H → D.1 Publication
Corresponds to variant rs1049544 [ dbSNP | Ensembl ].
VAR_058849
Natural varianti419 – 4191T → A.
Corresponds to variant rs1130643 [ dbSNP | Ensembl ].
VAR_056578

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 125125Missing in isoform 2. 1 PublicationVSP_056678Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82157 mRNA. Translation: CAA57650.1.
X86693 mRNA. Translation: CAA60386.1.
AK304494 mRNA. Translation: BAG65302.1.
AC093906 Genomic DNA. No translation available.
AC112250 Genomic DNA. No translation available.
CCDSiCCDS3622.1. [Q14515-1]
CCDS77939.1. [Q14515-2]
PIRiS60062.
RefSeqiNP_001121782.1. NM_001128310.2. [Q14515-1]
NP_001278905.1. NM_001291976.1. [Q14515-2]
NP_001278906.1. NM_001291977.1. [Q14515-2]
NP_004675.3. NM_004684.5. [Q14515-1]
UniGeneiHs.62886.

Genome annotation databases

EnsembliENST00000282470; ENSP00000282470; ENSG00000152583. [Q14515-1]
ENST00000418378; ENSP00000414856; ENSG00000152583. [Q14515-1]
ENST00000503414; ENSP00000422903; ENSG00000152583. [Q14515-2]
GeneIDi8404.
KEGGihsa:8404.
UCSCiuc003hqs.5. human. [Q14515-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82157 mRNA. Translation: CAA57650.1.
X86693 mRNA. Translation: CAA60386.1.
AK304494 mRNA. Translation: BAG65302.1.
AC093906 Genomic DNA. No translation available.
AC112250 Genomic DNA. No translation available.
CCDSiCCDS3622.1. [Q14515-1]
CCDS77939.1. [Q14515-2]
PIRiS60062.
RefSeqiNP_001121782.1. NM_001128310.2. [Q14515-1]
NP_001278905.1. NM_001291976.1. [Q14515-2]
NP_001278906.1. NM_001291977.1. [Q14515-2]
NP_004675.3. NM_004684.5. [Q14515-1]
UniGeneiHs.62886.

3D structure databases

ProteinModelPortaliQ14515.
SMRiQ14515. Positions 433-663.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113992. 3 interactions.
IntActiQ14515. 3 interactions.
STRINGi9606.ENSP00000282470.

PTM databases

iPTMnetiQ14515.
PhosphoSiteiQ14515.
UniCarbKBiQ14515.

Polymorphism and mutation databases

BioMutaiSPARCL1.
DMDMi259016170.

Proteomic databases

PaxDbiQ14515.
PRIDEiQ14515.

Protocols and materials databases

DNASUi8404.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000282470; ENSP00000282470; ENSG00000152583. [Q14515-1]
ENST00000418378; ENSP00000414856; ENSG00000152583. [Q14515-1]
ENST00000503414; ENSP00000422903; ENSG00000152583. [Q14515-2]
GeneIDi8404.
KEGGihsa:8404.
UCSCiuc003hqs.5. human. [Q14515-1]

Organism-specific databases

CTDi8404.
GeneCardsiSPARCL1.
H-InvDBHIX0004360.
HGNCiHGNC:11220. SPARCL1.
HPAiCAB026225.
MIMi606041. gene.
neXtProtiNX_Q14515.
PharmGKBiPA36056.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4004. Eukaryota.
ENOG41101WW. LUCA.
GeneTreeiENSGT00510000046787.
HOGENOMiHOG000063702.
HOVERGENiHBG079212.
InParanoidiQ14515.
OMAiHCVCQDP.
OrthoDBiEOG738059.
PhylomeDBiQ14515.
TreeFamiTF319356.

Miscellaneous databases

ChiTaRSiSPARCL1. human.
GeneWikiiSPARCL1.
GenomeRNAii8404.
PROiQ14515.
SOURCEiSearch...

Gene expression databases

BgeeiQ14515.
CleanExiHS_SPARCL1.
ExpressionAtlasiQ14515. baseline and differential.
GenevisibleiQ14515. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR001999. Osteonectin_CS.
IPR016359. SPARC-like_p1.
IPR019577. SPARC/Testican_Ca-bd-dom.
[Graphical view]
PfamiPF09289. FOLN. 1 hit.
PF00050. Kazal_1. 1 hit.
PF10591. SPARC_Ca_bdg. 1 hit.
[Graphical view]
PIRSFiPIRSF002574. SPARC-like_p1. 1 hit.
SMARTiSM00274. FOLN. 1 hit.
SM00280. KAZAL. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS51465. KAZAL_2. 1 hit.
PS00612. OSTEONECTIN_1. 1 hit.
PS00613. OSTEONECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning from purified high endothelial venule cells of hevin, a close relative of the antiadhesive extracellular matrix protein SPARC."
    Girard J.-P., Springer T.A.
    Immunity 2:113-123(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-49 AND ASP-106.
    Tissue: Tonsil.
  2. "An alternative PCR-based method for the direct isolation of cDNA ends (DICE)."
    Schraml P., Shipman R., Ludwig C.U.
    Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lung.
  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] (ISOFORM 2).
    Tissue: Uterus.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-412.
    Tissue: Plasma.
  6. "Enrichment of glycopeptides for glycan structure and attachment site identification."
    Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
    Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-398 AND THR-399, STRUCTURE OF CARBOHYDRATES.
    Tissue: Cerebrospinal fluid.
  7. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
    Halim A., Ruetschi U., Larson G., Nilsson J.
    J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-31; THR-40; SER-44; THR-116 AND THR-398, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSPRL1_HUMAN
AccessioniPrimary (citable) accession number: Q14515
Secondary accession number(s): B4E2Z0, E7ESU2, Q14800
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 22, 2009
Last modified: June 8, 2016
This is version 140 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.